{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T19:47:29Z","timestamp":1792093649391,"version":"4.4.0"},"reference-count":558,"publisher":"Elsevier BV","issue":"13","license":[{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Advanced Drug Delivery Reviews"],"published-print":{"date-parts":[[2011,10]]},"DOI":"10.1016\/j.addr.2011.07.006","type":"journal-article","created":{"date-parts":[[2011,8,2]],"date-time":"2011-08-02T23:48:18Z","timestamp":1312328898000},"page":"1118-1159","source":"Crossref","is-referenced-by-count":469,"title":["Protein\u2013excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development"],"prefix":"10.1016","volume":"63","author":[{"given":"Tim J.","family":"Kamerzell","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Reza","family":"Esfandiary","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sangeeta B.","family":"Joshi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C. Russell","family":"Middaugh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David B.","family":"Volkin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.addr.2011.07.006_bb0005","doi-asserted-by":"crossref","first-page":"2283","DOI":"10.1002\/jps.10154","article-title":"Excipient\u2013drug interactions in parenteral formulations","volume":"91","author":"Akers","year":"2002","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0010","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1007\/978-1-4615-0549-5_2","article-title":"Formulation development of protein dosage forms","volume":"14","author":"Akers","year":"2002","journal-title":"Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb0015","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S1461-5347(00)00248-0","article-title":"The formulation of biopharmaceutical products","volume":"3","author":"Parkins","year":"2000","journal-title":"Pharm. Sci. Technol. Today"},{"key":"10.1016\/j.addr.2011.07.006_bb0020","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0378-5173(99)00152-0","article-title":"Instability, stabilization, and formulation of liquid protein pharmaceuticals","volume":"185","author":"Wang","year":"1999","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb0025","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1517\/17425240903199143","article-title":"Recent trends in stabilising peptides and proteins in pharmaceutical formulation \u2014 considerations in the choice of excipients","volume":"6","author":"Jorgensen","year":"2009","journal-title":"Expert Opin. Drug Deliv."},{"key":"10.1016\/j.addr.2011.07.006_bb0030","first-page":"166","article-title":"Excipients and their use in injectable products","volume":"51","author":"Nema","year":"1997","journal-title":"PDA J. Pharm. Sci. Technol."},{"key":"10.1016\/j.addr.2011.07.006_bb0035","first-page":"238","article-title":"Compendium of excipients for parenteral formulations","volume":"52","author":"Powell","year":"1998","journal-title":"PDA J. Pharm. Sci. Technol."},{"key":"10.1016\/j.addr.2011.07.006_bb0040","series-title":"Excipient Development for Pharmaceutical, Biotechnology, and Drug Delivery Systems","author":"Katdare","year":"2006"},{"key":"10.1016\/j.addr.2011.07.006_bb0045","doi-asserted-by":"crossref","first-page":"4171","DOI":"10.1002\/jps.22618","article-title":"Multidimensional methods for the formulation of biopharmaceuticals and vaccines","volume":"100","author":"Maddux","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0050","series-title":"An Empirical Phase Diagram\u2014High-Throughput Screening Approach to the Characterization and Formulation of Biopharmaceuticals","author":"Joshi","year":"2010"},{"key":"10.1016\/j.addr.2011.07.006_bb0055","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1002\/jps.22350","article-title":"Application of a high-throughput screening procedure with PEG-induced precipitation to compare relative protein solubility during formulation development with IgG1 monoclonal antibodies","volume":"100","author":"Gibson","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0060","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1002\/jps.22371","article-title":"Formulation development of therapeutic monoclonal antibodies using high-throughput fluorescence and static light scattering techniques: role of conformational and colloidal stability","volume":"100","author":"Goldberg","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0065","doi-asserted-by":"crossref","first-page":"2598","DOI":"10.1002\/jps.22036","article-title":"Detection of IgG aggregation by a high throughput method based on extrinsic fluorescence","volume":"99","author":"He","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0070","doi-asserted-by":"crossref","first-page":"2120","DOI":"10.1002\/jps.22450","article-title":"High throughput formulation screening for global aggregation behaviors of three monoclonal antibodies","volume":"100","author":"Li","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0075","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1007\/s11095-011-0385-x","article-title":"The degradation of polysorbates 20 and 80 and its potential impact on the stability of biotherapeutics","volume":"28","author":"Kishore","year":"2011","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0080","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1002\/jps.22290","article-title":"Degradation of polysorbates 20 and 80: studies on thermal autoxidation and hydrolysis","volume":"100","author":"Kishore","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0085","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1007\/s11095-010-0080-3","article-title":"Metal impurities in food and drugs","volume":"27","author":"Abernethy","year":"2010","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0090","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1002\/jps.20726","article-title":"Evaluation of hydroperoxides in common pharmaceutical excipients","volume":"96","author":"Wasylaschuk","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0095","doi-asserted-by":"crossref","first-page":"2041","DOI":"10.1002\/jps.21152","article-title":"Endotoxin limits in formulations for preclinical research","volume":"97","author":"Malyala","year":"2008","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0100","first-page":"65","article-title":"Raw material considerations","volume":"91","author":"Lubiniecki","year":"1997","journal-title":"Dev. Biol. Stand."},{"key":"10.1016\/j.addr.2011.07.006_bb0105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0014-827X(98)00101-3","article-title":"Quality and functionality of excipients","volume":"54","author":"Pifferi","year":"1999","journal-title":"Farmaco"},{"key":"10.1016\/j.addr.2011.07.006_bb0110","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/S0378-5173(99)00110-6","article-title":"Regulatory issues with excipients","volume":"187","author":"Robertson","year":"1999","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb0115","series-title":"Guidance for Industry-Nonclinical Studies for the Safety Evaluation of Pharmaceutical Excipients, Food and Drug Administration (FDA)","year":"2005"},{"key":"10.1016\/j.addr.2011.07.006_bb0120","series-title":"Guideline on Excipients in the Dossier for Application for Marketing Authorisation of a Medicinal Product, European Medicines Agency (EMEA)","year":"2007"},{"key":"10.1016\/j.addr.2011.07.006_bb0125","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1002\/btpr.523","article-title":"Effect of protein and solution properties on the Donnan effect during the ultrafiltration of proteins","volume":"27","author":"Bolton","year":"2011","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.addr.2011.07.006_bb0130","doi-asserted-by":"crossref","first-page":"2332","DOI":"10.1002\/jps.20145","article-title":"Protein\u2013solute interactions affect the outcome of ultrafiltration\/diafiltration operations","volume":"93","author":"Stoner","year":"2004","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0135","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.1002\/bit.23067","article-title":"Predicting diafiltration solution compositions for final ultrafiltration\/diafiltration steps of monoclonal antibodies","volume":"108","author":"Teeters","year":"2011","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb0140","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.biologicals.2010.07.005","article-title":"Excipient exchange in the comparison of preparations of the same biologic made by different manufacturing processes: an exploratory study with recombinant human growth hormone (rhGH)","volume":"38","author":"Cauchy","year":"2010","journal-title":"Biologicals"},{"key":"10.1016\/j.addr.2011.07.006_bb0145","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1007\/BF03259937","article-title":"Pharmaceutical excipients. Adverse effects associated with inactive ingredients in drug products (Part I)","volume":"3","author":"Golightly","year":"1988","journal-title":"Med. Toxicol. Adverse Drug Exp."},{"key":"10.1016\/j.addr.2011.07.006_bb0150","series-title":"Excipient Toxicity and Safety Drugs and the Pharmaceutical Sciences v.103","first-page":"21","article-title":"Purity of excipients","author":"Jakel","year":"2000"},{"key":"10.1016\/j.addr.2011.07.006_bb0155","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1016\/j.addr.2007.09.010","article-title":"Lipid excipients and delivery systems for pharmaceutical development: a regulatory perspective","volume":"60","author":"Chen","year":"2008","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.addr.2011.07.006_bb0160","series-title":"FDA Science Forum","article-title":"FDA's approach to the GRAS provision: a history of processes","author":"Gaynor","year":"2006"},{"key":"10.1016\/j.addr.2011.07.006_bb0170","unstructured":"Inactive Ingredient Search for Approved Drug Products, http:\/\/www.accessdata.fda.gov\/scripts\/cder\/iig\/index.cfm."},{"key":"10.1016\/j.addr.2011.07.006_bb0175","series-title":"The Handbook of Pharmaceutical Excipients","author":"Rowe","year":"2005"},{"key":"10.1016\/j.addr.2011.07.006_bb0180","doi-asserted-by":"crossref","first-page":"2220","DOI":"10.1002\/jps.10219","article-title":"Stabilization of proteins by low molecular weight multi-ions","volume":"91","author":"Maclean","year":"2002","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0185","first-page":"46","article-title":"A review and classification of emerging excipients in parenteral medications","author":"Apte","year":"2003","journal-title":"Pharm. Technol."},{"key":"10.1016\/j.addr.2011.07.006_bb0190","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1007\/s00253-006-0553-9","article-title":"Extremolytes: natural compounds from extremophiles for versatile applications","volume":"72","author":"Lentzen","year":"2006","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb0195","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/0076-6879(90)82006-N","article-title":"Buffers: principles and practice","volume":"182","author":"Stoll","year":"1990","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.addr.2011.07.006_bb0200","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.ijpharm.2005.10.024","article-title":"Influence of pH, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298","volume":"308","author":"Zheng","year":"2006","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb0205","doi-asserted-by":"crossref","first-page":"1212","DOI":"10.1002\/jps.20471","article-title":"Effect of buffer species on the thermally induced aggregation of interferon-tau","volume":"95","author":"Katayama","year":"2006","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0210","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.addr.2007.04.017","article-title":"Formulation of Neulasta (pegfilgrastim)","volume":"60","author":"Piedmonte","year":"2008","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.addr.2011.07.006_bb0215","doi-asserted-by":"crossref","first-page":"2478","DOI":"10.1007\/s11095-009-9963-6","article-title":"Carboxylate-dependent gelation of a monoclonal antibody","volume":"26","author":"Esue","year":"2009","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0220","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1023\/A:1011082911917","article-title":"Effect of initial buffer composition on pH changes during far-from-equilibrium freezing of sodium phosphate buffer solutions","volume":"18","author":"Gomez","year":"2001","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0225","doi-asserted-by":"crossref","first-page":"1969","DOI":"10.1002\/jps.10184","article-title":"Effect of glycine on pH changes and protein stability during freeze\u2013thawing in phosphate buffer systems","volume":"91","author":"Pikal-Cleland","year":"2002","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0230","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1006\/abbi.2000.2088","article-title":"Protein denaturation during freezing and thawing in phosphate buffer systems: monomeric and tetrameric beta-galactosidase","volume":"384","author":"Pikal-Cleland","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.addr.2011.07.006_bb0235","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1002\/btpr.377","article-title":"Impact of freezing on pH of buffered solutions and consequences for monoclonal antibody aggregation","volume":"26","author":"Kolhe","year":"2010","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.addr.2011.07.006_bb0240","doi-asserted-by":"crossref","first-page":"1354","DOI":"10.1021\/js980383n","article-title":"Effects of buffer composition and processing conditions on aggregation of bovine IgG during freeze-drying","volume":"88","author":"Sarciaux","year":"1999","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0245","doi-asserted-by":"crossref","first-page":"7154","DOI":"10.1021\/jp202167p","article-title":"Thermophysical properties of carboxylic and amino acid buffers at subzero temperatures: relevance to frozen state stabilization","volume":"115","author":"Sundaramurthi","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb0250","doi-asserted-by":"crossref","first-page":"1288","DOI":"10.1002\/jps.22374","article-title":"Predicting the crystallization propensity of carboxylic acid buffers in frozen systems\u2014relevance to freeze-drying","volume":"100","author":"Sundaramurthi","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0255","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1007\/s11095-010-0282-8","article-title":"The effect of crystallizing and non-crystallizing cosolutes on succinate buffer crystallization and the consequent pH shift in frozen solutions","volume":"28","author":"Sundaramurthi","year":"2011","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0260","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1007\/s11095-006-9178-z","article-title":"Glycine crystallization in frozen and freeze-dried systems: effect of pH and buffer concentration","volume":"24","author":"Varshney","year":"2007","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0265","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1002\/jps.1073","article-title":"Formaldehyde production by Tris buffer in peptide formulations at elevated temperature","volume":"90","author":"Song","year":"2001","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0270","doi-asserted-by":"crossref","first-page":"2152","DOI":"10.1002\/pro.495","article-title":"Photochemical degradation of citrate buffers leads to covalent acetonation of recombinant protein therapeutics","volume":"19","author":"Valliere-Douglass","year":"2010","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0275","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bpc.2006.12.007","article-title":"Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects","volume":"127","author":"Arakawa","year":"2007","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb0280","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1007\/s00726-007-0506-3","article-title":"Biotechnology applications of amino acids in protein purification and formulations","volume":"33","author":"Arakawa","year":"2007","journal-title":"Amino Acids"},{"key":"10.1016\/j.addr.2011.07.006_bb0285","doi-asserted-by":"crossref","first-page":"1952","DOI":"10.1023\/B:PHAM.0000008042.15988.c0","article-title":"Influence of histidine on the stability and physical properties of a fully human antibody in aqueous and solid forms","volume":"20","author":"Chen","year":"2003","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0290","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.ijpharm.2006.10.037","article-title":"Spectroscopic evaluation of the stabilization of humanized monoclonal antibodies in amino acid formulations","volume":"335","author":"Tian","year":"2007","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb0295","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/S0955-2863(98)00022-9","article-title":"Antioxidant characteristics of l-histidine","volume":"9","author":"Wade","year":"1998","journal-title":"J. Nutr. Biochem."},{"key":"10.1016\/j.addr.2011.07.006_bb0300","doi-asserted-by":"crossref","first-page":"18662","DOI":"10.1074\/jbc.M110.108597","article-title":"Histidine residue mediates radical-induced hinge cleavage of human IgG1","volume":"285","author":"Yates","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb0305","doi-asserted-by":"crossref","first-page":"408","DOI":"10.2174\/138920109788488851","article-title":"Suppression of protein aggregation by l-arginine","volume":"10","author":"Lange","year":"2009","journal-title":"Curr. Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb0310","doi-asserted-by":"crossref","first-page":"415","DOI":"10.2174\/138920109788488824","article-title":"To be excluded or to bind, that is the question: arginine effects on proteins","volume":"10","author":"Nakakido","year":"2009","journal-title":"Curr. Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb0315","doi-asserted-by":"crossref","first-page":"13426","DOI":"10.1021\/jp108399g","article-title":"Interaction of arginine with proteins and the mechanism by which it inhibits aggregation","volume":"114","author":"Shukla","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb0320","doi-asserted-by":"crossref","first-page":"1448","DOI":"10.1023\/A:1012209007411","article-title":"Phase transitions of glycine in frozen aqueous solutions and during freeze-drying","volume":"18","author":"Pyne","year":"2001","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0325","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1021\/js970143s","article-title":"Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2","volume":"86","author":"Lam","year":"1997","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0330","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.biologicals.2010.11.004","article-title":"Local tolerance and stability up to 24months of a new 20% proline-stabilized polyclonal immunoglobulin for subcutaneous administration","volume":"39","author":"Maeder","year":"2011","journal-title":"Biologicals"},{"key":"10.1016\/j.addr.2011.07.006_bb0335","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.ijpharm.2010.01.027","article-title":"Freeze-drying of proteins with glass-forming oligosaccharide-derived sugar alcohols","volume":"389","author":"Kadoya","year":"2010","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb0340","doi-asserted-by":"crossref","first-page":"8933","DOI":"10.1021\/ja049297h","article-title":"A simple method for improving protein solubility and long-term stability","volume":"126","author":"Golovanov","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb0345","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.abb.2009.09.007","article-title":"Role of naturally occurring osmolytes in protein folding and stability","volume":"491","author":"Kumar","year":"2009","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.addr.2011.07.006_bb0350","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/S0006-3495(85)83932-1","article-title":"The stabilization of proteins by osmolytes","volume":"47","author":"Arakawa","year":"1985","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb0355","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1002\/prot.22103","article-title":"Structural thermodynamics of protein preferential solvation: osmolyte solvation of proteins, aminoacids, and peptides","volume":"73","author":"Auton","year":"2008","journal-title":"Proteins"},{"key":"10.1016\/j.addr.2011.07.006_bb0360","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.ymeth.2004.03.022","article-title":"Effects of naturally occurring osmolytes on protein stability and solubility: issues important in protein crystallization","volume":"34","author":"Bolen","year":"2004","journal-title":"Methods"},{"key":"10.1016\/j.addr.2011.07.006_bb0365","doi-asserted-by":"crossref","first-page":"13473","DOI":"10.1021\/bi020316e","article-title":"Protein hydration, thermodynamic binding, and preferential hydration","volume":"41","author":"Timasheff","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb0370","doi-asserted-by":"crossref","first-page":"41","DOI":"10.3410\/B1-41","article-title":"Osmolyte solutions and protein folding","volume":"1","author":"Hu","year":"2009","journal-title":"F1000 Biol. Rep."