{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T04:11:03Z","timestamp":1772770263923,"version":"3.50.1"},"reference-count":65,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2014,2,1]],"date-time":"2014-02-01T00:00:00Z","timestamp":1391212800000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"name":"National Key Basic Research and Development (973) Program of China","award":["2010CB912402"],"award-info":[{"award-number":["2010CB912402"]}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"crossref","award":["30970559"],"award-info":[{"award-number":["30970559"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"published-print":{"date-parts":[[2013,2]]},"DOI":"10.1016\/j.bbadis.2012.11.005","type":"journal-article","created":{"date-parts":[[2012,11,15]],"date-time":"2012-11-15T11:31:10Z","timestamp":1352979070000},"page":"302-311","source":"Crossref","is-referenced-by-count":25,"title":["Increasing \u03b2B1-crystallin sensitivity to proteolysis caused by the congenital cataract-microcornea syndrome mutation S129R"],"prefix":"10.1016","volume":"1832","author":[{"given":"Sha","family":"Wang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wei-Jie","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Huihui","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Haipeng","family":"Gong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yong-Bin","family":"Yan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbadis.2012.11.005_bb0005","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1364\/AO.10.000459","article-title":"Theory of transparency of the eye","volume":"10","author":"Benedek","year":"1971","journal-title":"Appl. Opt."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0010","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1152\/physrev.1997.77.1.21","article-title":"Physiological properties of the normal lens","volume":"77","author":"Mathias","year":"1997","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0015","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/exer.2001.1111","article-title":"Lens organelle degradation","volume":"74","author":"Bassnett","year":"2002","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0020","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.preteyeres.2005.10.001","article-title":"The lens of the eye as a focusing device and its response to stress","volume":"25","author":"Banh","year":"2006","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0025","doi-asserted-by":"crossref","first-page":"1754","DOI":"10.1016\/j.biocel.2007.06.021","article-title":"Lens cells: more than meets the eye","volume":"39","author":"Tholozan","year":"2007","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0030","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.preteyeres.2006.10.003","article-title":"Crystallins in the eye: function and pathology","volume":"26","author":"Andley","year":"2007","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0035","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.exer.2008.10.011","article-title":"Genetics of crystallins: cataract and beyond","volume":"88","author":"Graw","year":"2009","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0040","doi-asserted-by":"crossref","first-page":"10449","DOI":"10.1073\/pnas.89.21.10449","article-title":"\u03b1-Crystallin can function as a molecular chaperone","volume":"89","author":"Horwitz","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0045","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/j.pbiomolbio.2003.11.012","article-title":"Ageing and vision: structure, stability and function of lens crystallins","volume":"86","author":"Bloemendal","year":"2004","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0050","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.molmed.2012.03.005","article-title":"Protein misfolding and aggregation in cataract disease and prospects for prevention","volume":"18","author":"Moreau","year":"2012","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0055","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1038\/sj.eye.6701964","article-title":"External factors in the development of cataract","volume":"19","author":"Robman","year":"2005","journal-title":"Eye (Lond.)"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0060","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1016\/j.bbagen.2009.05.008","article-title":"Lens aging: effects of crystallins","volume":"1790","author":"Sharma","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0065","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/S1350-9462(98)00018-4","article-title":"Cataract mutations and lens development","volume":"18","author":"Graw","year":"1999","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0070","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1001\/archopht.125.2.165","article-title":"Genetic origins of cataract","volume":"125","author":"Shiels","year":"2007","journal-title":"Arch. Ophthalmol."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0075","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1073\/pnas.1014653107","article-title":"Cataract-associated mutant E107A of human \u03b3D-crystallin shows increased attraction to \u03b1-crystallin and enhanced light scattering","volume":"108","author":"Banerjee","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0080","doi-asserted-by":"crossref","first-page":"e20564","DOI":"10.1371\/journal.pone.0020564","article-title":"The congenital cataract-linked G61C mutation destabilizes \u03b3D-crystallin and promotes non-native aggregation","volume":"6","author":"Zhang","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0085","first-page":"476","article-title":"Identification of crystallin modifications in the human lens cortex and nucleus using laser capture microdissection and CyDye labeling","volume":"16","author":"Asomugha","year":"2010","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0090","doi-asserted-by":"crossref","first-page":"3107","DOI":"10.1167\/iovs.09-4308","article-title":"Age-dependent deamidation of lifelong proteins in the human lens","volume":"51","author":"Hains","year":"2010","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0095","doi-asserted-by":"crossref","first-page":"8477","DOI":"10.1074\/jbc.M705876200","article-title":"Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation","volume":"283","author":"Santhoshkumar","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0100","doi-asserted-by":"crossref","first-page":"39136","DOI":"10.1074\/jbc.M204684200","article-title":"Identification and properties of anti-chaperone-like peptides derived from oxidized bovine lens \u03b2L-crystallins","volume":"277","author":"Senthilkumar","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0105","first-page":"666","article-title":"Anti-chaperone \u03b2A3\/A1102-117 peptide interacting sites in human \u03b1B-crystallin","volume":"14","author":"Rao","year":"2008","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0110","doi-asserted-by":"crossref","first-page":"5942","DOI":"10.1111\/j.1742-4658.2005.05024.x","article-title":"Aspects on human amyloid forms and their fibril polypeptides","volume":"272","author":"Westermark","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0115","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.2353\/ajpath.2007.061232","article-title":"Calpain-cleavage of alpha-synuclein: connecting proteolytic processing to disease-linked aggregation","volume":"170","author":"Dufty","year":"2007","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0120","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1152\/physrev.00023.2009","article-title":"Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process","volume":"90","author":"De Strooper","year":"2010","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0125","doi-asserted-by":"crossref","first-page":"E2050","DOI":"10.1002\/humu.21436","article-title":"A novel mutation in CRYBB1 associated with congenital cataract-microcornea syndrome: the p.Ser129Arg mutation destabilizes the \u03b2B1\/\u03b2A3-crystallin heteromer but not the \u03b2B1-crystallin homomer","volume":"32","author":"Wang","year":"2011","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0130","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1111\/j.1432-1033.1989.tb14892.x","article-title":"Crystallin gene expression during rat lens development","volume":"183","author":"Aarts","year":"1989","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0135","doi-asserted-by":"crossref","first-page":"11250","DOI":"10.1074\/jbc.272.17.11250","article-title":"Size of human lens \u03b2-crystallin aggregates are distinguished by N-terminal truncation of \u03b2B1","volume":"272","author":"Ajaz","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0140","first-page":"2242","article-title":"A serine-type protease activity of human lens betaA3-crystallin is responsible for its autodegradation","volume":"16","author":"Gupta","year":"2010","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0145","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1242\/jcs.078790","article-title":"Mutation in the \u03b2A3\/A1-crystallin gene impairs phagosome degradation in the retinal pigmented epithelium of the rat","volume":"124","author":"Zigler","year":"2011","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0150","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0155","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/0014-5793(76)80003-8","article-title":"Ultra-violet fluorescence of actin. Determination of native actin content in actin preparations","volume":"62","author":"Turoverov","year":"1976","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0160","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1126\/science.7638615","article-title":"Resonance light scattering: a new technique for studying chromophore aggregation","volume":"269","author":"Pasternack","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0165","doi-asserted-by":"crossref","first-page":"2849","DOI":"10.1111\/j.1742-4658.2009.07008.x","article-title":"Conformational stability and multistate unfolding of poly(A)-specific ribonuclease","volume":"276","author":"He","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0170","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.bbapap.2007.12.001","article-title":"Multistate folding of a hyperthermostable Fe-superoxide dismutase (TcSOD) in guanidinium hydrochloride: the importance of the quaternary structure","volume":"1784","author":"Wang","year":"2008","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0175","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/0003-2697(79)90732-2","article-title":"A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels","volume":"98","author":"Switzer","year":"1979","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0180","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1016\/S0021-9258(19)75212-0","article-title":"Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis","volume":"252","author":"Cleveland","year":"1977","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0185","doi-asserted-by":"crossref","first-page":"10727","DOI":"10.1021\/bi00091a025","article-title":"Limited proteolysis of creatine kinase. Implications for three-dimensional structure and for conformational substrates","volume":"32","author":"Wyss","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0190","doi-asserted-by":"crossref","first-page":"29511","DOI":"10.1074\/jbc.272.47.29511","article-title":"Subunit exchange of \u03b1A-crystallin","volume":"272","author":"Bova","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0195","doi-asserted-by":"crossref","first-page":"7179","DOI":"10.1021\/bi900313c","article-title":"Truncated human \u03b2B1-crystallin shows altered structural properties and interaction with human \u03b2A3-crystallin","volume":"48","author":"Srivastava","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0200","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1023\/A:1015277805345","article-title":"Kinetics of protein aggregation. Quantitative estimation of the chaperone-like activity in test-systems based on suppression of protein aggregation","volume":"67","author":"Kurganov","year":"2002","journal-title":"Biochemistry (Moscow)"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0205","doi-asserted-by":"crossref","first-page":"2901","DOI":"10.3390\/ijms12052901","article-title":"Dissimilar roles of the four conserved acidic residues in the thermal stability of poly(A)-specific ribonuclease","volume":"12","author":"He","year":"2011","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0210","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1038\/nprot.2006.4","article-title":"Tricine-SDS-PAGE","volume":"1","author":"Schagger","year":"2006","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0215","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1038\/nprot.2006.62","article-title":"Blue native PAGE","volume":"1","author":"Wittig","year":"2006","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0220","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/jcc.20289","article-title":"Scalable molecular dynamics with NAMD","volume":"26","author":"Phillips","year":"2005","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0225","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1016\/j.bpj.2012.07.002","article-title":"Chaperone-like effect