{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T05:04:44Z","timestamp":1777525484142,"version":"3.51.4"},"reference-count":44,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"vor","delay-in-days":365,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31872724"],"award-info":[{"award-number":["31872724"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81700815"],"award-info":[{"award-number":["81700815"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81900837"],"award-info":[{"award-number":["81900837"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004147","name":"Tsinghua University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004147","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"published-print":{"date-parts":[[2021,2]]},"DOI":"10.1016\/j.bbadis.2020.166018","type":"journal-article","created":{"date-parts":[[2020,11,24]],"date-time":"2020-11-24T21:06:58Z","timestamp":1606252018000},"page":"166018","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"title":["\u03b2B2 W151R mutant is prone to degradation, aggregation and exposes the hydrophobic side chains in the fourth Greek Key motif"],"prefix":"10.1016","volume":"1867","author":[{"given":"Jingjie","family":"Xu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Huaxia","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ailing","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jia","family":"Xu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chenxi","family":"Fu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhekun","family":"Jia","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ke","family":"Yao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiangjun","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"49\u201350","key":"10.1016\/j.bbadis.2020.166018_bb0005","first-page":"445","article-title":"Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats","volume":"16","author":"Sakthivel","year":"2010","journal-title":"Mol. Vis."},{"issue":"1","key":"10.1016\/j.bbadis.2020.166018_bb0010","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1750-1172-9-26","article-title":"Novel and recurrent PITX3 mutations in Belgian families with autosomal dominant congenital cataract and anterior segment dysgenesis have similar phenotypic and functional characteristics","volume":"9","author":"Verdin","year":"2014","journal-title":"Orphanet Journal of Rare Diseases."},{"issue":"10094","key":"10.1016\/j.bbadis.2020.166018_bb0015","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1016\/S0140-6736(17)30544-5","article-title":"Cataracts","volume":"390","author":"Liu","year":"2017","journal-title":"Lancet."},{"issue":"1","key":"10.1016\/j.bbadis.2020.166018_bb0020","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1097\/ICU.0000000000000340","article-title":"The global state of cataract blindness","volume":"28","author":"Lee","year":"2017","journal-title":"Curr. Opin. Ophthalmol."},{"issue":"5","key":"10.1016\/j.bbadis.2020.166018_bb0025","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."},{"issue":"10","key":"10.1016\/j.bbadis.2020.166018_bb0030","first-page":"1911","article-title":"Cataract as a protein condensation disease: the proctor lecture","volume":"38","author":"Benedek","year":"1997","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"issue":"3","key":"10.1016\/j.bbadis.2020.166018_bb0035","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":"Progress in Biophysics & Molecular Biology."},{"issue":"16","key":"10.1016\/j.bbadis.2020.166018_bb0040","doi-asserted-by":"crossref","first-page":"11585","DOI":"10.1074\/jbc.275.16.11585","article-title":"Human lens beta-crystallin solubility","volume":"275","author":"Feng","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2020.166018_bb0045","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2017.05.109","article-title":"Effects of cataract-causing mutations W59C and W151C on \u03b2B2-crystallin structure, stability and folding","volume":"103","author":"Zhao","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbadis.2020.166018_bb0050","doi-asserted-by":"crossref","unstructured":"Gillespie RL, O'Sullivan J, Ashworth J, et al. Personalized diagnosis and management of congenital cataract by next-generation sequencing. Ophthalmology. 2014;121(11):2124\u20132137.e2122.","DOI":"10.1016\/j.ophtha.2014.06.006"},{"issue":"17","key":"10.1016\/j.bbadis.2020.166018_bb0055","doi-asserted-by":"crossref","first-page":"2765","DOI":"10.1016\/j.jmb.2015.07.001","article-title":"Congenital cataract-causing mutation G129C in gammaC-crystallin promotes the accumulation of two distinct unfolding intermediates that form highly toxic aggregates","volume":"427","author":"Xi","year":"2015","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbadis.2020.166018_bb0060","doi-asserted-by":"crossref","unstructured":"Qi LB, Hu LD, Liu H, Li HY, Leng XY, Yan YB. Cataract-causing mutation S228P promotes \u03b2B1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain. Protein & Cell. 2016;7(7).","DOI":"10.1007\/s13238-016-0284-3"},{"issue":"7562","key":"10.1016\/j.bbadis.2020.166018_bb0065","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1038\/nature14650","article-title":"Lanosterol reverses protein aggregation in cataracts","volume":"523","author":"Zhao","year":"2015","journal-title":"Nature."},{"issue":"1 Suppl","key":"10.1016\/j.bbadis.2020.166018_bb0070","first-page":"25","article-title":"ImageJ for microscopy","volume":"43","author":"Collins","year":"2007","journal-title":"Biotechniques."},{"issue":"7","key":"10.1016\/j.bbadis.2020.166018_bb0075","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1007\/s13238-016-0284-3","article-title":"Cataract-causing mutation S228P promotes betaB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain","volume":"7","author":"Qi","year":"2016","journal-title":"Protein Cell."},{"key":"10.1016\/j.bbadis.2020.166018_bb0080","unstructured":"Lindahl A, Hess, van der Spoel. GROMACS 2019.1 Manual. February 2019."},{"issue":"16","key":"10.1016\/j.bbadis.2020.166018_bb0085","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.2020.166018_bb0090","doi-asserted-by":"crossref","unstructured":"Das P, King JA, Zhou R. \u03b2-Strand interactions at the domain interface critical for the stability of human lens \u03b3D-crystallin. Protein Sci. 2010;19(1):0\u20130.","DOI":"10.1002\/pro.296"},{"issue":"2","key":"10.1016\/j.bbadis.2020.166018_bb0095","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1159\/000455752","article-title":"Inherited congenital cataract: a guide to suspect the genetic etiology in the cataract genesis","volume":"8","author":"Messina-Baas","year":"2017","journal-title":"Molecular Syndromology."