{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T12:16:50Z","timestamp":1777465010354,"version":"3.51.4"},"reference-count":39,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,8,1]],"date-time":"2018-08-01T00:00:00Z","timestamp":1533081600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,8,1]],"date-time":"2018-08-01T00:00:00Z","timestamp":1533081600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2019,6,19]],"date-time":"2019-06-19T00:00:00Z","timestamp":1560902400000},"content-version":"am","delay-in-days":322,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["MCB-1157506"],"award-info":[{"award-number":["MCB-1157506"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"Intramural Research Program of the Vaccine Research Center, NIAID, National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Analytical Biochemistry"],"published-print":{"date-parts":[[2018,8]]},"DOI":"10.1016\/j.ab.2018.05.008","type":"journal-article","created":{"date-parts":[[2018,5,8]],"date-time":"2018-05-08T12:30:30Z","timestamp":1525782630000},"page":"61-69","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"special_numbering":"C","title":["Long term stability of a HIV-1 neutralizing monoclonal antibody using isothermal calorimetry"],"prefix":"10.1016","volume":"554","author":[{"given":"Benjamin R.","family":"Clarkson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rajoshi","family":"Chaudhuri","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Arne","family":"Sch\u00f6n","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jonathan W.","family":"Cooper","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lisa","family":"Kueltzo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2335-6419","authenticated-orcid":false,"given":"Ernesto","family":"Freire","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.ab.2018.05.008_bib1","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1126\/science.1187659","article-title":"Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1","volume":"329","author":"Wu","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.ab.2018.05.008_bib2","doi-asserted-by":"crossref","first-page":"12669","DOI":"10.1128\/JVI.02213-14","article-title":"Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo","volume":"88","author":"Rudicell","year":"2014","journal-title":"J. Virol."},{"key":"10.1016\/j.ab.2018.05.008_bib3","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. Pharmacol. Sci."},{"key":"10.1016\/j.ab.2018.05.008_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/jps.20727","article-title":"Antibody structure, instability, and formulation","volume":"96","author":"Wang","year":"2007","journal-title":"J. Pharmaceut. Sci."},{"key":"10.1016\/j.ab.2018.05.008_bib5","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1208\/s12248-013-9539-6","article-title":"High-throughput biophysical analysis of protein therapeutics to examine interrelationships between aggregate formation and conformational stability","volume":"16","author":"Chaudhuri","year":"2014","journal-title":"AAPS J."},{"key":"10.1016\/j.ab.2018.05.008_bib6","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. Pharmacol. Sci."},{"key":"10.1016\/j.ab.2018.05.008_bib7","doi-asserted-by":"crossref","first-page":"2307","DOI":"10.1002\/jps.23150","article-title":"Accelerated stability studies of abatacept formulations: comparison of freeze-thawing- and agitation-induced stresses","volume":"101","author":"Cordes","year":"2012","journal-title":"J. Pharmacol. Sci."},{"key":"10.1016\/j.ab.2018.05.008_bib8","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1002\/jps.22812","article-title":"Forced degradation of therapeutic proteins","volume":"101","author":"Hawe","year":"2012","journal-title":"J. Pharmacol. Sci."},{"key":"10.1016\/j.ab.2018.05.008_bib9","doi-asserted-by":"crossref","first-page":"2520","DOI":"10.1002\/jps.23645","article-title":"Effect of ionic strength and pH on the physical and chemical stability of a monoclonal antibody antigen-binding fragment","volume":"102","author":"Wang","year":"2013","journal-title":"J. Pharmacol. Sci."},{"key":"10.1016\/j.ab.2018.05.008_bib10","doi-asserted-by":"crossref","first-page":"1246","DOI":"10.1002\/jps.21521","article-title":"Principles, approaches, and challenges for predicting protein aggregation rates and shelf life","volume":"98","author":"Weiss","year":"2009","journal-title":"J. Pharmacol. Sci."},{"key":"10.1016\/j.ab.2018.05.008_bib11","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1146\/annurev.bb.19.060190.001111","article-title":"Calorimetrically determined dynamics of complex unfolding transitions in proteins","volume":"19","author":"Freire","year":"1990","journal-title":"Annu. Rev. Biophys. Biophys. Chem."},{"key":"10.1016\/j.ab.2018.05.008_bib12","doi-asserted-by":"crossref","first-page":"1648","DOI":"10.1021\/bi00405a039","article-title":"Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin","volume":"27","author":"Sanchez-Ruiz","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/j.ab.2018.05.008_bib13","doi-asserted-by":"crossref","first-page":"2009","DOI":"10.1002\/prot.25354","article-title":"Temperature stability of proteins: Analysis of irreversible denaturation using isothermal calorimetry","volume":"85","author":"Sch\u00f6n","year":"2017","journal-title":"Proteins Struct. Funct. Bioinf."},{"key":"10.1016\/j.ab.2018.05.008_bib14","series-title":"Analysis of Long Term Stability of Biologics by Isothermal Calorimetry","author":"Sch\u00f6n","year":"2017"},{"key":"10.1016\/j.ab.2018.05.008_bib15","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0153495","article-title":"Kinetics of thermal denaturation and aggregation of bovine serum albumin","volume":"11","author":"Borzova","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.ab.2018.05.008_bib16","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/0076-6879(86)31033-4","article-title":"Scanning microcalorimetry in studying temperature-induced changes in proteins","volume":"131","author":"Privalov","year":"1986","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.ab.2018.05.008_bib17","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.1002\/jps.21104","article-title":"Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies","volume":"97","author":"Ionescu","year":"2008","journal-title":"J. Pharmacol. Sci."},{"key":"10.1016\/j.ab.2018.05.008_bib18","series-title":"Effect of Carbohydrate on Thermal Stability of Antibodies","author":"Wen","year":"2008"},{"key":"10.1016\/j.ab.2018.05.008_bib19","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1002\/jps.22820","article-title":"Applications of differential scanning calorimetry for thermal stability analysis of proteins: qualification of DSC","volume":"101","author":"Wen","year":"2012","journal-title":"J. Pharmacol. Sci."