of the linker on the isolated C-terminal domain of rabbit muscle creatine kinase","volume":"103","author":"Chen","year":"2012","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0230","doi-asserted-by":"crossref","first-page":"2606","DOI":"10.1110\/ps.03265903","article-title":"Crystal structure of truncated human \u03b2B1-crystallin","volume":"12","author":"van Montfort","year":"2003","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0235","doi-asserted-by":"crossref","first-page":"5221","DOI":"10.1021\/ja003834q","article-title":"Use of MM-PBSA in reproducing the binding free energies to HIV-1 RT of TIBO derivatives and predicting the binding mode to HIV-1 RT of efavirenz by docking and MM-PBSA","volume":"123","author":"Wang","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0240","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/S0167-4838(97)00175-1","article-title":"The structural aspects of limited proteolysis of native proteins","volume":"1382","author":"Hubbard","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0245","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/S0014-4835(03)00173-8","article-title":"The stability of human acidic \u03b2-crystallin oligomers and hetero-oligomers","volume":"77","author":"Bateman","year":"2003","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0250","doi-asserted-by":"crossref","first-page":"11062","DOI":"10.1021\/bi8012438","article-title":"Association properties of \u03b2B1- and \u03b2A3-crystallins: ability to form heterotetramers","volume":"47","author":"Chan","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0255","doi-asserted-by":"crossref","first-page":"9684","DOI":"10.1021\/bi9013984","article-title":"N-terminal extension of \u03b2B1-crystallin: identification of a critical region that modulates protein interaction with \u03b2A3-crystallin","volume":"48","author":"Dolinska","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0260","doi-asserted-by":"crossref","first-page":"10451","DOI":"10.1021\/bi201375p","article-title":"The benefits of being \u03b2-crystallin heteromers: \u03b2B1-crystallin protects \u03b2A3-crystallin against aggregation during co-refolding","volume":"50","author":"Wang","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0265","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1110\/ps.0225503","article-title":"In vitro unfolding, refolding, and polymerization of human \u03b3D crystallin, a protein involved in cataract formation","volume":"12","author":"Kosinski-Collins","year":"2003","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0270","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1016\/j.biocel.2006.09.004","article-title":"Effects of the single point genetic mutation D54G on muscle creatine kinase activity, structure and stability","volume":"39","author":"Feng","year":"2007","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0275","first-page":"438","article-title":"Decreasing the homodimer interaction: a common mechanism shared by the \u0394G91 mutation and deamidation in \u03b2A3-crystallin","volume":"16","author":"Xu","year":"2010","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0280","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/0304-4165(84)90313-1","article-title":"Limited proteolysis of bovine lens \u03b1-crystallin by calpain, a Ca2+-dependent cysteine proteinase, isolated from the same tissue","volume":"798","author":"Yoshida","year":"1984","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2012.11.005_bb0285","doi-asserted-by":"crossref","first-page":"13760","DOI":"10.1016\/S0021-9258(18)67085-1","article-title":"The eye lens has an active ubiquitin\u2013protein conjugation system","volume":"261","author":"Jahngen","year":"1986","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0290","first-page":"785","article-title":"Cataract and the acceleration of calpain-induced beta-crystallin insolubilization occurring during normal maturation of rat lens","volume":"35","author":"David","year":"1994","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0295","doi-asserted-by":"crossref","first-page":"363","DOI":"10.3109\/02713689608995826","article-title":"Peptide hydrolysis in lens: role of leucine aminopeptidase, aminopeptidase III, prolyloligopeptidase and acylpeptidehydrolase","volume":"15","author":"Sharma","year":"1996","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0300","first-page":"194","article-title":"Role of calcium-dependent protease(s) in globulization of isolated rat lens cortical fiber cells","volume":"42","author":"Wang","year":"2001","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0305","doi-asserted-by":"crossref","first-page":"13542","DOI":"10.1074\/jbc.M900561200","article-title":"Calpain expression and activity during lens fiber cell differentiation","volume":"284","author":"De Maria","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0310","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1016\/S0022-2836(03)00368-1","article-title":"Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease","volume":"328","author":"Ferrao-Gonzales","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0315","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1016\/j.jmb.2005.06.046","article-title":"Solvational tuning of the unfolding, aggregation and amyloidogenesis of insulin","volume":"351","author":"Grudzielanek","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0320","doi-asserted-by":"crossref","first-page":"650","DOI":"10.2174\/092986608785133645","article-title":"Oligomerization and aggregation of bovine pancreatic ribonuclease A: backbone hydration probed by infrared band-shift","volume":"15","author":"Zhang","year":"2008","journal-title":"Protein Pept. Lett."},{"key":"10.1016\/j.bbadis.2012.11.005_bb0325","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1021\/jp809817s","article-title":"Effect of dehydration on the aggregation kinetics of two amyloid peptides","volume":"113","author":"Mukherjee","year":"2009","journal-title":"J. Phys. Chem. B"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443912002566?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443912002566?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,1,31]],"date-time":"2022-01-31T10:11:07Z","timestamp":1643623867000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0925443912002566"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,2]]},"references-count":65,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2013,2]]}},"alternative-id":["S0925443912002566"],"URL":"https:\/\/doi.org\/10.1016\/j.bbadis.2012.11.005","relation":{},"ISSN":["0925-4439"],"issn-type":[{"value":"0925-4439","type":"print"}],"subject":[],"published":{"date-parts":[[2013,2]]}}}