{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T11:41:05Z","timestamp":1789990865597,"version":"4.0.1"},"reference-count":78,"publisher":"Public Library of Science (PLoS)","issue":"11","license":[{"start":{"date-parts":[[2014,11,12]],"date-time":"2014-11-12T00:00:00Z","timestamp":1415750400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0112309","type":"journal-article","created":{"date-parts":[[2014,11,12]],"date-time":"2014-11-12T19:07:08Z","timestamp":1415819228000},"page":"e112309","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":38,"title":["Comparative Analysis of Human \u03b3D-Crystallin Aggregation under Physiological and Low pH Conditions"],"prefix":"10.1371","volume":"9","author":[{"given":"Josephine W.","family":"Wu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mei-Er","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wen-Sing","family":"Wen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wei-An","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chien-Ting","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chih-Kai","family":"Chang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chun-Hsien","family":"Lo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hwai-Shen","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven S.-S.","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2014,11,12]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0968-0004(99)01445-0","article-title":"Protein misfolding, evolution and disease","volume":"24","author":"CM Dobson","year":"1999","journal-title":"Trends Biochem Sci"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"R9","DOI":"10.1016\/S1359-0278(98)00002-9","article-title":"Protein aggregation: folding aggregates, inclusion bodies and amyloid","volume":"3","author":"AL Fink","year":"1998","journal-title":"Fold Des"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"11937","DOI":"10.1073\/pnas.0904191106","article-title":"Design of therapeutic proteins with enhanced stability","volume":"106","author":"N Chennamsetty","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"F Chiti","year":"2006","journal-title":"Annu Rev Biochem"},{"key":"ref5","unstructured":"Organization WH (2011) Visual impairment and blindness report. Fact Sheet N 282: WHO."},{"key":"ref6","first-page":"8","article-title":"Selenite nuclear cataract: review of the model","volume":"3","author":"TR Shearer","year":"1997","journal-title":"Mol Vis"},{"key":"ref7","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":"P Santhoshkumar","year":"2008","journal-title":"J Biol Chem"},{"key":"ref8","unstructured":"Oyster CW (1999) The human eye structure and function: Sinauer Associates, Inc."},{"key":"ref9","doi-asserted-by":"crossref","first-page":"10449","DOI":"10.1073\/pnas.89.21.10449","article-title":"Alpha-crystallin can function as a molecular chaperone","volume":"89","author":"J Horwitz","year":"1992","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1074\/jbc.M308203200","article-title":"Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation","volume":"279","author":"S Meehan","year":"2004","journal-title":"J Biol Chem"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1006\/exer.2000.0868","article-title":"The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage","volume":"71","author":"SR Hanson","year":"2000","journal-title":"Exp Eye Res"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1006\/exer.1996.0149","article-title":"Increase in the intramolecular disulfide bonding of alpha-A crystallin during aging of the human lens","volume":"63","author":"L Takemoto","year":"1996","journal-title":"Exp Eye Res"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1016\/j.exer.2004.12.007","article-title":"Age-related nuclear cataract-oxidation is the key","volume":"80","author":"RJ Truscott","year":"2005","journal-title":"Exp Eye Res"},{"key":"ref14","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":"PG Hains","year":"2010","journal-title":"Invest Ophthalmol Vis Sci"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.molmed.2003.12.007","article-title":"Calpains: targets of cataract prevention?","volume":"10","author":"S Biswas","year":"2004","journal-title":"Trends Mol Med"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/0097-8485(95)00028-Q","article-title":"Protein folds and functional similarity; the Greek key\/immunoglobulin fold","volume":"19","author":"MJ Crabbe","year":"1995","journal-title":"Comput Chem"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1110\/ps.0225503","article-title":"In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation","volume":"12","author":"MS Kosinski-Collins","year":"2003","journal-title":"Protein Sci"},{"key":"ref18","first-page":"81","article-title":"Formation of amyloid fibrils in vitro by human gammaD-crystallin and its isolated domains","volume":"14","author":"K Papanikolopoulou","year":"2008","journal-title":"Mol Vis"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"3329","DOI":"10.1073\/pnas.1117704109","article-title":"Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human gammaD-crystallin amyloid fibrils","volume":"109","author":"SD Moran","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1007\/s00424-001-0760-2","article-title":"pH gating of lens fibre