},{"key":"10.1016\/j.addr.2011.07.006_bb0375","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1007\/s12038-009-0036-0","article-title":"Living with urea stress","volume":"34","author":"Singh","year":"2009","journal-title":"J. Biosci."},{"key":"10.1016\/j.addr.2011.07.006_bb0380","doi-asserted-by":"crossref","first-page":"11084","DOI":"10.1021\/bi900649t","article-title":"Mechanisms of protein stabilization and prevention of protein aggregation by glycerol","volume":"48","author":"Vagenende","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb0385","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.lfs.2010.10.020","article-title":"Protein and DNA destabilization by osmolytes: the other side of the coin","volume":"88","author":"Singh","year":"2011","journal-title":"Life Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0390","doi-asserted-by":"crossref","first-page":"26458","DOI":"10.1074\/jbc.M300815200","article-title":"Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose","volume":"278","author":"Kaushik","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb0395","doi-asserted-by":"crossref","first-page":"11917","DOI":"10.1073\/pnas.94.22.11917","article-title":"Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: role in restricted conformational mobility and compaction of native state","volume":"94","author":"Kendrick","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb0400","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.1110\/ps.0242603","article-title":"Effects of sucrose on conformational equilibria and fluctuations within the native-state ensemble of proteins","volume":"12","author":"Kim","year":"2003","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0405","doi-asserted-by":"crossref","first-page":"2020","DOI":"10.1002\/jps.22458","article-title":"Trehalose: current use and future applications","volume":"100","author":"Ohtake","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0410","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1080\/10837450701481157","article-title":"Protein stability during freezing: separation of stresses and mechanisms of protein stabilization","volume":"12","author":"Bhatnagar","year":"2007","journal-title":"Pharm. Dev. Technol."},{"key":"10.1016\/j.addr.2011.07.006_bb0415","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1002\/jps.21825","article-title":"Mechanisms of protein stabilization in the solid state","volume":"98","author":"Chang","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0420","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1002\/jps.20364","article-title":"Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specific interaction, and\/or immobilization in a glassy matrix?","volume":"94","author":"Chang","year":"2005","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0425","doi-asserted-by":"crossref","first-page":"1445","DOI":"10.1002\/jps.20363","article-title":"Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: implications for the mechanism of protein stabilization in the solid state","volume":"94","author":"Chang","year":"2005","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0430","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1002\/1520-6017(200103)90:3<310::AID-JPS6>3.0.CO;2-R","article-title":"A specific molar ratio of stabilizer to protein is required for storage stability of a lyophilized monoclonal antibody","volume":"90","author":"Cleland","year":"2001","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0435","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1007\/s11095-011-0388-7","article-title":"Effect of sugar molecules on the viscosity of high concentration monoclonal antibody solutions","volume":"28","author":"He","year":"2011","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0440","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1007\/s11095-006-9131-1","article-title":"Sorbitol crystallization can lead to protein aggregation in frozen protein formulations","volume":"24","author":"Piedmonte","year":"2007","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0445","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.ejps.2009.05.008","article-title":"Impact of bulking agents on the stability of a lyophilized monoclonal antibody","volume":"38","author":"Meyer","year":"2009","journal-title":"Eur. J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0450","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1002\/jps.10094","article-title":"Mannitol\u2013sucrose mixtures\u2014versatile formulations for protein lyophilization","volume":"91","author":"Johnson","year":"2002","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0455","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.ijpharm.2009.10.029","article-title":"Development of inhalable dry powder formulation of basic fibroblast growth factor","volume":"385","author":"Ibrahim","year":"2010","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb0460","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0168-3659(00)00362-X","article-title":"Influence of formulation excipients and physical characteristics of inhalation dry powders on their aerosolization performance","volume":"70","author":"Bosquillon","year":"2001","journal-title":"J. Control. Release"},{"key":"10.1016\/j.addr.2011.07.006_bb0465","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1038\/nrd2153","article-title":"Inhaling medicines: delivering drugs to the body through the lungs","volume":"6","author":"Patton","year":"2007","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.addr.2011.07.006_bb0470","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.1002\/jps.21931","article-title":"Inhibition of agitation-induced aggregation of an IgG-antibody by hydroxypropyl-beta-cyclodextrin","volume":"99","author":"Serno","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0475","doi-asserted-by":"crossref","first-page":"2800","DOI":"10.1002\/jps.22053","article-title":"The effects of substituted cyclodextrins on the colloidal and conformational stability of selected proteins","volume":"99","author":"Samra","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0480","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1023\/A:1015870521744","article-title":"Use of 2-hydroxypropyl-beta-cyclodextrin as a solubilizing and stabilizing excipient for protein drugs","volume":"8","author":"Brewster","year":"1991","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0485","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1016\/S0731-7085(03)00163-8","article-title":"Quantification of 5-HMF and dextrose in commercial aqueous dextrose solutions","volume":"32","author":"Xu","year":"2003","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.addr.2011.07.006_bb0490","doi-asserted-by":"crossref","first-page":"4501","DOI":"10.1002\/jps.21749","article-title":"The effect of sucrose hydrolysis on the stability of protein therapeutics during accelerated formulation studies","volume":"98","author":"Banks","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0495","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1002\/bit.10161","article-title":"Protein modification during anti-viral heat-treatment bioprocessing of factor VIII concentrates, factor IX concentrates, and model proteins in the presence of sucrose","volume":"77","author":"Smales","year":"2002","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb0500","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1021\/js950456s","article-title":"Effects of reducing sugars on the chemical stability of human relaxin in the lyophilized state","volume":"85","author":"Li","year":"1996","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0505","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1023\/A:1015396825274","article-title":"Pharmaceutical strategies utilizing recombinant human serum albumin","volume":"19","author":"Chuang","year":"2002","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0510","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/nbt0595-493","article-title":"Aggregation of a lyophilized pharmaceutical protein, recombinant human albumin: effect of moisture and stabilization by excipients","volume":"13","author":"Costantino","year":"1995","journal-title":"Biotechnology (N Y)"},{"key":"10.1016\/j.addr.2011.07.006_bb0515","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1080\/10837450701247350","article-title":"Formulation development for hydrophobic therapeutic proteins","volume":"12","author":"Hawe","year":"2007","journal-title":"Pharm. Dev. Technol."},{"key":"10.1016\/j.addr.2011.07.006_bb0520","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1211\/0022357991772574","article-title":"Stability study of human serum albumin pharmaceutical preparations","volume":"51","author":"Oliva","year":"1999","journal-title":"J. Pharm. Pharmacol."},{"key":"10.1016\/j.addr.2011.07.006_bb0525","doi-asserted-by":"crossref","first-page":"3363","DOI":"10.1002\/jps.21022","article-title":"The structure, stability, and complex behavior of recombinant human gelatins","volume":"96","author":"Thyagarajapuram","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0530","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1023\/A:1012194220970","article-title":"Dependence of the molecular mobility and protein stability of freeze-dried gamma-globulin formulations on the molecular weight of dextran","volume":"14","author":"Yoshioka","year":"1997","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0535","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1002\/jps.10587","article-title":"Optimizing storage stability of lyophilized recombinant human interleukin-11 with disaccharide\/hydroxyethyl starch mixtures","volume":"93","author":"Garzon-Rodriguez","year":"2004","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0540","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1021\/js9703378","article-title":"Effect of high molecular mobility of poly(vinyl alcohol) on protein stability of lyophilized gamma-globulin formulations","volume":"87","author":"Yoshioka","year":"1998","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0545","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1023\/A:1018903624373","article-title":"The stabilization of a human IgM monoclonal antibody with poly(vinylpyrrolidone)","volume":"11","author":"Gombotz","year":"1994","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0550","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.1023\/A:1026412107574","article-title":"Freeze-concentration separates proteins and polymer excipients into different amorphous phases","volume":"17","author":"Izutsu","year":"2000","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0555","doi-asserted-by":"crossref","first-page":"2557","DOI":"10.1002\/jps.22054","article-title":"Delivery of therapeutic proteins","volume":"99","author":"Pisal","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0560","doi-asserted-by":"crossref","first-page":"605","DOI":"10.3109\/10717544.2010.509359","article-title":"Carrier mediated protein and peptide stabilization","volume":"17","author":"Tiwari","year":"2010","journal-title":"Drug Deliv."},{"key":"10.1016\/j.addr.2011.07.006_bb0565","doi-asserted-by":"crossref","DOI":"10.1016\/S1461-5347(98)00072-8","article-title":"Pharmaceutical applications of naturally-occurring water-soluble polymers","volume":"1","author":"Guo","year":"1998","journal-title":"Pharm. Sci. Technol. Today"},{"key":"10.1016\/j.addr.2011.07.006_bb0570","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1023\/A:1018939228201","article-title":"Formulation design of acidic fibroblast growth factor","volume":"10","author":"Tsai","year":"1993","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0575","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1007\/0-306-47452-2_3","article-title":"The characterization, stabilization, and formulation of acidic fibroblast growth factor","volume":"9","author":"Volkin","year":"1996","journal-title":"Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb0580","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1146\/annurev.physchem.59.032607.093635","article-title":"Chemistry of Hofmeister anions and osmolytes","volume":"61","author":"Zhang","year":"2010","journal-title":"Annu. Rev. Phys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb0585","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1016\/j.cbpa.2006.09.020","article-title":"Interactions between macromolecules and ions: the Hofmeister series","volume":"10","author":"Zhang","year":"2006","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb0590","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1002\/pro.591","article-title":"Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions","volume":"20","author":"Gokarn","year":"2011","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0595","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1007\/s11095-008-9792-z","article-title":"Effect of ions on agitation- and temperature-induced aggregation reactions of antibodies","volume":"26","author":"Fesinmeyer","year":"2009","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0600","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1007\/s11095-008-9722-0","article-title":"Anion binding mediated precipitation of a peptibody","volume":"26","author":"Saluja","year":"2009","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0605","doi-asserted-by":"crossref","first-page":"1928","DOI":"10.1002\/jps.20347","article-title":"Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution","volume":"94","author":"Liu","year":"2005","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0610","doi-asserted-by":"crossref","first-page":"6109","DOI":"10.1021\/jp9001548","article-title":"Increasing IgG concentration modulates the conformational heterogeneity and bonding network that influence solution properties","volume":"113","author":"Kamerzell","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb0615","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1080\/10837450701212826","article-title":"Effect of cations and anions on glass transition temperatures in excipient solutions","volume":"12","author":"Nesarikar","year":"2007","journal-title":"Pharm. Dev. Technol."},{"key":"10.1016\/j.addr.2011.07.006_bb0620","doi-asserted-by":"crossref","first-page":"1931","DOI":"10.1007\/s11095-005-7249-1","article-title":"Displacement of adsorbed insulin by Tween 80 monitored using total internal reflection fluorescence and ellipsometry","volume":"22","author":"Mollmann","year":"2005","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0625","doi-asserted-by":"crossref","first-page":"3200","DOI":"10.1002\/jps.21740","article-title":"Physical and biophysical effects of polysorbate 20 and 80 on darbepoetin alfa","volume":"98","author":"Deechongkit","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0630","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1007\/978-1-4615-0557-0_7","article-title":"Surfactant\u2013protein interactions","volume":"13","author":"Randolph","year":"2002","journal-title":"Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb0635","doi-asserted-by":"crossref","first-page":"4525","DOI":"10.1002\/jps.21776","article-title":"Surface activity of a monoclonal antibody","volume":"98","author":"Mahler","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0640","doi-asserted-by":"crossref","first-page":"2924","DOI":"10.1002\/jps.21190","article-title":"Polysorbates 20 and 80 used in the formulation of protein biotherapeutics: structure and degradation pathways","volume":"97","author":"Kerwin","year":"2008","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0645","doi-asserted-by":"crossref","first-page":"1554","DOI":"10.1021\/js980175v","article-title":"Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions","volume":"87","author":"Bam","year":"1998","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0650","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1021\/js980126i","article-title":"Effect of Tween 20 on freeze\u2013thawing- and agitation-induced aggregation of recombinant human factor XIII","volume":"87","author":"Kreilgaard","year":"1998","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0655","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.ijpharm.2007.06.042","article-title":"Dual effects of Tween 80 on protein stability","volume":"347","author":"Wang","year":"2008","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb0660","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1021\/js960080y","article-title":"Surface-induced denaturation of proteins during freezing and its inhibition by surfactants","volume":"85","author":"Chang","year":"1996","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0665","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1002\/jps.10033","article-title":"A new mechanism for decreasing aggregation of recombinant human interferon-gamma by a surfactant: slowed dissolution of lyophilized formulations in a solution containing 0.03% polysorbate 20","volume":"91","author":"Webb","year":"2002","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0670","doi-asserted-by":"crossref","first-page":"2252","DOI":"10.1002\/jps.10216","article-title":"Peroxide formation in polysorbate 80 and protein stability","volume":"91","author":"Ha","year":"2002","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0675","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1002\/jps.21029","article-title":"Behaviour of polysorbate 20 during dialysis, concentration and filtration using membrane separation techniques","volume":"97","author":"Mahler","year":"2008","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0680","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1002\/1520-6017(200103)90:3<253::AID-JPS1>3.0.CO;2-W","article-title":"Oxidative degradation of pharmaceuticals: theory, mechanisms and inhibition","volume":"90","author":"Hovorka","year":"2001","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0685","doi-asserted-by":"crossref","first-page":"3987","DOI":"10.1002\/jps.21696","article-title":"Measurement and decomposition kinetics of residual hydrogen peroxide in the presence of commonly used excipients and preservatives","volume":"98","author":"Towne","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0690","doi-asserted-by":"crossref","first-page":"532","DOI":"10.2307\/3579271","article-title":"Catalytic metals, ascorbate and free radicals: combinations to avoid","volume":"145","author":"Buettner","year":"1996","journal-title":"Radiat. