{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,7]],"date-time":"2026-04-07T23:23:44Z","timestamp":1775604224874,"version":"3.50.1"},"reference-count":65,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,8,1]],"date-time":"2017-08-01T00:00:00Z","timestamp":1501545600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Experimental Eye Research"],"published-print":{"date-parts":[[2017,8]]},"DOI":"10.1016\/j.exer.2017.05.005","type":"journal-article","created":{"date-parts":[[2017,5,18]],"date-time":"2017-05-18T02:16:35Z","timestamp":1495073795000},"page":"163-173","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"special_numbering":"C","title":["A structural and functional study of Gln147 deamidation in \u03b1A-crystallin, a site of modification in human cataract"],"prefix":"10.1016","volume":"161","author":[{"given":"Nicholas J.","family":"Ray","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Damien","family":"Hall","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2441-8108","authenticated-orcid":false,"given":"John A.","family":"Carver","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.exer.2017.05.005_bib1","first-page":"2407","article-title":"Structural and functional roles of deamidation of N146 and\/or truncation of NH2-or COOH-termini in human \u03b1B-crystallin","volume":"17","author":"Asomugha","year":"2011","journal-title":"Mol. Vis."},{"key":"10.1016\/j.exer.2017.05.005_bib2","doi-asserted-by":"crossref","first-page":"3069","DOI":"10.1021\/bi0518141","article-title":"Mini-\u03b1B-crystallin: a functional element of \u03b1B-crystallin with chaperone-like activity","volume":"45","author":"Bhattacharyya","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.exer.2017.05.005_bib3","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.exer.2017.05.005_bib4","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/0009-2614(80)80041-8","article-title":"Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy","volume":"69","author":"Bodenhausen","year":"1980","journal-title":"Chem. Phys. Lett."},{"key":"10.1016\/j.exer.2017.05.005_bib5","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1074\/jbc.275.2.1035","article-title":"Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations","volume":"275","author":"Bova","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.exer.2017.05.005_bib6","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/S1350-9462(98)00027-5","article-title":"Probing the structure and interactions of crystallin proteins by NMR spectroscopy","volume":"18","author":"Carver","year":"1999","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.exer.2017.05.005_bib7","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0014-5793(92)81386-Z","article-title":"Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens \u03b1-crystallin","volume":"311","author":"Carver","year":"1992","journal-title":"FEBS Lett."},{"key":"10.1016\/j.exer.2017.05.005_bib8","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1016\/S0022-2836(02)00144-4","article-title":"The interaction of the molecular chaperone \u03b1-crystallin with unfolding \u03b1-lactalbumin: a structural and kinetic spectroscopic study","volume":"318","author":"Carver","year":"2002","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.exer.2017.05.005_bib9","doi-asserted-by":"crossref","first-page":"22618","DOI":"10.1074\/jbc.M116.739250","article-title":"Small heat shock proteins prevent alpha-synuclein aggregation via transient interactions and their efficacy is affected by the rate of aggregation","volume":"291","author":"Cox","year":"2016","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.exer.2017.05.005_bib10","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1146\/annurev.bb.20.060191.002511","article-title":"Defining solution conformations of small linear peptides","volume":"20","author":"Dyson","year":"1991","journal-title":"Annu. Rev. Biophys. Biophys. Chem."},{"key":"10.1016\/j.exer.2017.05.005_bib11","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1007\/s00018-008-8327-4","article-title":"Crystallin proteins and amyloid fibrils","volume":"66","author":"Ecroyd","year":"2009","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.exer.2017.05.005_bib12","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/S0021-9258(19)75855-4","article-title":"Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation","volume":"262","author":"Geiger","year":"1987","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.exer.2017.05.005_bib13","doi-asserted-by":"crossref","first-page":"7870","DOI":"10.1021\/ja00231a044","article-title":"Clean TOCSY for proton spin system identification in macromolecules","volume":"110","author":"Griesinger","year":"1988","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.exer.2017.05.005_bib14","doi-asserted-by":"crossref","first-page":"11579","DOI":"10.1074\/jbc.M110.148627","article-title":"The common modification in \u03b1A-crystallin in the lens, N101D, is associated with increased opacity in a mouse