},{"key":"10.1016\/j.ab.2018.05.008_bib20","doi-asserted-by":"crossref","first-page":"9616","DOI":"10.1021\/bi9703305","article-title":"Are there equilibrium intermediate states in the urea-induced unfolding of hen egg-white lysozyme?","volume":"36","author":"Ibarra-Molero","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.ab.2018.05.008_bib21","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/S0301-4622(97)80552-2","article-title":"Analysis of differential scanning calorimetry data for proteins. Criteria of validity of one-step mechanism of irreversible protein denaturation","volume":"69","author":"Kurganov","year":"1997","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.ab.2018.05.008_bib22","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1016\/S0006-3495(92)81899-4","article-title":"Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry","volume":"61","author":"Sanchez-Ruiz","year":"1992","journal-title":"Biophys. J."},{"key":"10.1016\/j.ab.2018.05.008_bib23","doi-asserted-by":"crossref","first-page":"42","DOI":"10.4161\/mabs.2.1.10787","article-title":"Cold denaturation of monoclonal antibodies","volume":"2","author":"Lazar","year":"2010","journal-title":"mAbs"},{"key":"10.1016\/j.ab.2018.05.008_bib24","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1021\/cr960383c","article-title":"Protein structure and the energetics of protein stability","volume":"97","author":"Robertson","year":"1997","journal-title":"Chem. Rev."},{"key":"10.1016\/j.ab.2018.05.008_bib25","first-page":"17","article-title":"Protein stabilization by naturally occurring osmolytes","volume":"168","author":"Bolen","year":"2001","journal-title":"Meth. Mol. Biol."},{"key":"10.1016\/j.ab.2018.05.008_bib26","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1016\/j.addr.2011.06.011","article-title":"Interactions of formulation excipients with proteins in solution and in the dried state","volume":"63","author":"Ohtake","year":"2011","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.ab.2018.05.008_bib27","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.ab.2018.05.008_bib28","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.ejpb.2011.03.004","article-title":"Development of high concentration protein biopharmaceuticals: the use of platform approaches in formulation development","volume":"78","author":"Warne","year":"2011","journal-title":"Eur. J. Pharm. Biopharm."},{"key":"10.1016\/j.ab.2018.05.008_bib29","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1016\/j.addr.2011.07.006","article-title":"Protein-excipient interactions: mechanisms and biophysical characterization applied to protein formulation development","volume":"63","author":"Kamerzell","year":"2011","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.ab.2018.05.008_bib30","first-page":"191","article-title":"Differential scanning calorimetry","volume":"40","author":"Freire","year":"1995","journal-title":"Meth. Mol. Biol."},{"key":"10.1016\/j.ab.2018.05.008_bib31","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1002\/bip.1978.360170212","article-title":"Statistical mechanical deconvolution of thermal transitions in macromolecules. I. Theory and application to homogeneous systems","volume":"17","author":"Freire","year":"1978","journal-title":"Biopolymers"},{"key":"10.1016\/j.ab.2018.05.008_bib32","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/S0022-2836(05)80197-4","article-title":"Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect","volume":"213","author":"Makhatadze","year":"1990","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ab.2018.05.008_bib33","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/S0065-3233(08)60556-2","article-title":"Thermodynamics of structural stability and cooperative folding behavior in proteins","volume":"43","author":"Murphy","year":"1992","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.ab.2018.05.008_bib34","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/0022-2836(91)90506-2","article-title":"Solid model compounds and the thermodynamics of protein unfolding","volume":"222","author":"Murphy","year":"1991","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ab.2018.05.008_bib35","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/S0022-2836(05)80198-6","article-title":"Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects","volume":"213","author":"Privalov","year":"1990","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ab.2018.05.008_bib36","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1016\/0022-2836(89)90318-5","article-title":"Heat capacity and conformation of proteins in the denatured state","volume":"205","author":"Privalov","year":"1989","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ab.2018.05.008_bib37","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1021\/mp400666b","article-title":"Examination of thermal unfolding and aggregation profiles of a series of developable therapeutic monoclonal antibodies","volume":"12","author":"Brader","year":"2015","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.ab.2018.05.008_bib38","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.ab.2013.02.014","article-title":"Monitoring protein aggregation kinetics with simultaneous multiple sample light scattering","volume":"437","author":"Drenski","year":"2013","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.ab.2018.05.008_bib39","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1208\/s12248-013-9485-3","article-title":"Non-Arrhenius protein aggregation","volume":"15","author":"Wang","year":"2013","journal-title":"AAPS J."}],"container-title":["Analytical Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003269718302744?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003269718302744?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,12]],"date-time":"2025-09-12T21:23:11Z","timestamp":1757712191000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003269718302744"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,8]]},"references-count":39,"alternative-id":["S0003269718302744"],"URL":"https:\/\/doi.org\/10.1016\/j.ab.2018.05.008","relation":{},"ISSN":["0003-2697"],"issn-type":[{"value":"0003-2697","type":"print"}],"subject":[],"published":{"date-parts":[[2018,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Long term stability of a HIV-1 neutralizing monoclonal antibody using isothermal calorimetry","name":"articletitle","label":"Article Title"},{"value":"Analytical Biochemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ab.2018.05.008","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}