connexins","volume":"443","author":"R Eckert","year":"2002","journal-title":"Pflugers Arch"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"39532","DOI":"10.1074\/jbc.M204855200","article-title":"Mildly acidic pH activates the extracellular molecular chaperone clusterin","volume":"277","author":"S Poon","year":"2002","journal-title":"J Biol Chem"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.jtice.2010.10.002","article-title":"High-level expression and purification of human gamma D-crystallin in Escherichia coli","volume":"42","author":"WS Wen","year":"2011","journal-title":"Journal of the Taiwan Institute of Chemical Engineers"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1110\/ps.04627004","article-title":"Probing folding and fluorescence quenching in human gammaD crystallin Greek key domains using triple tryptophan mutant proteins","volume":"13","author":"MS Kosinski-Collins","year":"2004","journal-title":"Protein Sci"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"1993","DOI":"10.1073\/pnas.040554397","article-title":"Molecular basis of a progressive juvenile-onset hereditary cataract","volume":"97","author":"A Pande","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1167\/iovs.09-3987","article-title":"Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin","volume":"51","author":"Y Wang","year":"2010","journal-title":"Invest Ophthalmol Vis Sci"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/0003-2697(85)90442-7","article-title":"Measurement of protein using bicinchoninic acid","volume":"150","author":"PK Smith","year":"1985","journal-title":"Anal Biochem"},{"key":"ref27","first-page":"2777","article-title":"Examining the influence of ultraviolet C irradiation on recombinant human gammaD-crystallin","volume":"16","author":"SS Wang","year":"2010","journal-title":"Mol Vis"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1111\/j.1751-1097.1996.tb02469.x","article-title":"Effect of the UV modification of alpha-crystallin on its ability to suppress nonspecific aggregation","volume":"64","author":"AR Ellozy","year":"1996","journal-title":"Photochemistry and Photobiology"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.bbrc.2006.03.024","article-title":"Mechanism of thioflavin T accumulation inside cells overexpressing P-glycoprotein or multidrug resistance-associated protein: Role of lipophilicity and positive charge","volume":"343","author":"N Darghal","year":"2006","journal-title":"Biochemical and Biophysical Research Communications"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"W668","DOI":"10.1093\/nar\/gkh371","article-title":"DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data","volume":"32","author":"L Whitmore","year":"2004","journal-title":"Nucleic Acids Research"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1002\/bip.20853","article-title":"Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases","volume":"89","author":"L Whitmore","year":"2008","journal-title":"Biopolymers"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.bej.2009.04.005","article-title":"The role of disulfide bond formation in the conformational folding kinetics of denatured\/reduced lysozyme","volume":"46","author":"GZ Wang","year":"2009","journal-title":"Biochemical Engineering Journal"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1093\/bioinformatics\/bti242","article-title":"Improved prediction of protein-protein binding sites using a support vector machines approach","volume":"21","author":"JR Bradford","year":"2005","journal-title":"Bioinformatics"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1002\/jcc.20291","article-title":"GROMACS: fast, flexible, and free","volume":"26","author":"D Van Der Spoel","year":"2005","journal-title":"J Comput Chem"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"2031","DOI":"10.1002\/jcc.21773","article-title":"Optimization of parameters for molecular dynamics simulation using smooth particle-mesh Ewald in GROMACS 4.5","volume":"32","author":"MJ Abraham","year":"2011","journal-title":"J Comput Chem"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"8577","DOI":"10.1063\/1.470117","article-title":"A Smooth Particle Mesh Ewald Method","volume":"103","author":"U Essmann","year":"1995","journal-title":"Journal of Chemical Physics"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H","article-title":"LINCS: A linear constraint solver for molecular simulations","volume":"18","author":"B Hess","year":"1997","journal-title":"Journal of Computational Chemistry"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1002\/jcc.1078","article-title":"An improved GROMOS96 force field for aliphatic hydrocarbons in the condensed phase","volume":"22","author":"LD Schuler","year":"2001","journal-title":"Journal of Computational Chemistry"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/S0022-2836(02)00672-1","article-title":"Increasing temperature accelerates protein unfolding without changing the pathway of unfolding","volume":"322","author":"R Day","year":"2002","journal-title":"J Mol Biol"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"W Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1016\/j.jneumeth.2006.09.013","article-title":"Linear quantitation of A beta aggregation using Thioflavin T: Reduction in fibril formation by