model","volume":"286","author":"Gupta","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.exer.2017.05.005_bib15","doi-asserted-by":"crossref","first-page":"44258","DOI":"10.1074\/jbc.M405648200","article-title":"Deamidation affects structural and functional properties of human \u03b1A-crystallin and its oligomerization with \u03b1B-crystallin","volume":"279","author":"Gupta","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.exer.2017.05.005_bib16","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1167\/iovs.03-0720","article-title":"Effect of deamidation of asparagine 146 on functional and structural properties of human lens \u03b1B-crystallin","volume":"45","author":"Gupta","year":"2004","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.exer.2017.05.005_bib18","doi-asserted-by":"crossref","first-page":"3935","DOI":"10.1021\/pr070138h","article-title":"Post-translational modifications in the nuclear region of young, aged, and cataract human lenses","volume":"6","author":"Hains","year":"2007","journal-title":"J.\u00a0Proteom. Res."},{"key":"10.1016\/j.exer.2017.05.005_bib17","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.exer.2017.05.005_bib19","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1016\/j.febslet.2015.01.032","article-title":"A\u00a0multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation","volume":"589","author":"Hall","year":"2015","journal-title":"FEBS Lett."},{"key":"10.1016\/j.exer.2017.05.005_bib20","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.ab.2015.11.021","article-title":"Protein aggregate turbidity: simulation of turbidity profiles for mixed-aggregation reactions","volume":"498","author":"Hall","year":"2016","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.exer.2017.05.005_bib21","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.ab.2016.07.013","article-title":"Recognizing and analyzing variability in amyloid formation kinetics: simulation and statistical methods","volume":"510","author":"Hall","year":"2016","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.exer.2017.05.005_bib22","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1006\/exer.2000.0868","article-title":"The major in\u00a0vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage","volume":"71","author":"Hanson","year":"2000","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.exer.2017.05.005_bib23","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1110\/ps.03427504","article-title":"Laser light-scattering evidence for an altered association of \u03b2B1-crystallin deamidated in the connecting peptide","volume":"13","author":"Harms","year":"2004","journal-title":"Protein Sci."},{"key":"10.1016\/j.exer.2017.05.005_bib24","doi-asserted-by":"crossref","first-page":"6398","DOI":"10.1167\/iovs.14-14623","article-title":"Molecular mechanism of formation of cortical opacity in CRYAAN101D transgenic mice","volume":"55","author":"Hegde","year":"2014","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.exer.2017.05.005_bib25","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.pbiomolbio.2014.03.003","article-title":"Dynamical structure of \u03b1B-crystallin","volume":"115","author":"Hochberg","year":"2014","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"10.1016\/j.exer.2017.05.005_bib26","doi-asserted-by":"crossref","first-page":"6127","DOI":"10.3168\/jds.2013-6831","article-title":"Caseins and the casein micelle: their biological functions, structures, and behavior in foods","volume":"96","author":"Holt","year":"2013","journal-title":"J.\u00a0Dairy Sci."},{"key":"10.1016\/j.exer.2017.05.005_bib27","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/S0014-4835(02)00278-6","article-title":"Alpha-crystallin","volume":"76","author":"Horwitz","year":"2003","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.exer.2017.05.005_bib28","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1038\/nsmb.1891","article-title":"Solid-state NMR and SAXS studies provide a structural basis for the activation of \u03b1B-crystallin oligomers","volume":"17","author":"Jehle","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.exer.2017.05.005_bib29","doi-asserted-by":"crossref","first-page":"14076","DOI":"10.1021\/bi026288h","article-title":"Deamidation, but not truncation, decreases the urea stability of a lens structural protein, \u03b2B1-crystallin","volume":"41","author":"Kim","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.exer.2017.05.005_bib30","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1042\/BJ20121187","article-title":"The small heat-shock protein alphaB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of alpha-lactalbumin","volume":"448","author":"Kulig","year":"2012","journal-title":"Biochem. J."},{"key":"10.1016\/j.exer.2017.05.005_bib31","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0006-291X(80)90695-6","article-title":"A\u00a0two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules","volume":"95","author":"Kumar","year":"1980","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.exer.2017.05.005_bib32","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1002\/pro.380","article-title":"Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function","volume":"19","author":"Laganowsky","year":"2010","journal-title":"Prot. Sci."