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0695","doi-asserted-by":"crossref","first-page":"4239","DOI":"10.1002\/jps.22141","article-title":"Comparative evaluation of disodium edetate and diethylenetriaminepentaacetic acid as iron chelators to prevent metal-catalyzed destabilization of a therapeutic monoclonal antibody","volume":"99","author":"Zhou","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0700","doi-asserted-by":"crossref","first-page":"2458","DOI":"10.1002\/jps.20157","article-title":"Development of stable liquid formulations for adenovirus-based vaccines","volume":"93","author":"Evans","year":"2004","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0705","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1002\/(SICI)1520-6017(200001)89:1<76::AID-JPS8>3.0.CO;2-U","article-title":"Evaluation of degradation pathways for plasmid DNA in pharmaceutical formulations via accelerated stability studies","volume":"89","author":"Evans","year":"2000","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0710","doi-asserted-by":"crossref","first-page":"1924","DOI":"10.1002\/jps.20112","article-title":"Characterization and biological evaluation of a microparticle adjuvant formulation for plasmid DNA vaccines","volume":"93","author":"Evans","year":"2004","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0715","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1002\/jps.22330","article-title":"Identifying stabilizers of plasmid DNA for pharmaceutical use","volume":"100","author":"Zeng","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0720","doi-asserted-by":"crossref","first-page":"3117","DOI":"10.1002\/jps.21617","article-title":"Characterization of the photodegradation of a human IgG1 monoclonal antibody formulated as a high-concentration liquid dosage form","volume":"98","author":"Qi","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0725","doi-asserted-by":"crossref","first-page":"2549","DOI":"10.1002\/jps.20167","article-title":"Effect of metal cations on the conformation and inactivation of recombinant human factor VIII","volume":"93","author":"Derrick","year":"2004","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0730","first-page":"11","article-title":"Root cause analysis of tungsten-induced protein aggregation in pre-filled syringes","volume":"64","author":"Liu","year":"2010","journal-title":"PDA J. Pharm. Sci. Technol."},{"key":"10.1016\/j.addr.2011.07.006_bb0735","doi-asserted-by":"crossref","first-page":"4695","DOI":"10.1002\/jps.21778","article-title":"Tungsten-induced protein aggregation: solution behavior","volume":"98","author":"Jiang","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0740","doi-asserted-by":"crossref","first-page":"3155","DOI":"10.1002\/jps.20976","article-title":"Antimicrobial preservative use in parenteral products: past and present","volume":"96","author":"Meyer","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0745","doi-asserted-by":"crossref","first-page":"E8","DOI":"10.1208\/ps050208","article-title":"Development of a multidose formulation for a humanized monoclonal antibody using experimental design techniques","volume":"5","author":"Gupta","year":"2003","journal-title":"AAPS PharmSci"},{"key":"10.1016\/j.addr.2011.07.006_bb0750","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/0378-5173(96)04577-2","article-title":"Aggregation of recombinant human growth hormone induced by phenolic compounds","volume":"140","author":"Maa","year":"1996","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb0755","doi-asserted-by":"crossref","first-page":"3076","DOI":"10.1002\/jps.20219","article-title":"Mechanism for benzyl alcohol-induced aggregation of recombinant human interleukin-1 receptor antagonist in aqueous solution","volume":"93","author":"Zhang","year":"2004","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0760","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jps.10589","article-title":"Benzyl alcohol-induced destabilization of interferon-gamma: a study by hydrogen\u2013deuterium isotope exchange","volume":"93","author":"Tobler","year":"2004","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0765","doi-asserted-by":"crossref","first-page":"1480","DOI":"10.1002\/jps.20619","article-title":"Effects of pH, temperature, and sucrose on benzyl alcohol-induced aggregation of recombinant human granulocyte colony stimulating factor","volume":"95","author":"Thirumangalathu","year":"2006","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0770","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1023\/A:1012190120061","article-title":"The effect of benzyl alcohol on recombinant human interferon-gamma","volume":"14","author":"Lam","year":"1997","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0775","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1023\/A:1012101027814","article-title":"Solvent effects on the solubility and physical stability of human insulin-like growth factor I","volume":"14","author":"Fransson","year":"1997","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0780","doi-asserted-by":"crossref","first-page":"3898","DOI":"10.1021\/bi052132g","article-title":"Temperature dependence of benzyl alcohol- and 8-anilinonaphthalene-1-sulfonate-induced aggregation of recombinant human interleukin-1 receptor antagonist","volume":"45","author":"Roy","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb0785","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1021\/js980273g","article-title":"Influence of calcium ions on the structure and stability of recombinant human deoxyribonuclease I in the aqueous and lyophilized states","volume":"88","author":"Chen","year":"1999","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0790","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1007\/0-306-47452-2_11","article-title":"Stability characterization and formulation development of recombinant human deoxyribonuclease I [Pulmozyme, (dornase alpha)]","volume":"9","author":"Shire","year":"1996","journal-title":"Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb0795","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1021\/js960475h","article-title":"Size and conformational stability of the hepatitis A virus used to prepare VAQTA, a highly purified inactivated vaccine","volume":"86","author":"Volkin","year":"1997","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0800","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1002\/bit.260351013","article-title":"Lysine and other diamines dramatically stabilize poliovirus against thermoinactivation","volume":"35","author":"Dorval","year":"1990","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb0805","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1007\/978-1-4899-1236-7_11","article-title":"Insulin structure and stability","volume":"5","author":"Brange","year":"1993","journal-title":"Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb0810","doi-asserted-by":"crossref","first-page":"2611","DOI":"10.1007\/s11095-006-9098-y","article-title":"Chemical and thermal stability of insulin: effects of zinc and ligand binding to the insulin zinc-hexamer","volume":"23","author":"Huus","year":"2006","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb0815","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1208\/s12248-011-9268-7","article-title":"A new strategy to stabilize oxytocin in aqueous solutions: I. The effects of divalent metal ions and citrate buffer","volume":"13","author":"Avanti","year":"2011","journal-title":"AAPS J."},{"key":"10.1016\/j.addr.2011.07.006_bb0820","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1006\/abbi.1993.1005","article-title":"Physical stabilization of acidic fibroblast growth factor by polyanions","volume":"300","author":"Volkin","year":"1993","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.addr.2011.07.006_bb0825","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1007\/978-1-4899-1236-7_3","article-title":"Stability characterization and formulation development of alteplase, a recombinant tissue plasminogen activator","volume":"5","author":"Nguyen","year":"1993","journal-title":"Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb0830","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1177\/1087057106292473","article-title":"High-throughput screening: update on practices and success","volume":"11","author":"Fox","year":"2006","journal-title":"J. Biomol. Screen."},{"key":"10.1016\/j.addr.2011.07.006_bb0835","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1038\/nrd3368","article-title":"Impact of high-throughput screening in biomedical research","volume":"10","author":"Macarron","year":"2011","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.addr.2011.07.006_bb0840","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1007\/s12033-010-9335-9","article-title":"Design and implementation of high throughput screening assays","volume":"47","author":"Macarron","year":"2011","journal-title":"Mol. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb0845","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1016\/j.coph.2009.08.004","article-title":"Novel trends in high-throughput screening","volume":"9","author":"Mayr","year":"2009","journal-title":"Curr. Opin. Pharmacol."},{"key":"10.1016\/j.addr.2011.07.006_bb0850","doi-asserted-by":"crossref","first-page":"14625","DOI":"10.1021\/ja803960x","article-title":"Carbohydrate\u2013pi interactions: what are they worth?","volume":"130","author":"Laughrey","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb0855","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1002\/bit.21906","article-title":"High-throughput screening of chromatographic separations: III. Monoclonal antibodies on ceramic hydroxyapatite","volume":"100","author":"Wensel","year":"2008","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb0860","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1002\/bit.21907","article-title":"High-throughput screening of chromatographic separations: II. Hydrophobic interaction","volume":"100","author":"Kramarczyk","year":"2008","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb0865","doi-asserted-by":"crossref","first-page":"950","DOI":"10.1002\/bit.21905","article-title":"High-throughput screening of chromatographic separations: IV. Ion-exchange","volume":"100","author":"Kelley","year":"2008","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb0870","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1002\/bit.21904","article-title":"High-throughput screening of chromatographic separations: I. Method development and column modeling","volume":"100","author":"Coffman","year":"2008","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb0875","doi-asserted-by":"crossref","first-page":"1330","DOI":"10.1002\/jps.22384","article-title":"Screening of monoclonal antibody formulations based on high-throughput thermostability and viscosity measurements: design of experiment and statistical analysis","volume":"100","author":"He","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0880","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1002\/jps.21955","article-title":"High throughput thermostability screening of monoclonal antibody formulations","volume":"99","author":"He","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0885","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.ab.2009.12.003","article-title":"High-throughput dynamic light scattering method for measuring viscosity of concentrated protein solutions","volume":"399","author":"He","year":"2010","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.addr.2011.07.006_bb0890","doi-asserted-by":"crossref","first-page":"390","DOI":"10.4161\/hv.6.5.10963","article-title":"Biophysical characterization of rotavirus serotypes G1, G3 and G4","volume":"6","author":"Esfandiary","year":"2010","journal-title":"Hum. Vaccin."},{"key":"10.1016\/j.addr.2011.07.006_bb0895","doi-asserted-by":"crossref","first-page":"5839","DOI":"10.1016\/j.vaccine.2006.04.067","article-title":"A systematic approach to stabilizing EBA-175 RII-NG for use as a malaria vaccine","volume":"24","author":"Peek","year":"2006","journal-title":"Vaccine"},{"key":"10.1016\/j.addr.2011.07.006_bb0900","doi-asserted-by":"crossref","first-page":"322","DOI":"10.4161\/hv.5.5.7559","article-title":"Towards development of stable formulations of a live attenuated bacterial vaccine: a preformulation study facilitated by a biophysical approach","volume":"5","author":"Zeng","year":"2009","journal-title":"Hum. Vaccin."},{"key":"10.1016\/j.addr.2011.07.006_bb0905","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1002\/jps.21418","article-title":"Evaluation of the physical stability of the EC5 domain of E-cadherin: effects of pH, temperature, ionic strength, and disulfide bonds","volume":"98","author":"Zheng","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0910","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1111\/j.1747-0285.2009.00818.x","article-title":"Characterization of multiple stable conformers of the EC5 domain of E-cadherin and the interaction of EC5 with E-cadherin peptides","volume":"73","author":"Zheng","year":"2009","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.addr.2011.07.006_bb0915","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.ijpharm.2008.02.022","article-title":"Stability of lyophilized human growth hormone","volume":"358","author":"Salnikova","year":"2008","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb0920","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1002\/jps.21197","article-title":"A biophysical characterization of the peptide drug pramlintide (AC137) using empirical phase diagrams","volume":"97","author":"Nonoyama","year":"2008","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0925","doi-asserted-by":"crossref","first-page":"1830","DOI":"10.1002\/prot.21864","article-title":"pH sensitivity of type III secretion system tip proteins","volume":"71","author":"Markham","year":"2008","journal-title":"Proteins"},{"key":"10.1016\/j.addr.2011.07.006_bb0930","doi-asserted-by":"crossref","first-page":"3304","DOI":"10.1002\/jps.20980","article-title":"Stabilization of proteins by recombinant human gelatins","volume":"96","author":"Thyagarajapuram","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0935","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1021\/mp060097h","article-title":"Effects of pH and polyanions on the thermal stability of fibroblast growth factor 20","volume":"4","author":"Fan","year":"2007","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb0940","doi-asserted-by":"crossref","first-page":"1490","DOI":"10.1002\/jps.20796","article-title":"Effects of solutes on empirical phase diagrams of human fibroblast growth factor 1","volume":"96","author":"Fan","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0945","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1002\/jps.20797","article-title":"Effect of polyanions on the structure and stability of repifermin (keratinocyte growth factor-2)","volume":"96","author":"Derrick","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0950","doi-asserted-by":"crossref","first-page":"2432","DOI":"10.1002\/jps.21619","article-title":"Using empirical phase diagrams to understand the role of intramolecular dynamics in immunoglobulin G stability","volume":"98","author":"Ramsey","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0955","doi-asserted-by":"crossref","first-page":"3343","DOI":"10.1002\/jps.22123","article-title":"Development of a microflow digital imaging assay to characterize protein particulates during storage of a high concentration IgG1 monoclonal antibody formulation","volume":"99","author":"Wuchner","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0960","doi-asserted-by":"crossref","first-page":"2120","DOI":"10.1002\/jps.22450","article-title":"High throughput formulation screening for global aggregation behaviors of three monoclonal antibodies","volume":"100","author":"Li","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0965","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1002\/jps.22304","article-title":"H1N1 influenza virus-like particles: physical degradation pathways and identification of stabilizers","volume":"100","author":"Kissmann","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0970","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1586\/erv.10.73","article-title":"Vaccines as physically and chemically well-defined pharmaceutical dosage forms","volume":"9","author":"Volkin","year":"2010","journal-title":"Expert Rev. Vaccines"},{"key":"10.1016\/j.addr.2011.07.006_bb0975","doi-asserted-by":"crossref","DOI":"10.4161\/hv.6.2.10254","article-title":"Using spectroscopic and microscopic methods to probe the structural stability of human adenovirus type 4","volume":"6","author":"He","year":"2010","journal-title":"Hum. Vaccin."},{"key":"10.1016\/j.addr.2011.07.006_bb0980","doi-asserted-by":"crossref","first-page":"3340","DOI":"10.1002\/jps.21657","article-title":"Structural stability of hepatitis C virus envelope glycoprotein E1: effect of pH and dissociative detergents","volume":"98","author":"He","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0985","doi-asserted-by":"crossref","first-page":"1376","DOI":"10.1002\/jps.21508","article-title":"Structural stability of vault particles","volume":"98","author":"Esfandiary","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb0990","doi-asserted-by":"crossref","first-page":"350","DOI":"10.4161\/hv.4.5.5863","article-title":"Stabilization of measles virus for vaccine formulation","volume":"4","author":"Kissmann","year":"2008","journal-title":"Hum. Vaccin."},{"key":"10.1016\/j.addr.2011.07.006_bb0995","doi-asserted-by":"crossref","first-page":"4208","DOI":"10.1002\/jps.21315","article-title":"Physical stabilization of Norwalk virus-like particles","volume":"97","author":"Kissmann","year":"2008","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1000","doi-asserted-by":"crossref","first-page":"94","DOI":"10.4161\/hv.3.3.4149","article-title":"High-throughput screening of stabilizers for respiratory syncytial virus: identification of stabilizers and their effects on the conformational thermostability of viral particles","volume":"3","author":"Ausar","year":"2007","journal-title":"Hum. Vaccin."},{"key":"10.1016\/j.addr.2011.07.006_bb1005","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1002\/jps.20617","article-title":"Thermal stability of adenovirus type 2 as a function of pH","volume":"95","author":"Rexroad","year":"2006","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1010","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1002\/jps.20496","article-title":"Effect of pH and ionic strength on the physical stability of adenovirus type 5","volume":"95","author":"Rexroad","year":"2006","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1015","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1017\/S0033583502003815","article-title":"What vibrations tell us about proteins","volume":"35","author":"Barth","year":"2002","journal-title":"Q. Rev. Biophys."},{"key":"10.1016\/j.addr.2011.07.006_bb1020","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/j.jpba.2008.08.014","article-title":"Pharmaceutical applications of vibrational chemical imaging and chemometrics: a review","volume":"48","author":"Gendrin","year":"2008","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.addr.2011.07.006_bb1025","first-page":"137","article-title":"Infrared spectroscopy","volume":"40","author":"Middaugh","year":"1995","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb1030","doi-asserted-by":"crossref","first-page":"1841","DOI":"10.1002\/bip.1972.360110906","article-title":"Normal vibrations of polyglycine II","volume":"11","author":"Abe","year":"1972","journal-title":"Biopolymers"},{"key":"10.1016\/j.addr.2011.07.006_bb1035","doi-asserted-by":"crossref","first-page":"2036","DOI":"10.1073\/pnas.96.5.2036","article-title":"The two-dimensional IR nonlinear spectroscopy of a cyclic penta-peptide in relation to its three-dimensional structure","volume":"96","author":"Hamm","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1040","doi-asserted-by":"crossref","first-page":"2788","DOI":"10.1073\/pnas.69.10.2788","article-title":"Intermolecular interaction effects in the amide I vibrations of polypeptides","volume":"69","author":"Krimm","year":"1972","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1045","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0065-3233(08)60528-8","article-title":"Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins","volume":"38","author":"Krimm","year":"1986","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1050","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1021\/jp972879j","article-title":"Effects of intermolecular hydrogen\u2013bonding interactions on the amide I mode of N-methylacetamide: matrix-isolation infrared studies and ab initio molecular orbital calculations","volume":"102","author":"Torii","year":"1998","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1055","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1002\/(SICI)1097-4555(199806)29:6<537::AID-JRS272>3.0.CO;2-X","article-title":"Effects of hydration on the structure, vibration wavenumbers, vibrational force field and resonance Raman intensities of N-methylacetamide","volume":"29","author":"Torii","year":"1998","journal-title":"J. Raman Spectrosc."