colostrinin","volume":"160","author":"M Bourhim","year":"2007","journal-title":"Journal of Neuroscience Methods"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"5960","DOI":"10.1111\/j.1742-4658.2009.07307.x","article-title":"The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds","volume":"276","author":"SA Hudson","year":"2009","journal-title":"Febs Journal"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1016\/j.biochi.2005.03.017","article-title":"Two distinct intermediates of trigger factor are populated during guanidine denaturation","volume":"87","author":"CP Liu","year":"2005","journal-title":"Biochimie"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"4484","DOI":"10.1021\/bi001822b","article-title":"The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL","volume":"40","author":"AL Smoot","year":"2001","journal-title":"Biochemistry"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/S0167-4838(98)00038-7","article-title":"Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-anilino-1-naphthalene sulfonate","volume":"1385","author":"I Sirangelo","year":"1998","journal-title":"Biochim Biophys Acta"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1002\/bip.360310111","article-title":"Study of the \u201cmolten globule\u201d intermediate state in protein folding by a hydrophobic fluorescent probe","volume":"31","author":"GV Semisotnov","year":"1991","journal-title":"Biopolymers"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1002\/9780470110560.ch3","article-title":"Fluorescence Techniques for Studying Protein-Structure","volume":"35","author":"MR Eftink","year":"1991","journal-title":"Methods of Biochemical Analysis"},{"key":"ref48","first-page":"276","article-title":"The use of fluorescence methods to monitor unfolding transitions in proteins","volume":"63","author":"MR Eftink","year":"1998","journal-title":"Biochemistry-Moscow"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.bpc.2003.09.005","article-title":"A fast and accurate procedure to collect and analyze unfolding fluorescence signal: the case of dystroglycan domains","volume":"107","author":"E Di Stasio","year":"2004","journal-title":"Biophysical Chemistry"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1007\/s00726-010-0524-4","article-title":"Acid-induced unfolding of didecameric keyhole limpet hemocyanin: detection and characterizations of decameric and tetrameric intermediate states","volume":"39","author":"A Varshney","year":"2010","journal-title":"Amino Acids"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1007\/s12013-011-9237-x","article-title":"pH-dependent conformational transitions in conalbumin (ovotransferrin), a metalloproteinase from hen egg white","volume":"61","author":"G Rabbani","year":"2011","journal-title":"Cell Biochem Biophys"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1110\/ps.04627004","article-title":"Probing folding and fluorescence quenching in human gammaD crystallin Greek key domains using triple tryptophan mutant proteins","volume":"13","author":"MS Kosinski-Collins","year":"2004","journal-title":"Protein Sci"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"1993","DOI":"10.1073\/pnas.040554397","article-title":"Molecular basis of a progressive juvenile-onset hereditary cataract","volume":"97","author":"A Pande","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"2533","DOI":"10.1007\/s00253-013-5123-3","article-title":"Structural characteristics of thermostable immunogenic outer membrane protein from Salmonella enterica serovar Typhi","volume":"98","author":"G Rabbani","year":"2014","journal-title":"Appl Microbiol Biotechnol"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1007\/BF02099940","article-title":"Evolution of a protein superfamily: relationships between vertebrate lens crystallins and microorganism dormancy proteins","volume":"30","author":"G Wistow","year":"1990","journal-title":"J Mol Evol"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1006\/jmbi.1997.1184","article-title":"Ca<sup>2+<\/sup>-loaded spherulin 3a from Physarum polycephalum adopts the prototype gamma-crystallin fold in aqueous solution","volume":"271","author":"B Rosinke","year":"1997","journal-title":"J Mol Biol"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1006\/jmbi.1998.2022","article-title":"NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure","volume":"282","author":"A Ohno","year":"1998","journal-title":"J Mol Biol"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"2427","DOI":"10.1110\/ps.072970207","article-title":"Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin","volume":"16","author":"IA Mills","year":"2007","journal-title":"Protein Sci"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"33285","DOI":"10.1074\/jbc.M109.031344","article-title":"Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin","volume":"284","author":"KL Moreau","year":"2009","journal-title":"J Biol Chem"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"10514","DOI":"10.1073\/pnas.1019152108","article-title":"Aggregation of gamma-crystallins associated with human cataracts via domain swapping at the C-terminal beta-strands","volume":"108","author":"P Das","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1002\/pro.296","article-title":"beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallin","volume":"19","author":"P