},{"key":"10.1016\/j.exer.2017.05.005_bib33","doi-asserted-by":"crossref","first-page":"3146","DOI":"10.1021\/bi052051k","article-title":"Deamidation in human lens \u03b2B2-crystallin destabilizes the dimer","volume":"45","author":"Lampi","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.exer.2017.05.005_bib34","first-page":"359","article-title":"Decreased heat stability and increased chaperone requirement of modified human betaB1-crystallins","volume":"8","author":"Lampi","year":"2002","journal-title":"Mol. Vis."},{"key":"10.1016\/j.exer.2017.05.005_bib35","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1006\/exer.1998.0481","article-title":"Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry","volume":"67","author":"Lampi","year":"1998","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.exer.2017.05.005_bib36","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.pbiomolbio.2014.02.004","article-title":"Lens \u03b2-crystallins: the role of deamidation and related modifications in aging and cataract","volume":"115","author":"Lampi","year":"2014","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"10.1016\/j.exer.2017.05.005_bib37","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1042\/bj3540079","article-title":"The molecular chaperone \u03b1-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of \u03b1-lactalbumin","volume":"354","author":"Lindner","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.exer.2017.05.005_bib38","doi-asserted-by":"crossref","first-page":"12494","DOI":"10.1016\/S0021-9258(18)99902-3","article-title":"Post-translational modifications of water-soluble human lens crystallins from young adults","volume":"269","author":"Miesbauer","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.exer.2017.05.005_bib39","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.exer.2017.05.005_bib40","doi-asserted-by":"crossref","first-page":"5885","DOI":"10.1111\/j.1742-4658.2008.06719.x","article-title":"Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity","volume":"275","author":"Morris","year":"2008","journal-title":"FEBS J."},{"key":"10.1016\/j.exer.2017.05.005_bib41","doi-asserted-by":"crossref","first-page":"6036","DOI":"10.1021\/bi002555c","article-title":"Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism","volume":"40","author":"Nielsen","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.exer.2017.05.005_bib42","doi-asserted-by":"crossref","first-page":"4890","DOI":"10.1021\/acs.biochem.5b00185","article-title":"Deamidation of human \u03b3S-crystallin increases net attractive protein interactions: implications for cataract","volume":"54","author":"Pande","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.exer.2017.05.005_bib43","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/0014-5793(95)00440-K","article-title":"Temperature dependent chaperone-like activity of alpha-crystallin","volume":"365","author":"Raman","year":"1995","journal-title":"FEBS Lett."},{"key":"10.1016\/j.exer.2017.05.005_bib44","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1007\/s12551-015-0176-4","article-title":"Biophysical chemistry of the ageing eye lens","volume":"7","author":"Ray","year":"2015","journal-title":"Biophys. Rev."},{"key":"10.1016\/j.exer.2017.05.005_bib45","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.bbagen.2015.08.015","article-title":"Deamidation of N76 in human \u03b3S-crystallin promotes dimer formation","volume":"1860","author":"Ray","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.exer.2017.05.005_bib46","doi-asserted-by":"crossref","first-page":"4565","DOI":"10.1074\/jbc.275.7.4565","article-title":"Temperature-dependent chaperone activity and structural properties of human \u03b1A-and \u03b1B-crystallins","volume":"275","author":"Reddy","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.exer.2017.05.005_bib47","doi-asserted-by":"crossref","first-page":"1281","DOI":"10.1007\/s00018-003-2287-5","article-title":"Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals?","volume":"60","author":"Reissner","year":"2003","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.exer.2017.05.005_bib48","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1016\/j.jmb.2004.05.054","article-title":"Interaction of the molecular chaperone \u03b1B-crystallin with \u03b1-synuclein: effects on amyloid fibril formation and chaperone activity","volume":"340","author":"Rekas","year":"2004","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.exer.2017.05.005_bib49","series-title":"Molecular clocks: deamidation of asparaginyl and glutaminyl residues in peptides and proteins","author":"Robinson","year":"2004"},{"key":"10.1016\/j.exer.2017.05.005_bib50","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1016\/S0300-9084(00)88890-2","article-title":"Protein thermostability in extremophiles","volume":"80","author":"Scandurra","year":"1998","journal-title":"Biochimie"},{"key":"10.1016\/j.exer.2017.05.005_bib51","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 BBA-Gen. Subj."