},{"key":"10.1016\/j.addr.2011.07.006_bb1060","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.1139\/v91-240","article-title":"Protein secondary structure from FT-IR spectroscopy: correlation with dihedral angles from three dimensional Ramachandran plots","volume":"69","author":"Jackson","year":"1991","journal-title":"Can. J. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1065","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1002\/bip.1976.360150403","article-title":"Infrared spectra and resonance interaction of amide-I vibration of the parallel-chain pleated sheets","volume":"15","author":"Chirgadze","year":"1976","journal-title":"Biopolymers"},{"key":"10.1016\/j.addr.2011.07.006_bb1070","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1002\/bip.1976.360150402","article-title":"Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain pleated sheet","volume":"15","author":"Chirgadze","year":"1976","journal-title":"Biopolymers"},{"key":"10.1016\/j.addr.2011.07.006_bb1075","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1002\/bip.1976.360150404","article-title":"Infrared spectra and resonance interactions of amide-I and II vibration of alpha-helix","volume":"15","author":"Nevskaya","year":"1976","journal-title":"Biopolymers"},{"key":"10.1016\/j.addr.2011.07.006_bb1080","doi-asserted-by":"crossref","first-page":"2946","DOI":"10.1529\/biophysj.105.072017","article-title":"Evaluation of the information content in infrared spectra for protein secondary structure determination","volume":"90","author":"Goormaghtigh","year":"2006","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1085","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.biophys.28.1.1","article-title":"Raman spectroscopy of protein and nucleic acid assemblies","volume":"28","author":"Thomas","year":"1999","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1016\/j.addr.2011.07.006_bb1090","doi-asserted-by":"crossref","first-page":"2861","DOI":"10.1002\/jps.20895","article-title":"Raman spectroscopy of protein pharmaceuticals","volume":"96","author":"Wen","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1095","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1006\/abio.1999.4034","article-title":"A holistic approach to protein secondary structure characterization using amide I band Raman spectroscopy","volume":"269","author":"Sane","year":"1999","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.addr.2011.07.006_bb1100","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1146\/annurev.anchem.1.031207.112814","article-title":"Surface-enhanced Raman spectroscopy","volume":"1","author":"Stiles","year":"2008","journal-title":"Annu. Rev. Anal. Chem. (Palo Alto Calif.)"},{"key":"10.1016\/j.addr.2011.07.006_bb1105","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1126\/science.1159499","article-title":"Measurement of the distribution of site enhancements in surface-enhanced Raman scattering","volume":"321","author":"Fang","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb1110","doi-asserted-by":"crossref","first-page":"8446","DOI":"10.1021\/ja0353311","article-title":"Single-molecule surface enhanced resonance Raman spectroscopy of the enhanced green fluorescent protein","volume":"125","author":"Habuchi","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb1115","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1039\/b708839f","article-title":"Single-molecule and single-nanoparticle SERS: from fundamental mechanisms to biomedical applications","volume":"37","author":"Qian","year":"2008","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.addr.2011.07.006_bb1120","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1021\/ar800249y","article-title":"A unified view of surface-enhanced Raman scattering","volume":"42","author":"Lombardi","year":"2009","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb1125","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1016\/S1367-5931(02)00369-1","article-title":"Protein and peptide secondary structure and conformational determination with vibrational circular dichroism","volume":"6","author":"Keiderling","year":"2002","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb1130","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1146\/annurev.pc.36.100185.001241","article-title":"Vibrational circular dichroism","volume":"36","author":"Stephens","year":"1985","journal-title":"Annu. Rev. Phys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1135","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.cplett.2010.03.090","article-title":"Vibrational optical activity","volume":"492","author":"Barron","year":"2010","journal-title":"Chem. Phys. Lett."},{"key":"10.1016\/j.addr.2011.07.006_bb1140","series-title":"The Handbook of Vibrational Spectroscopy","article-title":"Applications of vibrational optical activity in the pharmaceutical industry","author":"Nafie","year":"2007"},{"key":"10.1016\/j.addr.2011.07.006_bb1145","doi-asserted-by":"crossref","unstructured":"M.D. Fayer, Dynamics of water interacting with interfaces, molecules, and ions, Acc. Chem. Res. (in press), doi:10.1021\/ar2000088.","DOI":"10.1021\/ar2000088"},{"key":"10.1016\/j.addr.2011.07.006_bb1150","doi-asserted-by":"crossref","first-page":"17187","DOI":"10.1021\/jp109203b","article-title":"Conformational switching between protein substates studied with 2D IR vibrational echo spectroscopy and molecular dynamics simulations","volume":"114","author":"Bagchi","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1155","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1073\/pnas.0811489106","article-title":"Ion-water hydrogen-bond switching observed with 2D IR vibrational echo chemical exchange spectroscopy","volume":"106","author":"Moilanen","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1160","doi-asserted-by":"crossref","first-page":"1210","DOI":"10.1021\/ar900043h","article-title":"Water dynamics in salt solutions studied with ultrafast two-dimensional infrared (2D IR) vibrational echo spectroscopy","volume":"42","author":"Fayer","year":"2009","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb1165","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1146\/annurev-physchem-073108-112712","article-title":"Dynamics of liquids, molecules, and proteins measured with ultrafast 2D IR vibrational echo chemical exchange spectroscopy","volume":"60","author":"Fayer","year":"2009","journal-title":"Annu. Rev. Phys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1170","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1021\/ar068010d","article-title":"Ultrafast 2D IR vibrational echo spectroscopy","volume":"40","author":"Zheng","year":"2007","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb1175","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1021\/ar700188n","article-title":"Amide I two-dimensional infrared spectroscopy of proteins","volume":"41","author":"Ganim","year":"2008","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb1180","doi-asserted-by":"crossref","first-page":"2888","DOI":"10.1021\/jp053956a","article-title":"Visualization and characterization of the infrared active amide I vibrations of proteins","volume":"110","author":"Chung","year":"2006","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1185","doi-asserted-by":"crossref","first-page":"9731","DOI":"10.1021\/jp201794n","article-title":"Identification of arginine residues in peptides by 2D-IR echo spectroscopy","volume":"115","author":"Ghosh","year":"2011","journal-title":"J. Phys. Chem. A"},{"key":"10.1016\/j.addr.2011.07.006_bb1190","doi-asserted-by":"crossref","first-page":"15382","DOI":"10.1021\/jp9069256","article-title":"Ultrafast vibrational spectroscopy of a degenerate mode of guanidinium chloride","volume":"113","author":"Vorobyev","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1195","doi-asserted-by":"crossref","first-page":"17751","DOI":"10.1073\/pnas.0909888106","article-title":"2D IR provides evidence for mobile water molecules in beta-amyloid fibrils","volume":"106","author":"Kim","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1200","doi-asserted-by":"crossref","first-page":"14189","DOI":"10.1073\/pnas.0706002104","article-title":"Multidimensional ultrafast spectroscopy special feature: multidimensional ultrafast spectroscopy","volume":"104","author":"Hochstrasser","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1205","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/0076-6879(95)46006-3","article-title":"Circular dichroism","volume":"246","author":"Woody","year":"1995","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.addr.2011.07.006_bb1210","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/S0076-6879(04)83013-1","article-title":"Computation and analysis of protein circular dichroism spectra","volume":"383","author":"Sreerama","year":"2004","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.addr.2011.07.006_bb1215","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1110\/ps.03258404","article-title":"On the analysis of membrane protein circular dichroism spectra","volume":"13","author":"Sreerama","year":"2004","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1220","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1002\/prot.340070302","article-title":"Protein secondary structure and circular dichroism: a practical guide","volume":"7","author":"Johnson","year":"1990","journal-title":"Proteins: Struct. Funct. Genet."},{"key":"10.1016\/j.addr.2011.07.006_bb1225","series-title":"Methods for Structural Analysis of Protein Pharmaceuticals","article-title":"Ultraviolet absorption spectroscopy","author":"Kueltzo","year":"2005"},{"key":"10.1016\/j.addr.2011.07.006_bb1230","first-page":"91","article-title":"Ultraviolet absorption spectroscopy","volume":"40","author":"Mach","year":"1995","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb1235","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1002\/jps.22385","article-title":"Ultraviolet spectroscopy as a tool in therapeutic protein development","volume":"100","author":"Mach","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1240","doi-asserted-by":"crossref","first-page":"1805","DOI":"10.1002\/jps.10439","article-title":"Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: a bGCSF case study","volume":"92","author":"Kueltzo","year":"2003","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1245","doi-asserted-by":"crossref","first-page":"2603","DOI":"10.1002\/pro.264","article-title":"Temperature dependent 2nd derivative absorbance spectroscopy of aromatic amino acids as a probe of protein dynamics","volume":"18","author":"Esfandiary","year":"2009","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1250","doi-asserted-by":"crossref","first-page":"2228","DOI":"10.1110\/ps.062133706","article-title":"Probing protein structure and dynamics by second-derivative ultraviolet absorption analysis of cation\u2013{pi} interactions","volume":"15","author":"Lucas","year":"2006","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1255","series-title":"Principles of Fluorescence Spectroscopy","author":"Lakowicz","year":"1999"},{"key":"10.1016\/j.addr.2011.07.006_bb1260","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1177\/37.8.2666510","article-title":"Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation","volume":"37","author":"Klunk","year":"1989","journal-title":"J. Histochem. Cytochem."},{"key":"10.1016\/j.addr.2011.07.006_bb1265","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/S0076-6879(99)09020-5","article-title":"Quantification of beta-sheet amyloid fibril structures with thioflavin T","volume":"309","author":"LeVine","year":"1999","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.addr.2011.07.006_bb1270","doi-asserted-by":"crossref","first-page":"15288","DOI":"10.1021\/bi061712q","article-title":"Conformational flexibility, hydration and state parameter fluctuations of fibroblast growth factor-10: effects of ligand binding","volume":"45","author":"Kamerzell","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb1275","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1002\/jps.20762","article-title":"Effects of stabilizers on the destabilization of proteins upon adsorption to aluminum salt adjuvants","volume":"96","author":"Peek","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1280","series-title":"Broadband Dielectric Spectroscopy","author":"Kremer","year":"2002"},{"key":"10.1016\/j.addr.2011.07.006_bb1285","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1002\/jps.2600840902","article-title":"Dielectric relaxation spectroscopy and some applications in the pharmaceutical sciences","volume":"84","author":"Smith","year":"1995","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1290","doi-asserted-by":"crossref","first-page":"3240","DOI":"10.1021\/jp710061a","article-title":"Immunoglobulin dynamics, conformational fluctuations, and nonlinear elasticity and their effects on stability","volume":"112","author":"Kamerzell","year":"2008","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1295","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1002\/bip.360330103","article-title":"Hydrational and intrinsic compressibilities of globular proteins","volume":"33","author":"Kharakoz","year":"1993","journal-title":"Biopolymers"},{"key":"10.1016\/j.addr.2011.07.006_bb1300","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1146\/annurev.bb.20.060191.001541","article-title":"Ultrasonic velocimetry of biological compounds","volume":"20","author":"Sarvazyan","year":"1991","journal-title":"Annu. Rev. Biophys. Biophys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1305","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1110\/ps.062393707","article-title":"The effects of cosolutes on protein dynamics: the reversal of denaturant-induced protein fluctuations by trimethylamine N-oxide","volume":"16","author":"Doan-Nguyen","year":"2007","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1310","doi-asserted-by":"crossref","first-page":"2605","DOI":"10.1002\/pro.5560041218","article-title":"Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy","volume":"4","author":"Frank","year":"1995","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1315","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1038\/78963","article-title":"Protein dynamics from NMR","volume":"7","author":"Ishima","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb1320","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1126\/science.1124964","article-title":"New tools provide new insights in NMR studies of protein dynamics","volume":"312","author":"Mittermaier","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb1325","doi-asserted-by":"crossref","first-page":"4670","DOI":"10.1002\/jps.21378","article-title":"High-field solution NMR spectroscopy as a tool for assessing protein interactions with small molecule ligands","volume":"97","author":"Skinner","year":"2008","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1330","doi-asserted-by":"crossref","first-page":"2643","DOI":"10.1002\/jps.22055","article-title":"Probing residue-specific interactions in the stabilization of proteins using high-resolution NMR: a study of disulfide bond compensation","volume":"99","author":"Skinner","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1335","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1002\/bip.1980.360190509","article-title":"Fluctuations of protein structure as expressed in the distribution of hydrogen exchange rate constants","volume":"19","author":"Knox","year":"1980","journal-title":"Biopolymers"},{"key":"10.1016\/j.addr.2011.07.006_bb1340","doi-asserted-by":"crossref","first-page":"1757","DOI":"10.1021\/cr040432i","article-title":"Protein folding pathways studied by pulsed- and native-state hydrogen exchange","volume":"106","author":"Bai","year":"2006","journal-title":"Chem. Rev."},{"key":"10.1016\/j.addr.2011.07.006_bb1345","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1126\/science.7618079","article-title":"Protein folding intermediates: native-state hydrogen exchange","volume":"269","author":"Bai","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb1350","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1002\/pro.5560060517","article-title":"Hydrogen exchange: the modern legacy of Linderstrom-Lang","volume":"6","author":"Englander","year":"1997","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1355","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/S0959-440X(96)80090-X","article-title":"Mechanisms and uses of hydrogen exchange","volume":"6","author":"Englander","year":"1996","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb1360","doi-asserted-by":"crossref","first-page":"9762","DOI":"10.1021\/bi700645k","article-title":"Two-dimensional correlation spectroscopy reveals coupled immunoglobulin regions of differential flexibility that influence stability","volume":"46","author":"Kamerzell","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb1365","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.ab.2004.04.031","article-title":"Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery","volume":"332","author":"Lo","year":"2004","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.addr.2011.07.006_bb1370","doi-asserted-by":"crossref","first-page":"4497","DOI":"10.1002\/jps.22195","article-title":"Formulation and immunogenicity of a potential multivalent type III secretion system-based protein vaccine","volume":"99","author":"Markham","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1375","doi-asserted-by":"crossref","first-page":"3494","DOI":"10.1002\/jps.21269","article-title":"The complex inter-relationships between protein flexibility and stability","volume":"97","author":"Kamerzell","year":"2008","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1380","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1002\/bio.671","article-title":"The red-edge effects: 30years of exploration","volume":"17","author":"Demchenko","year":"2002","journal-title":"Luminescence"},{"key":"10.1016\/j.addr.2011.07.006_bb1385","doi-asserted-by":"crossref","first-page":"3013","DOI":"10.1021\/bi00308a026","article-title":"Red-edge excitation of fluorescence and dynamic properties of proteins and membranes","volume":"23","author":"Lakowicz","year":"1984","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb1390","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.bpc.2010.12.010","article-title":"Applications of pressure perturbation calorimetry in biophysical studies","volume":"156","author":"Zhai","year":"2011","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1395","doi-asserted-by":"crossref","first-page":"16881","DOI":"10.1021\/jp105627w","article-title":"Volume changes associated with guanidine hydrochloride, temperature, and ethanol induced unfolding of lysozyme","volume":"114","author":"Sirotkin","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1400","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1002\/cphc.200301080","article-title":"Pressure perturbation calorimetry: a new technique provides surprising results on the effects of co-solvents on protein solvation and unfolding behaviour","volume":"5","author":"Ravindra","year":"2004","journal-title":"Chemphyschem"},{"key":"10.1016\/j.addr.2011.07.006_bb1405","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1146\/annurev-physchem-032210-103504","article-title":"Probing free-energy surfaces with differential scanning calorimetry","volume":"62","author":"Sanchez-Ruiz","year":"2011","journal-title":"Annu. Rev. Phys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1410","series-title":"Methods in Molecular Biology: Microscopy, Optical Spectroscopy, and Macroscopic Techniques","article-title":"Differential scanning calorimetry","author":"Cooper","year":"1994"},{"key":"10.1016\/j.addr.2011.07.006_bb1415","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/S1367-5931(99)00008-3","article-title":"Thermodynamic analysis of biomolecular interactions","volume":"3","author":"Cooper","year":"1999","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb1420","doi-asserted-by":"crossref","first-page":"950A","DOI":"10.1021\/ac00217a002","article-title":"Isothermal titration calorimetry","volume":"62","author":"Freire","year":"1990","journal-title":"Anal. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1425","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/nprot.2006.28","article-title":"Isothermal titration calorimetry to determine association constants for high-affinity ligands","volume":"1","author":"Velazquez-Campoy","year":"2006","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.addr.2011.07.006_bb1430","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/S0076-6879(08)04205-5","article-title":"Isothermal titration calorimetry: general formalism using binding polynomials","volume":"455","author":"Freire","year":"2009","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.addr.2011.07.006_bb1435","doi-asserted-by":"crossref","first-page":"1368","DOI":"10.1002\/jps.21056","article-title":"The interaction of heparin\/polyanions with bovine, porcine, and human growth hormone","volume":"97","author":"Joshi","year":"2008","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1440","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.1110\/ps.062613807","article-title":"Parathyroid hormone is a heparin\/polyanion binding protein: binding energetics and structure modification","volume":"16","author":"Kamerzell","year":"2007","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1445","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1002\/jps.20753","article-title":"Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability","volume":"96","author":"Harn","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1450","doi-asserted-by":"crossref","first-page":"9195","DOI":"10.1021\/bi9630164","article-title":"Preferential solvation changes upon lysozyme heat denaturation in mixed solvents","volume":"36","author":"Kovrigin","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb1455","doi-asserted-by":"crossref","first-page":"8621","DOI":"10.1021\/bi00027a011","article-title":"An osmolyte effect on the heat capacity change for protein folding","volume":"34","author":"Plaza del Pino","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb1460","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1002\/bip.1975.360140509","article-title":"Macromolecular binding","volume":"14","author":"Schellman","year":"1975","journal-title":"Biopolymers"},{"key":"10.1016\/j.addr.2011.07.006_bb1465","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/0301-4622(90)88013-I","article-title":"A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures","volume":"37","author":"Schellman","year":"1990","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1470","first-page":"1201","article-title":"Microcalorimetric study of the effect of dimethylsulfoxide on the heat denaturation of lysozyme","volume":"41","author":"Kovrigin","year":"1996","journal-title":"Biofizika"},{"key":"10.1016\/j.addr.2011.07.006_bb1475","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S0301-4622(99)00122-2","article-title":"On the stabilizing action of protein denaturants: acetonitrile effect on stability of lysozyme in aqueous solutions","volume":"83","author":"Kovrigin","year":"2000","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1480","doi-asserted-by":"crossref","first-page":"3336","DOI":"10.1021\/bi036106z","article-title":"Effects of chaotropic and kosmotropic cosolvents on the pressure-induced unfolding and denaturation of proteins: an FT-IR study on staphylococcal nuclease","volume":"43","author":"Herberhold","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb1485","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1126\/science.1166135","article-title":"Four-dimensional electron microscopy","volume":"328","author":"Zewail","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb1490","doi-asserted-by":"crossref","first-page":"8702","DOI":"10.1364\/OE.15.008702","article-title":"Target-locking acquisition with real-time confocal (TARC) microscopy","volume":"15","author":"Lu","year":"2007","journal-title":"Opt. Express"},{"key":"10.1016\/j.addr.2011.07.006_bb1495","series-title":"Encyclopedia of Biomaterials and Biomedical Engineering","article-title":"Confocal microscopy","author":"Semwogerere","year":"2005"},{"key":"10.1016\/j.addr.2011.07.006_bb1500","doi-asserted-by":"crossref","first-page":"113102","DOI":"10.1088\/0953-8984\/19\/11\/113102","article-title":"Confocal microscopy of colloids","volume":"19","author":"Prasad","year":"2007","journal-title":"J. Phys. Condens. Matter"},{"key":"10.1016\/j.addr.2011.07.006_bb1505","doi-asserted-by":"crossref","first-page":"14678","DOI":"10.1073\/pnas.96.26.14678","article-title":"Varieties of imaging with scanning probe microscopes","volume":"96","author":"Hansma","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1510","doi-asserted-by":"crossref","first-page":"1110","DOI":"10.1126\/science.1176210","article-title":"The chemical structure of a molecule resolved by atomic force microscopy","volume":"325","author":"Gross","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb1515","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1038\/nmeth871","article-title":"Detection and localization of single molecular recognition events using atomic force microscopy","volume":"3","author":"Hinterdorfer","year":"2006","journal-title":"Nat. Methods"},{"key":"10.1016\/j.addr.2011.07.006_bb1520","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1016\/S0006-3495(93)81433-4","article-title":"Imaging viscoelasticity by force modulation with the atomic force microscope","volume":"64","author":"Radmacher","year":"1993","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1525","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/j.sbi.2009.09.005","article-title":"Force and function: probing proteins with AFM-based force spectroscopy","volume":"19","author":"Puchner","year":"2009","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb1530","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1038\/nmat1925","article-title":"Nanoscale compositional mapping with gentle forces","volume":"6","author":"Garcia","year":"2007","journal-title":"Nat. Mater."},{"key":"10.1016\/j.addr.2011.07.006_bb1535","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/nnano.2007.226","article-title":"An atomic force microscope tip designed to measure time-varying nanomechanical forces","volume":"2","author":"Sahin","year":"2007","journal-title":"Nat. Nanotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb1540","doi-asserted-by":"crossref","first-page":"9759","DOI":"10.1073\/pnas.1101934108","article-title":"Probing osmolyte participation in the unfolding transition state of a protein","volume":"108","author":"Dougan","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1545","doi-asserted-by":"crossref","first-page":"10540","DOI":"10.1073\/pnas.0902090106","article-title":"Osmolyte-induced separation of the mechanical folding phases of ubiquitin","volume":"106","author":"Garcia-Manyes","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1550","doi-asserted-by":"crossref","first-page":"3185","DOI":"10.1073\/pnas.0706075105","article-title":"Solvent molecules bridge the mechanical unfolding transition state of a protein","volume":"105","author":"Dougan","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1555","doi-asserted-by":"crossref","first-page":"2156","DOI":"10.1110\/ps.037325.108","article-title":"The effects of macromolecular crowding on the mechanical stability of protein molecules","volume":"17","author":"Yuan","year":"2008","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1560","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1016\/j.jmb.2007.10.024","article-title":"How do chemical denaturants affect the mechanical folding and unfolding of proteins?","volume":"375","author":"Cao","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb1565","doi-asserted-by":"crossref","first-page":"38438","DOI":"10.1074\/jbc.M110.183913","article-title":"Naturally occurring osmolytes modulate the nanomechanical properties of polycystic kidney disease domains","volume":"285","author":"Ma","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1570","doi-asserted-by":"crossref","first-page":"e1176","DOI":"10.1371\/journal.pone.0001176","article-title":"Inhibition of protein aggregation: supramolecular assemblies of arginine hold the key","volume":"2","author":"Das","year":"2007","journal-title":"PLoS One"},{"key":"10.1016\/j.addr.2011.07.006_bb1575","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1023\/A:1016286600229","article-title":"Stability of protein formulations: investigation of surfactant effects by a novel EPR spectroscopic technique","volume":"12","author":"Bam","year":"1995","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb1580","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1023\/A:1018809632395","article-title":"Investigation of protein\u2013surfactant interactions by analytical ultracentrifugation and electron paramagnetic resonance: the use of recombinant human tissue factor as an example","volume":"16","author":"Jones","year":"1999","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb1585","doi-asserted-by":"crossref","first-page":"2464","DOI":"10.1002\/jps.21632","article-title":"The fate of free radicals in a cellulose based hydrogel: detection by electron paramagnetic resonance spectroscopy","volume":"98","author":"Basumallick","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1590","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/S0001-8686(99)00017-2","article-title":"Dynamic surface tension and adsorption mechanisms of surfactants at the air\u2013water interface","volume":"85","author":"Eastoe","year":"2000","journal-title":"Adv. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1595","doi-asserted-by":"crossref","first-page":"15366","DOI":"10.1021\/la102721m","article-title":"Interfacial activity and interfacial shear rheology of native beta-lactoglobulin monomers and their heat-induced fibers","volume":"26","author":"Jung","year":"2010","journal-title":"Langmuir"},{"key":"10.1016\/j.addr.2011.07.006_bb1600","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1021\/la1040757","article-title":"Adsorption of protein\u2013surfactant complexes at the water\/oil interface","volume":"27","author":"Pradines","year":"2011","journal-title":"Langmuir"},{"key":"10.1016\/j.addr.2011.07.006_bb1605","doi-asserted-by":"crossref","first-page":"1759","DOI":"10.1002\/bip.1978.360170711","article-title":"Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air\u2013water interface","volume":"17","author":"De Feijter","year":"1978","journal-title":"Biopolymers"},{"key":"10.1016\/j.addr.2011.07.006_bb1610","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.cis.2005.01.001","article-title":"Interfacial dynamics and structure of surfactant layers","volume":"113","author":"Zhmud","year":"2005","journal-title":"Adv. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1615","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1039\/B111163A","article-title":"Neutron reflection studies of interactions between surfactants and proteins at interfaces","volume":"98","author":"Lu","year":"2002","journal-title":"Annu. Rep. Prog. Chem. C: Phys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1620","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0001-8686(99)00019-6","article-title":"Surfactant layers at the air\/water interface: structure and composition","volume":"84","author":"Lu","year":"2000","journal-title":"Adv. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1625","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.cocis.2007.02.001","article-title":"Protein adsorption studied by neutron reflection","volume":"12","author":"Lu","year":"2007","journal-title":"Curr. Opin. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1630","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1039\/f19817701437","article-title":"Critical reflection of neutrons. A new technique for investigating interfacial phenomena","volume":"77","author":"Hayter","year":"1981","journal-title":"J. Chem. Soc., Faraday Trans. 1 F"},{"key":"10.1016\/j.addr.2011.07.006_bb1635","doi-asserted-by":"crossref","first-page":"2179","DOI":"10.1039\/b515934b","article-title":"The adsorbed conformation of globular proteins at the air\/water interface","volume":"8","author":"Lad","year":"2006","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.addr.2011.07.006_bb1640","doi-asserted-by":"crossref","first-page":"3478","DOI":"10.1039\/b506558p","article-title":"Protein\u2013lipid interactions at the air\/water interface","volume":"7","author":"Lad","year":"2005","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.addr.2011.07.006_bb1645","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/S0006-3495(83)84328-8","article-title":"Immunoglobulin surface-binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy","volume":"43","author":"Thompson","year":"1983","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1650","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/S0006-3495(81)84905-3","article-title":"Measuring surface dynamics of biomolecules by total internal reflection fluorescence with photobleaching recovery or correlation spectroscopy","volume":"33","author":"Thompson","year":"1981","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1655","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1016\/j.jcis.2007.09.089","article-title":"Protein\u2013surfactant interactions at hydrophobic interfaces studied with total internal reflection fluorescence correlation spectroscopy (TIR-FCS)","volume":"317","author":"Sonesson","year":"2008","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1660","doi-asserted-by":"crossref","first-page":"5591","DOI":"10.1073\/pnas.1031596100","article-title":"Hessian eigenmaps: locally linear embedding techniques for high-dimensional data","volume":"100","author":"Donoho","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1665","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1097\/01.NNR.0000280659.88760.7c","article-title":"Multidimensional scaling: a brief overview","volume":"57","author":"Mugavin","year":"2008","journal-title":"Nurs. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb1670","series-title":"Multidimensional Scaling","author":"Cox","year":"2001"},{"key":"10.1016\/j.addr.2011.07.006_bb1675","doi-asserted-by":"crossref","first-page":"2323","DOI":"10.1126\/science.290.5500.2323","article-title":"Nonlinear dimensionality reduction by locally linear embedding","volume":"290","author":"Roweis","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb1680","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1016\/S0893-6080(02)00069-2","article-title":"How to make large self-organizing maps for nonvectorial data","volume":"15","author":"Kohonen","year":"2002","journal-title":"Neural Netw."},{"key":"10.1016\/j.addr.2011.07.006_bb1685","doi-asserted-by":"crossref","first-page":"1227a","DOI":"10.1126\/science.235.4793.1227a","article-title":"Computing with neural networks","volume":"235","author":"Kohonen","year":"1987","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb1690","series-title":"Pattern Recognition","author":"Theodoridis","year":"2009"},{"key":"10.1016\/j.addr.2011.07.006_bb1695","series-title":"Two-dimensional Correlation Spectroscopy: Applications in Vibrational and Optical Spectroscopy","author":"Noda","year":"2004"},{"key":"10.1016\/j.addr.2011.07.006_bb1700","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1366\/0003702904087398","article-title":"Two-dimensional infrared (2D IR) spectroscopy: theory and applications","volume":"44","author":"Noda","year":"1990","journal-title":"Appl. Spectrosc."},{"key":"10.1016\/j.addr.2011.07.006_bb1705","first-page":"520","volume":"31","author":"Noda","year":"1986","journal-title":"Bull. Am. Phys. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb1710","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1002\/jps.22389","article-title":"The relative rate of immunoglobulin gamma 1 fragmentation","volume":"100","author":"Kamerzell","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1715","series-title":"Principal Component Analysis","author":"Jolliffe","year":"2004"},{"key":"10.1016\/j.addr.2011.07.006_bb1720","doi-asserted-by":"crossref","first-page":"1438","DOI":"10.1016\/S0006-3495(91)82180-4","article-title":"Measuring electrostatic, van der Waals, and hydration forces in electrolyte solutions with an atomic force microscope","volume":"60","author":"Butt","year":"1991","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1725","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/S0006-3495(91)82112-9","article-title":"Electrostatic interaction in atomic force microscopy","volume":"60","author":"Butt","year":"1991","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1730","doi-asserted-by":"crossref","first-page":"3277","DOI":"10.1016\/S0006-3495(02)75669-5","article-title":"Myoglobin-CO conformational substate dynamics: 2D vibrational echoes and MD simulations","volume":"82","author":"Merchant","year":"2002","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1735","doi-asserted-by":"crossref","first-page":"11016","DOI":"10.1021\/jp050257p","article-title":"Amide I vibrational dynamics of N-methylacetamide in polar solvents: the role of electrostatic interactions","volume":"109","author":"DeCamp","year":"2005","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1740","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/nnano.2007.293","article-title":"Label-free and high-resolution protein\/DNA nanoarray analysis using Kelvin probe force microscopy","volume":"2","author":"Sinensky","year":"2007","journal-title":"Nat. Nanotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb1745","doi-asserted-by":"crossref","first-page":"2769","DOI":"10.1021\/nl9012979","article-title":"Imaging surface charges of individual biomolecules","volume":"9","author":"Leung","year":"2009","journal-title":"Nano Lett."},{"key":"10.1016\/j.addr.2011.07.006_bb1750","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1006\/jmbi.1999.3470","article-title":"Thermodynamics of DNA binding and condensation: isothermal titration calorimetry and electrostatic mechanism","volume":"296","author":"Matulis","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb1755","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.cocis.2004.05.018","article-title":"Influence of salts on rhodopsin photoproduct equilibria and protein stability","volume":"9","author":"Vogel","year":"2004","journal-title":"Curr. Opin. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1760","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/S0301-4622(02)00168-0","article-title":"Use of T4 lysozyme charge mutants to examine electrophoretic models","volume":"101\u2013102","author":"Durant","year":"2002","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1765","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1039\/b616078f","article-title":"Ultrafast dynamics in complex fluids observed through the ultrafast optically-heterodyne-detected optical-Kerr-effect (OHD-OKE)","volume":"9","author":"Hunt","year":"2007","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.addr.2011.07.006_bb1770","doi-asserted-by":"crossref","first-page":"2972","DOI":"10.1021\/jp8067393","article-title":"Stark realities","volume":"113","author":"Boxer","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1775","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1103\/PhysRevLett.17.463","article-title":"Electric-field level-crossing spectroscopy","volume":"17","author":"Khadjavi","year":"1966","journal-title":"Phys. Rev. Lett."},{"key":"10.1016\/j.addr.2011.07.006_bb1780","doi-asserted-by":"crossref","first-page":"4510","DOI":"10.1063\/1.1727531","article-title":"Molecular level-crossing spectroscopy","volume":"45","author":"Zare","year":"1966","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.addr.2011.07.006_bb1785","doi-asserted-by":"crossref","first-page":"2693","DOI":"10.1021\/cr0006876","article-title":"Molecular bonding and interactions at aqueous surfaces as probed by vibrational sum frequency spectroscopy","volume":"102","author":"Richmond","year":"2002","journal-title":"Chem. Rev."},{"key":"10.1016\/j.addr.2011.07.006_bb1790","doi-asserted-by":"crossref","first-page":"2056","DOI":"10.1016\/S0006-3495(96)79404-3","article-title":"How Hofmeister ion interactions affect protein stability","volume":"71","author":"Baldwin","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1795","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1038\/nchem.154","article-title":"Water dynamics: ion-ing out the details","volume":"1","author":"Bakker","year":"2009","journal-title":"Nat. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1800","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1126\/science.1084801","article-title":"Negligible effect of ions on the hydrogen-bond structure in liquid water","volume":"301","author":"Omta","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb1805","doi-asserted-by":"crossref","first-page":"1006","DOI":"10.1126\/science.1183512","article-title":"Cooperativity in ion hydration","volume":"328","author":"Tielrooij","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb1810","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1002\/pro.20","article-title":"Ion-specific modulation of protein interactions: anion-induced, reversible oligomerization of a fusion protein","volume":"18","author":"Gokarn","year":"2009","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb1815","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/0167-4838(93)90031-L","article-title":"Sucralfate and soluble sucrose octasulfate bind and stabilize acidic fibroblast growth factor","volume":"1203","author":"Volkin","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.addr.2011.07.006_bb1820","doi-asserted-by":"crossref","first-page":"6419","DOI":"10.1021\/bi00076a015","article-title":"Effect of polyanions on the unfolding of acidic fibroblast growth factor","volume":"32","author":"Burke","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb1825","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1021\/jp108586b","article-title":"Preferential interaction coefficients of proteins in aqueous arginine solutions and their molecular origins","volume":"115","author":"Shukla","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1830","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1021\/cr9603744","article-title":"The cation\u2013pi interaction","volume":"97","author":"Ma","year":"1997","journal-title":"Chem. Rev."},{"key":"10.1016\/j.addr.2011.07.006_bb1835","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1126\/science.271.5246.163","article-title":"Cation\u2013pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp","volume":"271","author":"Dougherty","year":"1996","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb1840","doi-asserted-by":"crossref","first-page":"9459","DOI":"10.1073\/pnas.96.17.9459","article-title":"Cation\u2013pi interactions in structural biology","volume":"96","author":"Gallivan","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1845","doi-asserted-by":"crossref","first-page":"1737","DOI":"10.1021\/ja043475p","article-title":"Structural and thermodynamic studies on cation\u2013pi interactions in lectin\u2013ligand complexes: high-affinity galectin-3 inhibitors through fine-tuning of an arginine\u2013arene interaction","volume":"127","author":"Sorme","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb1850","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pep.2005.03.028","article-title":"Is arginine a protein-denaturant?","volume":"42","author":"Ishibashi","year":"2005","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.addr.2011.07.006_bb1855","doi-asserted-by":"crossref","first-page":"4919","DOI":"10.1021\/bi047528r","article-title":"Role of arginine in the stabilization of proteins against aggregation","volume":"44","author":"Baynes","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb1860","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1002\/prot.20417","article-title":"Cation\u2013pi interactions in protein\u2013protein interfaces","volume":"59","author":"Crowley","year":"2005","journal-title":"Proteins"},{"key":"10.1016\/j.addr.2011.07.006_bb1865","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/0076-6879(79)61005-4","article-title":"Measurements of preferential solvent interactions by densimetric techniques","volume":"61","author":"Lee","year":"1979","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.addr.2011.07.006_bb1870","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1021\/bi00699a005","article-title":"Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride","volume":"13","author":"Lee","year":"1974","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb1875","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1529\/biophysj.105.078790","article-title":"Chemical potential derivatives and preferential interaction parameters in biological systems from Kirkwood\u2013Buff theory","volume":"91","author":"Smith","year":"2006","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1880","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/S0006-3495(03)74459-2","article-title":"Protein stability in mixed solvents: a balance of contact interaction and excluded volume","volume":"85","author":"Schellman","year":"2003","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1885","doi-asserted-by":"crossref","first-page":"9721","DOI":"10.1073\/pnas.122225399","article-title":"Protein\u2013solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components","volume":"99","author":"Timasheff","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1890","doi-asserted-by":"crossref","first-page":"3987","DOI":"10.1073\/pnas.97.8.3987","article-title":"Osmotic stress, crowding, preferential hydration, and binding: a comparison of perspectives","volume":"97","author":"Parsegian","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1895","doi-asserted-by":"crossref","first-page":"4586","DOI":"10.1021\/bi00839a053","article-title":"Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25 degrees","volume":"8","author":"Aune","year":"1969","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb1900","doi-asserted-by":"crossref","first-page":"7447","DOI":"10.1021\/jp111920y","article-title":"Arginine and the hofmeister series: the role of ion\u2013ion interactions in protein aggregation suppression","volume":"115","author":"Schneider","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1905","doi-asserted-by":"crossref","first-page":"2050","DOI":"10.1021\/jp808042w","article-title":"Investigation of cosolute\u2013protein preferential interaction coefficients: new insight into the mechanism by which arginine inhibits aggregation","volume":"113","author":"Schneider","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1910","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1016\/j.bpj.2010.11.087","article-title":"An effective solvent theory connecting the underlying mechanisms of osmolytes and denaturants for protein stability","volume":"100","author":"Linhananta","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1915","doi-asserted-by":"crossref","first-page":"13997","DOI":"10.1073\/pnas.0606236103","article-title":"A molecular mechanism for osmolyte-induced protein stability","volume":"103","author":"Street","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1920","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1021\/ja004206b","article-title":"The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea","volume":"124","author":"Zou","year":"2002","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb1925","doi-asserted-by":"crossref","first-page":"4038","DOI":"10.1021\/jp805458p","article-title":"Destabilization of the hydrogen-bond structure of water by the osmolyte trimethylamine N-oxide","volume":"113","author":"Rezus","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1930","doi-asserted-by":"crossref","first-page":"14797","DOI":"10.1021\/jp904001m","article-title":"Effects of urea and trimethylamine-N-oxide on the properties of water and the secondary structure of hen egg white lysozyme","volume":"113","author":"Panuszko","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1935","doi-asserted-by":"crossref","first-page":"11743","DOI":"10.1021\/jp903413v","article-title":"Molecular anatomy of preferential interaction coefficients by elucidating protein solvation in mixed solvents: methodology and application for lysozyme in aqueous glycerol","volume":"113","author":"Vagenende","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1940","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1016\/S0006-3495(03)74512-3","article-title":"Specific ion effects: why the properties of lysozyme in salt solutions follow a Hofmeister series","volume":"85","author":"Bostrom","year":"2003","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1945","doi-asserted-by":"crossref","first-page":"16928","DOI":"10.1073\/pnas.0808427105","article-title":"Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding","volume":"105","author":"Hua","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb1950","doi-asserted-by":"crossref","first-page":"7379","DOI":"10.1021\/ja051020+","article-title":"Molecular recognition of saccharides by proteins. Insights on the origin of the carbohydrate\u2013aromatic interactions","volume":"127","author":"del Carmen Fernandez-Alonso","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb1955","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1016\/S0006-3495(96)79641-8","article-title":"Van der Waals interactions involving proteins","volume":"70","author":"Roth","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb1960","doi-asserted-by":"crossref","first-page":"2538","DOI":"10.1021\/j100806a008","article-title":"Additivity of intermolecular forces at interfaces. I. Determination of the contribution to surface and interfacial tensions of dispersion forces in various liquids","volume":"67","author":"Fowkes","year":"1963","journal-title":"J. Phys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb1965","doi-asserted-by":"crossref","first-page":"2117","DOI":"10.1111\/j.1151-2916.2000.tb01527.x","article-title":"Origins and applications of London dispersion forces and hamaker constants in ceramics","volume":"83","author":"French","year":"2000","journal-title":"J. Am. Ceram. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb1970","doi-asserted-by":"crossref","first-page":"3500","DOI":"10.1021\/la00009a036","article-title":"Electrostatic and van der Waals contributions to protein adsorption: comparison of theory and experiment","volume":"11","author":"Roth","year":"1995","journal-title":"Langmuir"},{"key":"10.1016\/j.addr.2011.07.006_bb1975","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1021\/ar50090a001","article-title":"Structure and properties of van der Waals molecules","volume":"8","author":"Ewing","year":"1975","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb1980","series-title":"Molecular Spectroscopy","author":"McHale","year":"1999"},{"key":"10.1016\/j.addr.2011.07.006_bb1985","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1021\/jp9084926","article-title":"Effects of urea, tetramethyl urea, and trimethylamine N-oxide on aqueous solution structure and solvation of protein backbones: a molecular dynamics simulation study","volume":"114","author":"Wei","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb1990","doi-asserted-by":"crossref","first-page":"1535","DOI":"10.1021\/ja807887g","article-title":"Urea's action on hydrophobic interactions","volume":"131","author":"Zangi","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb1995","doi-asserted-by":"crossref","first-page":"3323","DOI":"10.1021\/la903061h","article-title":"Why direct or reversed Hofmeister series? Interplay of hydration, non-electrostatic potentials, and ion size","volume":"26","author":"Parsons","year":"2010","journal-title":"Langmuir"},{"key":"10.1016\/j.addr.2011.07.006_bb2000","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.bpc.2005.05.010","article-title":"Why forces between proteins follow different Hofmeister series for pH above and below pI","volume":"117","author":"Bostrom","year":"2005","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb2005","doi-asserted-by":"crossref","first-page":"24489","DOI":"10.1021\/jp0551869","article-title":"Specific ion effects in solutions of globular proteins: comparison between analytical models and simulation","volume":"109","author":"Bostrom","year":"2005","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb2010","doi-asserted-by":"crossref","first-page":"2619","DOI":"10.1021\/la047437v","article-title":"Hofmeister effects in surface tension of aqueous electrolyte solution","volume":"21","author":"Bostrom","year":"2005","journal-title":"Langmuir"},{"key":"10.1016\/j.addr.2011.07.006_bb2015","doi-asserted-by":"crossref","first-page":"2502","DOI":"10.1110\/ps.04812804","article-title":"Energetics of galactose- and glucose\u2013aromatic amino acid interactions: implications for binding in galactose-specific proteins","volume":"13","author":"Sujatha","year":"2004","journal-title":"Protein Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2020","doi-asserted-by":"crossref","first-page":"8554","DOI":"10.1021\/bi050298b","article-title":"Insights into the role of the aromatic residue in galactose-binding sites: MP2\/6-311G++** study on galactose- and glucose\u2013aromatic residue analogue complexes","volume":"44","author":"Sujatha","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb2025","doi-asserted-by":"crossref","first-page":"2890","DOI":"10.1021\/ja066633g","article-title":"A simple model system for the study of carbohydrate\u2013aromatic interactions","volume":"129","author":"Terraneo","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb2030","doi-asserted-by":"crossref","first-page":"4444","DOI":"10.1039\/b704792d","article-title":"Carbohydrate molecular recognition: a spectroscopic investigation of carbohydrate\u2013aromatic interactions","volume":"9","author":"Stanca-Kaposta","year":"2007","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.addr.2011.07.006_bb2035","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1016\/S0959-440X(94)90170-8","article-title":"Structure and energetics of protein\u2013carbohydrate complexes","volume":"4","author":"Toone","year":"1994","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb2040","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/S0968-0004(97)01146-8","article-title":"Lectin\u2013carbohydrate interactions: different folds, common recognition principles","volume":"22","author":"Elgavish","year":"1997","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2045","doi-asserted-by":"crossref","first-page":"6369","DOI":"10.1073\/pnas.1016653108","article-title":"Quantum nature of the hydrogen bond","volume":"108","author":"Li","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb2050","doi-asserted-by":"crossref","first-page":"184112","DOI":"10.1063\/1.2378807","article-title":"The nature of the hydrogen bond: a synthesis from the interacting quantum atoms picture","volume":"125","author":"Martin Pendas","year":"2006","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.addr.2011.07.006_bb2055","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1021\/cr60277a004","article-title":"The theory of the hydrogen bond","volume":"72","author":"Kollman","year":"1972","journal-title":"Chem. Rev."},{"key":"10.1016\/j.addr.2011.07.006_bb2060","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/0076-6879(86)27009-3","article-title":"Low frequency Raman scattering from water and aqueous solution: a direct measure of hydrogen bonding","volume":"127","author":"Walrafen","year":"1986","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.addr.2011.07.006_bb2065","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/0076-6879(86)27014-7","article-title":"Determination of water structure around biomolecules using X-ray and neutron diffraction methods","volume":"127","author":"Savage","year":"1986","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.addr.2011.07.006_bb2070","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/S0076-6879(02)38217-X","article-title":"Scalar couplings across hydrogen bonds","volume":"338","author":"Grzesiek","year":"2001","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.addr.2011.07.006_bb2075","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.biophys.32.110601.142417","article-title":"Protein analysis by hydrogen exchange mass spectrometry","volume":"32","author":"Hoofnagle","year":"2003","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1016\/j.addr.2011.07.006_bb2080","doi-asserted-by":"crossref","first-page":"3916","DOI":"10.1021\/bi00435a044","article-title":"An infrared spectroscopic study of the interactions of carbohydrates with dried proteins","volume":"28","author":"Carpenter","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb2085","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/0011-2240(88)90032-6","article-title":"The mechanism of cryoprotection of proteins by solutes","volume":"25","author":"Carpenter","year":"1988","journal-title":"Cryobiology"},{"key":"10.1016\/j.addr.2011.07.006_bb2090","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/0304-4165(87)90133-4","article-title":"Stabilization of phosphofructokinase with sugars during freeze-drying: characterization of enhanced protection in the presence of divalent cations","volume":"923","author":"Carpenter","year":"1987","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.addr.2011.07.006_bb2095","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/0011-2240(87)90049-6","article-title":"Stabilization of phosphofructokinase during air-drying with sugars and sugar\/transition metal mixtures","volume":"24","author":"Carpenter","year":"1987","journal-title":"Cryobiology"},{"key":"10.1016\/j.addr.2011.07.006_bb2100","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1016\/0011-2240(88)90045-4","article-title":"Long-term preservation of dried phosphofructokinase by sugars and sugar\/zinc mixtures","volume":"25","author":"Carpenter","year":"1988","journal-title":"Cryobiology"},{"key":"10.1016\/j.addr.2011.07.006_bb2105","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1016\/S0006-3495(93)81120-2","article-title":"Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers","volume":"65","author":"Prestrelski","year":"1993","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb2110","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1006\/abbi.1999.1175","article-title":"Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding","volume":"365","author":"Allison","year":"1999","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.addr.2011.07.006_bb2115","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1002\/(SICI)1520-6017(200002)89:2<199::AID-JPS7>3.0.CO;2-B","article-title":"Optimization