Das","year":"2010","journal-title":"Protein Sci"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1110\/ps.041111405","article-title":"Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin","volume":"14","author":"SL Flaugh","year":"2005","journal-title":"Protein Sci"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"2030","DOI":"10.1110\/ps.051460505","article-title":"Interdomain side-chain interactions in human gammaD crystallin influencing folding and stability","volume":"14","author":"SL Flaugh","year":"2005","journal-title":"Protein Sci"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"30782","DOI":"10.1074\/jbc.M603882200","article-title":"Glutamine deamidation destabilizes human gammaD-crystallin and lowers the kinetic barrier to unfolding","volume":"281","author":"SL Flaugh","year":"2006","journal-title":"J Biol Chem"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1002\/pro.583","article-title":"Contributions of aromatic pairs to the folding and stability of long-lived human gammaD-crystallin","volume":"20","author":"F Kong","year":"2011","journal-title":"Protein Sci"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1076\/0271-3683(200006)2061-YFT462","article-title":"Amyloid-like protein structure in mammalian ocular lenses","volume":"20","author":"PH Frederikse","year":"2000","journal-title":"Current Eye Research"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"6005","DOI":"10.1093\/emboj\/cdf609","article-title":"Altered aggregation properties of mutant gamma-crystallins cause inherited cataract","volume":"21","author":"A Sandilands","year":"2002","journal-title":"The EMBO journal"},{"key":"ref68","doi-asserted-by":"crossref","unstructured":"Zhang W, Cai HC, Li FF, Xi YB, Ma X, <etal>et al<\/etal>.. (2011) The congenital cataract-linked G61C mutation destabilizes gamma D-crystallin and promotes non-native aggregation. Plos One 6.","DOI":"10.1371\/journal.pone.0020564"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"8654","DOI":"10.1021\/bi00151a036","article-title":"Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro","volume":"31","author":"W Colon","year":"1992","journal-title":"Biochemistry"},{"key":"ref70","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.pep.2007.09.019","article-title":"Production and comprehensive quality control of recombinant human Interleukin-1beta: a case study for a process development strategy","volume":"57","author":"H Block","year":"2008","journal-title":"Protein Expr Purif"},{"key":"ref71","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1016\/j.pep.2007.01.004","article-title":"Expression, purification, and in vitro cysteine-10 modification of native sequence recombinant human transthyretin","volume":"53","author":"JS Kingsbury","year":"2007","journal-title":"Protein Expr Purif"},{"key":"ref72","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1006\/exer.1996.0029","article-title":"Distribution and type of morphological damage in human nuclear age-related cataracts","volume":"62","author":"KJ Al-Ghoul","year":"1996","journal-title":"Exp Eye Res"},{"key":"ref73","first-page":"120","article-title":"Multilamellar bodies as potential scattering particles in human age-related nuclear cataracts","volume":"7","author":"KO Gilliland","year":"2001","journal-title":"Mol Vis"},{"key":"ref74","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.sbi.2006.01.011","article-title":"Protein aggregation and amyloidosis: confusion of the kinds?","volume":"16","author":"F Rousseau","year":"2006","journal-title":"Current Opinion in Structural Biology"},{"key":"ref75","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1016\/j.bpj.2010.12.3691","article-title":"Separating instability from aggregation propensity in gammaS-crystallin variants","volume":"100","author":"WD Brubaker","year":"2011","journal-title":"Biophys J"},{"key":"ref76","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/nchembio.131","article-title":"Amyloid formation by globular proteins under native conditions","volume":"5","author":"F Chiti","year":"2009","journal-title":"Nat Chem Biol"},{"key":"ref77","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1021\/bi100978r","article-title":"Computational design and biophysical characterization of aggregation-resistant point mutations for gammaD crystallin illustrate a balance of conformational stability and intrinsic aggregation propensity","volume":"50","author":"E Sahin","year":"2011","journal-title":"Biochemistry"},{"key":"ref78","first-page":"1","article-title":"In silico Investigation of the Disease-Associated Retinoschisin C110Y and C219G Mutants","volume":"29","author":"JW Wu","year":"2012","journal-title":"J Biomol Struct Dyn"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0112309","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,4]],"date-time":"2024-06-04T23:18:34Z","timestamp":1717543114000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0112309"}},"subtitle":[],"editor":[{"given":"Rizwan H.","family":"Khan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2014,11,12]]},"references-count":78,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2014,11,12]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0112309","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,11,12]]}}}