},{"key":"10.1016\/j.exer.2017.05.005_bib52","doi-asserted-by":"crossref","first-page":"3407","DOI":"10.1021\/bi00742a007","article-title":"Selective reduction of cystine I-VIII in \u03b1-lactalbumin of bovine milk","volume":"12","author":"Shechter","year":"1973","journal-title":"Biochemistry"},{"key":"10.1016\/j.exer.2017.05.005_bib53","doi-asserted-by":"crossref","first-page":"1979","DOI":"10.1016\/S0021-9258(18)97414-4","article-title":"The deaggregation of bovine lens \u03b1-crystallin","volume":"240","author":"Spector","year":"1965","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.exer.2017.05.005_bib54","first-page":"94","article-title":"Post-translationally modified human lens crystallin fragments show aggregation in\u00a0vitro","volume":"10","author":"Srivastava","year":"2017","journal-title":"Biochem. Biophys. Rep."},{"key":"10.1016\/j.exer.2017.05.005_bib55","doi-asserted-by":"crossref","first-page":"6220","DOI":"10.1074\/jbc.272.10.6220","article-title":"Conformational and functional differences between recombinant human lens \u03b1A-and \u03b1B-crystallin","volume":"272","author":"Sun","year":"1997","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.exer.2017.05.005_bib56","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1110\/ps.035410.108","article-title":"Deamidation destabilizes and triggers aggregation of a lens protein, \u03b2A3-crystallin","volume":"17","author":"Takata","year":"2008","journal-title":"Protein Sci."},{"key":"10.1016\/j.exer.2017.05.005_bib57","doi-asserted-by":"crossref","first-page":"17027","DOI":"10.1021\/bi051352r","article-title":"Amyloid fibril formation by bovine milk \u03ba-casein and its inhibition by the molecular chaperones \u03b1S-and \u03b2-casein","volume":"44","author":"Thorn","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.exer.2017.05.005_bib58","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1111\/j.1742-4658.2004.04507.x","article-title":"R120G \u03b1B-crystallin promotes the unfolding of reduced \u03b1-lactalbumin and is inherently unstable","volume":"272","author":"Treweek","year":"2005","journal-title":"Febs J."},{"key":"10.1016\/j.exer.2017.05.005_bib59","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1016\/j.exer.2010.08.015","article-title":"A\u00a0quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, \u03b1A- and \u03b1B-crystallin","volume":"91","author":"Treweek","year":"2010","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.exer.2017.05.005_bib60","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1016\/j.exer.2004.12.007","article-title":"Age-related nuclear cataract\u2014oxidation is the key","volume":"80","author":"Truscott","year":"2005","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.exer.2017.05.005_bib61","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1159\/000267940","article-title":"The influence of some post-translational modifications on the chaperone-like activity of \u03b1-crystallin","volume":"28","author":"Van Boekel","year":"1996","journal-title":"Ophthalmic Res."},{"key":"10.1016\/j.exer.2017.05.005_bib62","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1002\/prot.20449","article-title":"The CCPN data model for NMR spectroscopy: development of a software pipeline","volume":"59","author":"Vranken","year":"2005","journal-title":"Proteins Struct. Funct. Bioinforma."},{"key":"10.1016\/j.exer.2017.05.005_bib63","first-page":"2196","article-title":"Cataract-specific posttranslational modifications and changes in the composition of urea-soluble protein fraction from the rat lens","volume":"19","author":"Yanshole","year":"2013","journal-title":"Mol. Vis."},{"key":"10.1016\/j.exer.2017.05.005_bib64","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1016\/j.jmb.2011.06.007","article-title":"The molecular refractive function of lens \u03b3-crystallins","volume":"411","author":"Zhao","year":"2011","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.exer.2017.05.005_bib65","first-page":"1","article-title":"Measurement of amyloid formation by turbidity assay\u2014seeing through the cloud","author":"Zhao","year":"2016","journal-title":"Biophys. Rev."}],"container-title":["Experimental Eye Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0014483516303098?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0014483516303098?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,4,3]],"date-time":"2021-04-03T14:38:53Z","timestamp":1617460733000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0014483516303098"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,8]]},"references-count":65,"alternative-id":["S0014483516303098"],"URL":"https:\/\/doi.org\/10.1016\/j.exer.2017.05.005","relation":{},"ISSN":["0014-4835"],"issn-type":[{"value":"0014-4835","type":"print"}],"subject":[],"published":{"date-parts":[[2017,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"A structural and functional study of Gln147 deamidation in \u03b1A-crystallin, a site of modification in human cataract","name":"articletitle","label":"Article Title"},{"value":"Experimental Eye Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.exer.2017.05.005","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}