of storage stability of lyophilized actin using combinations of disaccharides and dextran","volume":"89","author":"Allison","year":"2000","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2120","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1002\/jps.10305","article-title":"Effects of types of sugar on the stabilization of protein in the dried state","volume":"92","author":"Imamura","year":"2003","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2125","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/S0076-6879(94)47023-5","article-title":"Mapping of hydrogen bonding between saccharides and proteins in solution","volume":"247","author":"Glaudemans","year":"1994","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.addr.2011.07.006_bb2130","doi-asserted-by":"crossref","first-page":"10345","DOI":"10.1021\/ja802668w","article-title":"Thermal signature of hydrophobic hydration dynamics","volume":"130","author":"Qvist","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb2135","doi-asserted-by":"crossref","first-page":"1958","DOI":"10.1021\/ja039335h","article-title":"Impact of protein denaturants and stabilizers on water structure","volume":"126","author":"Batchelor","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.addr.2011.07.006_bb2140","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/S0091-679X(07)84022-2","article-title":"A practical guide on how osmolytes modulate macromolecular properties","volume":"84","author":"Harries","year":"2008","journal-title":"Methods Cell Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb2145","doi-asserted-by":"crossref","first-page":"2809","DOI":"10.1002\/cphc.200800522","article-title":"Effect of osmolytes on pressure-induced unfolding of proteins: a high-pressure SAXS study","volume":"9","author":"Krywka","year":"2008","journal-title":"Chemphyschem"},{"key":"10.1016\/j.addr.2011.07.006_bb2150","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1006\/abbi.2001.2351","article-title":"Maintenance of quaternary structure in the frozen state stabilizes lactate dehydrogenase during freeze-drying","volume":"390","author":"Anchordoquy","year":"2001","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.addr.2011.07.006_bb2155","doi-asserted-by":"crossref","first-page":"1390","DOI":"10.1002\/jps.20079","article-title":"Challenges in the development of high protein concentration formulations","volume":"93","author":"Shire","year":"2004","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2160","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1002\/jps.21797","article-title":"Understanding and modulating opalescence and viscosity in a monoclonal antibody formulation","volume":"99","author":"Salinas","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2165","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1529\/biophysj.107.116152","article-title":"Protein phase behavior in aqueous solutions: crystallization, liquid\u2013liquid phase separation, gels, and aggregates","volume":"94","author":"Dumetz","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb2170","series-title":"The Physics of Phase Transitions","author":"Papon","year":"2006"},{"key":"10.1016\/j.addr.2011.07.006_bb2175","series-title":"Principles of Condensed Matter Physics","author":"Chaikin","year":"1995"},{"key":"10.1016\/j.addr.2011.07.006_bb2180","series-title":"Soft Condensed Matter","author":"Jones","year":"2002"},{"key":"10.1016\/j.addr.2011.07.006_bb2185","doi-asserted-by":"crossref","first-page":"10081","DOI":"10.1021\/jp809710d","article-title":"Freezing-induced phase separation and spatial microheterogeneity in protein solutions","volume":"113","author":"Dong","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb2190","series-title":"Coarse-Graining of Condensed Phase and Biomolecular Systems","author":"Voth","year":"2009"},{"key":"10.1016\/j.addr.2011.07.006_bb2195","first-page":"725","article-title":"Intrinsic phosphorescence from proteins in the solid state","volume":"39","author":"Strambini","year":"1984","journal-title":"Photochem. Photobiol."},{"key":"10.1016\/j.addr.2011.07.006_bb2200","doi-asserted-by":"crossref","first-page":"6527","DOI":"10.1021\/bi00394a036","article-title":"Phosphorescence anisotropy of liver alcohol dehydrogenase in the crystalline state. Apparent glasslike rigidity of the coenzyme-binding domain","volume":"26","author":"Strambini","year":"1987","journal-title":"Biochemistry"},{"key":"10.1016\/j.addr.2011.07.006_bb2205","doi-asserted-by":"crossref","first-page":"21222","DOI":"10.1021\/jp0639804","article-title":"A small-angle scattering study on equilibrium clusters in lysozyme solutions","volume":"110","author":"Stradner","year":"2006","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb2210","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1038\/nature03109","article-title":"Equilibrium cluster formation in concentrated protein solutions and colloids","volume":"432","author":"Stradner","year":"2004","journal-title":"Nature"},{"key":"10.1016\/j.addr.2011.07.006_bb2215","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.ab.2009.10.033","article-title":"Vibrational spectroscopy and chemometrics to characterize and quantitate trehalose crystallization","volume":"399","author":"Connolly","year":"2010","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.addr.2011.07.006_bb2220","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nature06931","article-title":"Gelation of particles with short-range attraction","volume":"453","author":"Lu","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.addr.2011.07.006_bb2225","doi-asserted-by":"crossref","first-page":"028306","DOI":"10.1103\/PhysRevLett.96.028306","article-title":"Fluids of clusters in attractive colloids","volume":"96","author":"Lu","year":"2006","journal-title":"Phys. Rev. Lett."},{"key":"10.1016\/j.addr.2011.07.006_bb2230","doi-asserted-by":"crossref","first-page":"5075","DOI":"10.1073\/pnas.0711928105","article-title":"Absence of equilibrium cluster phase in concentrated lysozyme solutions","volume":"105","author":"Shukla","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb2235","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1021\/jz900127c","article-title":"Formation of the dynamic clusters in concentrated lysozyme protein solutions","volume":"1","author":"Porcar","year":"2010","journal-title":"J. Phys. Chem. Lett."},{"key":"10.1016\/j.addr.2011.07.006_bb2240","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1023\/A:1018805232453","article-title":"The effect of formulation excipients on protein stability and aerosol performance of spray-dried powders of a recombinant humanized anti-IgE monoclonal antibody","volume":"16","author":"Andya","year":"1999","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb2245","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0169-409X(00)00144-7","article-title":"Factors affecting short-term and long-term stabilities of proteins","volume":"46","author":"Arakawa","year":"2001","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.addr.2011.07.006_bb2250","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1007\/s11095-005-6035-4","article-title":"The effect of stabilizers and denaturants on the cold denaturation temperatures of proteins and implications for freeze-drying","volume":"22","author":"Tang","year":"2005","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb2255","doi-asserted-by":"crossref","first-page":"3627","DOI":"10.3168\/jds.S0022-0302(90)79065-0","article-title":"Comparison of solute-induced protein stabilization in aqueous solution and in the frozen and dried states","volume":"73","author":"Carpenter","year":"1990","journal-title":"J. Dairy Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2260","doi-asserted-by":"crossref","first-page":"1358","DOI":"10.1021\/js960019t","article-title":"Effects of phase separating systems on lyophilized hemoglobin","volume":"85","author":"Heller","year":"1996","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2265","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1021\/js970135b","article-title":"Phase separation of excipients during lyophilization: effects on protein stability","volume":"86","author":"Randolph","year":"1997","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2270","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/0003-9861(59)90595-8","article-title":"The effect of addition of sodium and potassium chloride to the reciprocal system: KH2PO4\u2013Na2HPO4\u2013H2O on pH and composition during freezing","volume":"84","author":"Van Den Berg","year":"1959","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.addr.2011.07.006_bb2275","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/0003-9861(59)90209-7","article-title":"Effect of freezing on the pH and composition of sodium and potassium phosphate solutions; the reciprocal system KH2PO4\u2013Na2\u2013HPO4\u2013H2O","volume":"81","author":"Van Den Berg","year":"1959","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.addr.2011.07.006_bb2280","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.1023\/A:1018988823116","article-title":"Decreased protein-stabilizing effects of cryoprotectants due to crystallization","volume":"10","author":"Izutsu","year":"1993","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb2285","doi-asserted-by":"crossref","first-page":"281","DOI":"10.3109\/10409239009090612","article-title":"Cold denaturation of proteins","volume":"25","author":"Privalov","year":"1990","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.addr.2011.07.006_bb2290","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/S0006-3495(96)79640-6","article-title":"Proteins in frozen solutions: evidence of ice-induced partial unfolding","volume":"70","author":"Strambini","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb2295","doi-asserted-by":"crossref","first-page":"2131","DOI":"10.1529\/biophysj.106.099531","article-title":"Protein stability in ice","volume":"92","author":"Strambini","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb2300","doi-asserted-by":"crossref","first-page":"2087","DOI":"10.1016\/S0006-3495(96)79407-9","article-title":"Is trehalose special for preserving dry biomaterials?","volume":"71","author":"Crowe","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb2305","doi-asserted-by":"crossref","first-page":"830","DOI":"10.3168\/jds.S0022-0302(54)91334-X","article-title":"The effect of lactose crystallization on protein stability in frozen concentrated milk","volume":"37","author":"Tumerman","year":"1954","journal-title":"J. Dairy Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2310","doi-asserted-by":"crossref","first-page":"10255","DOI":"10.1021\/jp8030122","article-title":"Specific anions effects of on the stability of azurin in ice","volume":"112","author":"Strambini","year":"2008","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb2315","series-title":"Solid State Chemistry of Drugs","author":"Byrn","year":"1999"},{"key":"10.1016\/j.addr.2011.07.006_bb2320","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1023\/B:PHAM.0000032993.98705.73","article-title":"Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association","volume":"21","author":"Sukumar","year":"2004","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb2325","first-page":"48","article-title":"Formulation effects on opalescence of a high-concentration MAb","volume":"8","author":"Woods","year":"2010","journal-title":"BioProcess Int."},{"key":"10.1016\/j.addr.2011.07.006_bb2330","doi-asserted-by":"crossref","first-page":"4587","DOI":"10.1002\/jps.22650","article-title":"Opalescence of an IgG2 monoclonal antibody solution as it relates to liquid\u2013liquid phase separation","volume":"100","author":"Mason","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2335","doi-asserted-by":"crossref","first-page":"2628","DOI":"10.1002\/jps.22046","article-title":"Quantification and characterization of subvisible proteinaceous particles in opalescent mAb formulations using micro-flow imaging","volume":"99","author":"Sharma","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2340","doi-asserted-by":"crossref","first-page":"1360","DOI":"10.1023\/A:1015888704365","article-title":"Effect of freezing on aggregation of human growth hormone","volume":"8","author":"Eckhardt","year":"1991","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb2345","first-page":"64","article-title":"A turbidimetric method to determine visual appearance of protein solutions","volume":"48","author":"Eckhardt","year":"1994","journal-title":"J. Pharm. Sci. Technol."},{"key":"10.1016\/j.addr.2011.07.006_bb2350","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-1-4899-1236-7_1","article-title":"Stability and characterization of human growth hormone","volume":"5","author":"Pearlman","year":"1993","journal-title":"Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb2355","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1023\/A:1016270103863","article-title":"Surface denaturation at solid\u2013void interface\u2014a possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen activator at high temperatures","volume":"12","author":"Hsu","year":"1995","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb2360","series-title":"The 236th ACS National Meeting","article-title":"Opalescence in antibody formulations is a solution critical phenomenon","author":"Cromwell","year":"2008"},{"key":"10.1016\/j.addr.2011.07.006_bb2365","article-title":"Opalescence of an IgG1 monoclonal antibody formulation is mediated by ionic strength and excipients","volume":"22","author":"Wang","year":"2009","journal-title":"BioPharm. Int."},{"key":"10.1016\/j.addr.2011.07.006_bb2370","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1007\/s11095-010-0125-7","article-title":"Phase separation of an IgG1 antibody solution under a low ionic strength condition","volume":"27","author":"Nishi","year":"2010","journal-title":"Pharm. Res."},{"key":"10.1016\/j.addr.2011.07.006_bb2375","doi-asserted-by":"crossref","first-page":"3792","DOI":"10.1016\/j.bpj.2010.10.040","article-title":"Liquid\u2013liquid phase separation of a monoclonal antibody and nonmonotonic influence of Hofmeister anions","volume":"99","author":"Mason","year":"2010","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb2380","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1002\/btpr.536","article-title":"Interactions and phase behavior of a monoclonal antibody","volume":"27","author":"Lewus","year":"2011","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.addr.2011.07.006_bb2385","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1529\/biophysj.106.098293","article-title":"Phase behavior of an intact monoclonal antibody","volume":"93","author":"Ahamed","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb2390","doi-asserted-by":"crossref","first-page":"14165","DOI":"10.1073\/pnas.212507199","article-title":"Effect of polyethylene glycol on the liquid\u2013liquid phase transition in aqueous protein solutions","volume":"99","author":"Annunziata","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb2395","doi-asserted-by":"crossref","first-page":"6277","DOI":"10.1073\/pnas.110000497","article-title":"Control of protein crystal nucleation around the metastable liquid\u2013liquid phase boundary","volume":"97","author":"Galkin","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.addr.2011.07.006_bb2400","first-page":"771","article-title":"The effects of glycols, aldehydes, and acrylamide on phase separation and opacification in the calf lens","volume":"19","author":"Clark","year":"1980","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2405","doi-asserted-by":"crossref","first-page":"2140","DOI":"10.1021\/j100368a074","article-title":"Liquid\u2013liquid phase separation of aqueous lysozyme solutions: effects of pH and salt identity","volume":"94","author":"Taratuta","year":"1990","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.addr.2011.07.006_bb2410","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1111\/j.1541-4337.2005.tb00072.x","article-title":"Influence of cosolvent systems on the gelation mechanism of globular protein: thermodynamic, kinetic, and structural aspects of globular protein gelation","volume":"4","author":"Baier","year":"2005","journal-title":"Compr. Rev. Food Sci. Food Saf."},{"key":"10.1016\/j.addr.2011.07.006_bb2415","doi-asserted-by":"crossref","first-page":"5046","DOI":"10.1021\/jf000272l","article-title":"Effects of sugars on whey protein isolate gelation","volume":"48","author":"Rich","year":"2000","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb2420","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1021\/js9801384","article-title":"Aggregation of recombinant human interferon gamma: kinetics and structural transitions","volume":"87","author":"Kendrick","year":"1998","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2425","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1038\/386259a0","article-title":"Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes","volume":"386","author":"Aggeli","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.addr.2011.07.006_bb2430","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1007\/s00249-008-0389-6","article-title":"Thermal aggregation and ion-induced cold-gelation of bovine serum albumin","volume":"38","author":"Navarra","year":"2009","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb2435","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1021\/jf950529t","article-title":"Interactions involved in the gelation of bovine serum albumin","volume":"44","author":"Boye","year":"1996","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb2440","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1111\/j.1399-3011.1981.tb02002.x","article-title":"Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels","volume":"17","author":"Clark","year":"1981","journal-title":"Int. J. Pept. Protein Res."},{"key":"10.1016\/j.addr.2011.07.006_bb2445","doi-asserted-by":"crossref","first-page":"1270","DOI":"10.1021\/jf00120a032","article-title":"Effects of various anions on the rheological and gelling behavior of soy proteins: thermodynamic observations","volume":"31","author":"Babajimopoulos","year":"1983","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb2450","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/S0268-005X(09)80193-8","article-title":"Effects of anions on thermally induced whey protein isolate gels","volume":"9","author":"Bowland","year":"1995","journal-title":"Food Hydrocolloids"},{"key":"10.1016\/j.addr.2011.07.006_bb2455","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1271\/bbb.70.615","article-title":"Effects of sugars on the cross-linking formation and phase separation of high-pressure induced gel of whey protein from bovine milk","volume":"70","author":"He","year":"2006","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.addr.2011.07.006_bb2460","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1126\/science.281.5375.389","article-title":"Reversible hydrogels from self-assembling artificial proteins","volume":"281","author":"Petka","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.addr.2011.07.006_bb2465","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/S1359-0294(00)00057-1","article-title":"Globular protein gelation","volume":"5","author":"Gosal","year":"2000","journal-title":"Curr. Opin. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2470","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/0001-8686(86)80012-4","article-title":"Adsorption of proteins from solution at the solid\u2013liquid interface","volume":"25","author":"Norde","year":"1986","journal-title":"Adv. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2475","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/0378-5173(92)90034-Y","article-title":"The adsorption of proteins to pharmaceutical container surfaces","volume":"86","author":"Burke","year":"1992","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb2480","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1002\/(SICI)1097-0290(19970620)54:6<503::AID-BIT1>3.0.CO;2-N","article-title":"Protein denaturation by combined effect of shear and air\u2013liquid interface","volume":"54","author":"Maa","year":"1997","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb2485","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1529\/biophysj.104.051797","article-title":"Protein structural perturbation and aggregation on homogeneous surfaces","volume":"88","author":"Sethuraman","year":"2005","journal-title":"Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb2490","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1021\/bp070462h","article-title":"Current perspectives on stability of protein drug products during formulation, fill and finish operations","volume":"24","author":"Rathore","year":"2008","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.addr.2011.07.006_bb2495","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.biotechadv.2007.01.006","article-title":"Immunogenicity of therapeutic proteins. Part 2: impact of container closures","volume":"25","author":"Sharma","year":"2007","journal-title":"Biotechnol. Adv."},{"key":"10.1016\/j.addr.2011.07.006_bb2500","first-page":"297","article-title":"Interfacial protein adsorption and inactivation","volume":"3","author":"Sadana","year":"1992","journal-title":"Bioseparation"},{"key":"10.1016\/j.addr.2011.07.006_bb2505","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1016\/S0141-0229(01)00340-4","article-title":"Lysozyme inactivation under mechanical stirring: effect of physical and molecular interfaces","volume":"28","author":"Colombie","year":"2001","journal-title":"Enzyme Microb. Technol."},{"key":"10.1016\/j.addr.2011.07.006_bb2510","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/S1389-1723(01)80127-4","article-title":"On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon","volume":"91","author":"Nakanishi","year":"2001","journal-title":"J. Biosci. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb2515","doi-asserted-by":"crossref","first-page":"3218","DOI":"10.1002\/jps.21768","article-title":"Monoclonal antibody interactions with micro- and nanoparticles: adsorption, aggregation, and accelerated stress studies","volume":"98","author":"Bee","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2520","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1016\/0021-9797(81)90342-8","article-title":"Adsorption of catalase on hydroxyapatite","volume":"83","author":"Bagchi","year":"1981","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2525","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1006\/jcis.1998.5759","article-title":"Adsorption of catalase on hydroxyapatite","volume":"208","author":"Barroug","year":"1998","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2530","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/0922-338X(95)98168-K","article-title":"Adsorption of protein onto stainless-steel surfaces","volume":"80","author":"Fukuzaki","year":"1995","journal-title":"J. Ferment. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb2535","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1016\/0021-9797(91)90282-D","article-title":"The effect of pH and sodium chloride concentration on adsorption of B-lactoglobulin at hydrophilic and hydrophobic silicon surfaces","volume":"143","author":"Luey","year":"1991","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2540","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/0927-7765(93)80031-S","article-title":"Study of the adsorption of F(ab')2 onto polystyrene latex beads","volume":"1","author":"Ortega Vinuesa","year":"1993","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"10.1016\/j.addr.2011.07.006_bb2545","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1007\/BF00658288","article-title":"On the adsorption of IgG onto polystyrene particles: electrophoretic mobility and critical coagulation concentration","volume":"270","author":"Serra","year":"1992","journal-title":"Colloid Polym. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2550","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1006\/jcis.1993.1227","article-title":"The adsorption from solutions of beta-lactoblobulin mixed with lactoferrin or lysozyme onto silica and methylated silica surfaces","volume":"158","author":"Wahlgren","year":"1993","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2555","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1021\/la950665s","article-title":"Changes in the secondary structure of adsorbed IgG and F(ab')2 studied by FTIR spectroscopy","volume":"12","author":"Buijs","year":"1996","journal-title":"Langmuir"},{"key":"10.1016\/j.addr.2011.07.006_bb2560","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1016\/0021-9797(92)90043-L","article-title":"Adsorption competition between albumin and monoclonal immunogammaglobulins on polystyrene latexes","volume":"152","author":"Elgersma","year":"1992","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2565","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1006\/jcis.1993.1091","article-title":"Interfacial free energies in protein solution droplets on FEP-teflon by axisymmetric drop shape analysis by profile-IgG versus BSA","volume":"156","author":"Van der Vegt","year":"1993","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2570","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.colsurfb.2009.08.015","article-title":"The role of electrolytes on protein adsorption at a hydrophilic solid\u2013water interface","volume":"75","author":"Wendorf","year":"2010","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"10.1016\/j.addr.2011.07.006_bb2575","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1021\/jp806586n","article-title":"Buffer effect on protein adsorption at liquid\/solid interface","volume":"113","author":"Wei","year":"2009","journal-title":"J. Phys. Chem. C"},{"key":"10.1016\/j.addr.2011.07.006_bb2580","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S1387-2656(02)08004-3","article-title":"Protein formulation and fill-finish operations","volume":"8","author":"Patro","year":"2002","journal-title":"Biotechnol. Annu. Rev."},{"key":"10.1016\/j.addr.2011.07.006_bb2585","series-title":"Therapeutic Protein and Peptide Formulation and Delivery","article-title":"Surfactant stabilized protein formulations: a review of protein\u2013surfactant interactions and novel analytical methodologies","author":"Jones","year":"1997"},{"key":"10.1016\/j.addr.2011.07.006_bb2590","series-title":"Surface Activity of Proteins: Chemical and Physicochemical Modifications","author":"Jones","year":"1996"},{"key":"10.1016\/j.addr.2011.07.006_bb2595","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/S0001-8686(00)00032-4","article-title":"Dynamics of protein and mixed protein\/surfactant adsorption layers at the water\/fluid interface","volume":"86","author":"Miller","year":"2000","journal-title":"Adv. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2600","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1002\/jps.20237","article-title":"Heterogeneous nucleation-controlled particulate formation of recombinant human platelet-activating factor acetylhydrolase in pharmaceutical formulation","volume":"94","author":"Chi","year":"2005","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2605","doi-asserted-by":"crossref","first-page":"1368","DOI":"10.1002\/jps.20365","article-title":"Effects of Tween 20 and Tween 80 on the stability of Albutropin during agitation","volume":"94","author":"Chou","year":"2005","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2610","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/0378-5173(94)00402-Q","article-title":"Influence of surfactants upon protein\/peptide adsorption to glass and polypropylene","volume":"120","author":"Duncan","year":"1995","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.addr.2011.07.006_bb2615","doi-asserted-by":"crossref","first-page":"4347","DOI":"10.1002\/jps.21328","article-title":"Shaken, not stirred: mechanical stress testing of an IgG1 antibody","volume":"97","author":"Kiese","year":"2008","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2620","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/j.ejpb.2004.12.004","article-title":"Induction and analysis of aggregates in a liquid IgG1-antibody formulation","volume":"59","author":"Mahler","year":"2005","journal-title":"Eur. J. Pharm. Biopharm."},{"key":"10.1016\/j.addr.2011.07.006_bb2625","doi-asserted-by":"crossref","first-page":"659","DOI":"10.3109\/10837450902911929","article-title":"Polysorbate 20 prevents the precipitation of a monoclonal antibody during shear","volume":"14","author":"Patapoff","year":"2009","journal-title":"Pharm. Dev. Technol."},{"key":"10.1016\/j.addr.2011.07.006_bb2630","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1007\/s00249-009-0404-6","article-title":"Insights into protein\u2013polysorbate interactions analysed by means of isothermal titration and differential scanning calorimetry","volume":"38","author":"Hoffmann","year":"2009","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.addr.2011.07.006_bb2635","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.bbapap.2005.08.001","article-title":"Analysis of protein\u2013surfactant interactions\u2014a titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant","volume":"1752","author":"Nielsen","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.addr.2011.07.006_bb2640","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.bpc.2009.04.004","article-title":"A thermodynamic analysis of the binding interaction between polysorbate 20 and 80 with human serum albumins and immunoglobulins: a contribution to understand colloidal protein stabilisation","volume":"143","author":"Garidel","year":"2009","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb2645","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1006\/jcis.1998.5941","article-title":"Orogenic displacement of protein from the air\/water interface by competitive adsorption","volume":"210","author":"Mackie","year":"1999","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2650","doi-asserted-by":"crossref","first-page":"984","DOI":"10.1021\/bm0344957","article-title":"Effect of surfactant type on surfactant\u2013protein interactions at the air\u2013water interface","volume":"5","author":"Gunning","year":"2004","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.addr.2011.07.006_bb2655","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1002\/bit.20132","article-title":"Reduced protein adsorption at solid interfaces by sugar excipients","volume":"87","author":"Wendorf","year":"2004","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.addr.2011.07.006_bb2660","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1002\/jps.21419","article-title":"IgG particle formation during filling pump operation: a case study of heterogeneous nucleation on stainless steel nanoparticles","volume":"98","author":"Tyagi","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2665","doi-asserted-by":"crossref","first-page":"3290","DOI":"10.1002\/jps.21707","article-title":"Precipitation of a monoclonal antibody by soluble tungsten","volume":"98","author":"Bee","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2670","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1006\/jcis.1997.4841","article-title":"Adsorption of a formulated protein on a drug delivery device surface","volume":"189","author":"Tzannis","year":"1997","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2675","doi-asserted-by":"crossref","first-page":"3167","DOI":"10.1002\/jps.21719","article-title":"Silicone oil- and agitation-induced aggregation of a monoclonal antibody in aqueous solution","volume":"98","author":"Thirumangalathu","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2680","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1002\/jps.20321","article-title":"Silicone oil induced aggregation of proteins","volume":"94","author":"Jones","year":"2005","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2685","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1038\/nrmicro1681","article-title":"The perfect mix: recent progress in adjuvant research","volume":"5","author":"Guy","year":"2007","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.addr.2011.07.006_bb2690","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1002\/jps.21523","article-title":"Vaccine adjuvants: current challenges and future approaches","volume":"98","author":"Wilson-Welder","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2695","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1007\/978-1-4615-1823-5_9","article-title":"Structure and properties of aluminum-containing adjuvants","volume":"6","author":"Hem","year":"1995","journal-title":"Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb2700","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0169-409X(98)00008-8","article-title":"Aluminum compounds as vaccine adjuvants","volume":"32","author":"Gupta","year":"1998","journal-title":"Adv. Drug Deliv. Rev."},{"issue":"Suppl. 3","key":"10.1016\/j.addr.2011.07.006_bb2705","doi-asserted-by":"crossref","first-page":"S34","DOI":"10.1016\/S0264-410X(02)00169-X","article-title":"Mechanisms of stimulation of the immune response by aluminum adjuvants","volume":"20","author":"Hogenesch","year":"2002","journal-title":"Vaccine"},{"key":"10.1016\/j.addr.2011.07.006_bb2710","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1007\/978-1-4615-1823-5_7","article-title":"A compendium of vaccine adjuvants and excipients","volume":"6","author":"Vogel","year":"1995","journal-title":"Pharm. Biotechnol."},{"key":"10.1016\/j.addr.2011.07.006_bb2715","doi-asserted-by":"crossref","first-page":"1993","DOI":"10.1016\/j.vaccine.2004.10.014","article-title":"Immunogenicity in mice of anthrax recombinant protective antigen in the presence of aluminum adjuvants","volume":"23","author":"Berthold","year":"2005","journal-title":"Vaccine"},{"key":"10.1016\/j.addr.2011.07.006_bb2720","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/j.vaccine.2006.09.039","article-title":"Potentiation of the immune response to non-adsorbed antigens by aluminum-containing adjuvants","volume":"25","author":"Romero Mendez","year":"2007","journal-title":"Vaccine"},{"key":"10.1016\/j.addr.2011.07.006_bb2725","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/0264-410X(95)80009-3","article-title":"Contribution of electrostatic and hydrophobic interactions to the adsorption of proteins by aluminium-containing adjuvants","volume":"13","author":"al-Shakhshir","year":"1995","journal-title":"Vaccine"},{"key":"10.1016\/j.addr.2011.07.006_bb2730","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1586\/14760584.6.5.685","article-title":"Relationship between physical and chemical properties of aluminum-containing adjuvants and immunopotentiation","volume":"6","author":"Hem","year":"2007","journal-title":"Expert Rev. Vaccines"},{"key":"10.1016\/j.addr.2011.07.006_bb2735","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1016\/j.vaccine.2003.10.023","article-title":"Mechanism of adsorption of hepatitis B surface antigen by aluminum hydroxide adjuvant","volume":"22","author":"Iyer","year":"2004","journal-title":"Vaccine"},{"key":"10.1016\/j.addr.2011.07.006_bb2740","doi-asserted-by":"crossref","first-page":"1502","DOI":"10.1016\/j.vaccine.2004.08.048","article-title":"Effect of phosphorylation of ovalbumin on adsorption by aluminum-containing adjuvants and elution upon exposure to interstitial fluid","volume":"23","author":"Morefield","year":"2005","journal-title":"Vaccine"},{"key":"10.1016\/j.addr.2011.07.006_bb2745","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/0264-410X(91)90154-X","article-title":"Predicting the adsorption of proteins by aluminium-containing adjuvants","volume":"9","author":"Seeber","year":"1991","journal-title":"Vaccine"},{"key":"10.1016\/j.addr.2011.07.006_bb2750","doi-asserted-by":"crossref","first-page":"13406","DOI":"10.1074\/jbc.M500687200","article-title":"Effects of adsorption to aluminum salt adjuvants on the structure and stability of model protein antigens","volume":"280","author":"Jones","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.addr.2011.07.006_bb2755","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0378-4347(98)00425-3","article-title":"Evidence for the denaturation of recombinant hepatitis B surface antigen on aluminium hydroxide gel","volume":"720","author":"Tleugabulova","year":"1998","journal-title":"J. Chromatogr. B Biomed. Sci. Appl."},{"key":"10.1016\/j.addr.2011.07.006_bb2760","doi-asserted-by":"crossref","first-page":"2970","DOI":"10.1002\/jps.21498","article-title":"Stability of a trivalent recombinant protein vaccine formulation against botulinum neurotoxin during storage in aqueous solution","volume":"98","author":"Vessely","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2765","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1002\/jps.22282","article-title":"Application of extrinsic fluorescence spectroscopy for the high throughput formulation screening of aluminum-adjuvanted vaccines","volume":"100","author":"Ausar","year":"2011","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2770","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1002\/jps.20675","article-title":"A rapid, three-step process for the preformulation of a recombinant ricin toxin A-chain vaccine","volume":"96","author":"Peek","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2775","doi-asserted-by":"crossref","first-page":"4194","DOI":"10.1002\/jps.21300","article-title":"Preformulation studies of Clostridium difficile toxoids A and B","volume":"97","author":"Salnikova","year":"2008","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.addr.2011.07.006_bb2780","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.ijbiomac.2009.04.008","article-title":"Effects of immobilization onto aluminum hydroxide particles on the thermally induced conformational behavior of three model proteins","volume":"45","author":"Bai","year":"2009","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.addr.2011.07.006_bb2785","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/j.ab.2006.01.008","article-title":"Secondary structures of proteins adsorbed onto aluminum hydroxide: infrared spectroscopic analysis of proteins from low solution concentrations","volume":"351","author":"Dong","year":"2006","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.addr.2011.07.006_bb2790","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1016\/j.vaccine.2003.09.037","article-title":"Effect of microenvironment pH of aluminum hydroxide adjuvant on the chemical stability of adsorbed antigen","volume":"22","author":"Wittayanukulluk","year":"2004","journal-title":"Vaccine"},{"key":"10.1016\/j.addr.2011.07.006_bb2795","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1002\/jps.22284","article-title":"Vaccines with aluminum-containing adjuvants: optimizing vaccine efficacy and thermal stability","volume":"100","author":"Clapp","year":"2011","journal-title":"J. Pharm. Sci."}],"container-title":["Advanced Drug Delivery Reviews"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0169409X11002006?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0169409X11002006?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,4,9]],"date-time":"2024-04-09T09:59:56Z","timestamp":1712656796000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0169409X11002006"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,10]]},"references-count":558,"journal-issue":{"issue":"13","published-print":{"date-parts":[[2011,10]]}},"alternative-id":["S0169409X11002006"],"URL":"https:\/\/doi.org\/10.1016\/j.addr.2011.07.006","relation":{},"ISSN":["0169-409X"],"issn-type":[{"value":"0169-409X","type":"print"}],"subject":[],"published":{"date-parts":[[2011,10]]}}}