},{"key":"10.1016\/j.bbadis.2020.166018_bb0100","first-page":"2007","article-title":"Cat-Map: putting cataract on the map","volume":"16","author":"Shiels","year":"2010","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bbadis.2020.166018_bb0105","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.exer.2016.06.011","article-title":"Mutations and mechanisms in congenital and age-related cataracts","volume":"156","author":"Shiels","year":"2017","journal-title":"Exp. Eye Res."},{"issue":"1","key":"10.1016\/j.bbadis.2020.166018_bb0110","first-page":"159","article-title":"Genetic heterogeneity of the Coppock-like cataract: a mutation in CRYBB2 on chromosome 22q11.2","volume":"41","author":"Gill","year":"2000","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"issue":"6295","key":"10.1016\/j.bbadis.2020.166018_bb0115","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1038\/347776a0","article-title":"X-ray analysis of \u03b2B2-crystallin and evolution of oligomeric lens proteins","volume":"347","author":"Bax","year":"1990","journal-title":"Nature."},{"issue":"6","key":"10.1016\/j.bbadis.2020.166018_bb0120","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1016\/0014-4835(90)90114-A","article-title":"Interaction of an altered beta-crystallin with other proteins in the Philly mouse lens","volume":"50","author":"Russell","year":"1990","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.bbadis.2020.166018_bb0125","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0070336","article-title":"Structural integrity of the Greek Key motif in \u03b2\u03b3-crystallins is vital for central eye lens transparency","volume":"8","author":"Vendra","year":"2013","journal-title":"PLoS One"},{"issue":"48","key":"10.1016\/j.bbadis.2020.166018_bb0130","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 \u03b3D-crystallin","volume":"284","author":"Moreau","year":"2009","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.bbadis.2020.166018_bb0135","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 D-crystallin","volume":"14","author":"Flaugh","year":"2005","journal-title":"Protein Sci."},{"issue":"26","key":"10.1016\/j.bbadis.2020.166018_bb0140","doi-asserted-by":"crossref","first-page":"10514","DOI":"10.1073\/pnas.1019152108","article-title":"Aggregation of \u03b3-crystallins associated with human cataracts via domain swapping at the C-terminal \u03b2-strands","volume":"108","author":"Das","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2020.166018_bb0145","doi-asserted-by":"crossref","unstructured":"Fiumara F, Fioriti L, Kandel ER, Hendrickson WA. Essential role of coiled coils for aggregation and activity of Q\/N-rich prions and polyQ proteins. Cell. 2010;143(7):0\u20131135.","DOI":"10.1016\/j.cell.2010.11.042"},{"issue":"3","key":"10.1016\/j.bbadis.2020.166018_bb0150","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1016\/j.jsb.2014.01.013","article-title":"B?R K, et al. Your personalized protein structure: Andrei N. Lupas fused to GCN4 adaptors","volume":"186","author":"Deiss","year":"2014","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.bbadis.2020.166018_bb0155","article-title":"A missense mutation in CRYBB2 leads to progressive congenital membranous cataract by impacting the solubility and function of \u03b2B2-crystallin","volume":"8","author":"Chen","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bbadis.2020.166018_bb0160","doi-asserted-by":"crossref","unstructured":"Sun W, Xiao X, Li S, Guo X, Zhang Q. Exome sequencing of 18 Chinese families with congenital cataracts: a new sight of the NHS gene. PLoS ONE. 2014;9(6).","DOI":"10.1371\/journal.pone.0100455"},{"issue":"2","key":"10.1016\/j.bbadis.2020.166018_bb0165","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1159\/000445669","article-title":"Whole exome sequencing reveals a mutation in CRYBB2 in a large Mexican family with autosomal dominant pulverulent cataract","volume":"7","author":"Messina-Baas","year":"2016","journal-title":"Molecular Syndromology."},{"issue":"4","key":"10.1016\/j.bbadis.2020.166018_bb0170","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1002\/humu.22948","article-title":"Sporadic and familial congenital cataracts: mutational spectrum and new diagnoses using next-generation sequencing","volume":"37","author":"Ma","year":"2016","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbadis.2020.166018_bb0175","first-page":"144","article-title":"Characterization of a novel mutation in the CRYBB2 gene associated with autosomal dominant congenital posterior subcapsular cataract in a Chinese family","volume":"17","author":"Yao","year":"2011","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bbadis.2020.166018_bb0180","first-page":"1837","article-title":"Molecular analysis of cataract families in India: new mutations in the CRYBB2 and GJA3 genes and rare polymorphisms","volume":"16","author":"Santhiya","year":"2010","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bbadis.2020.166018_bb0185","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/bs.pmbts.2015.04.007","article-title":"Lens biology and biochemistry","volume":"134","author":"Hejtmancik","year":"2015","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"issue":"21","key":"10.1016\/j.bbadis.2020.166018_bb0190","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":"Horwitz","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2020.166018_bb0195","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/S0076-6879(98)90032-5","article-title":"Lens alpha-crystallin: chaperone-like properties","volume":"290","author":"Horwitz","year":"1998","journal-title":"Methods Enzymol."},{"issue":"16","key":"10.1016\/j.bbadis.2020.166018_bb0200","doi-asserted-by":"crossref","first-page":"16425","DOI":"10.1074\/jbc.M313402200","article-title":"Binding of destabilized betaB2-crystallin mutants to alpha-crystallin: the role of a folding intermediate","volume":"279","author":"Sathish","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"10","key":"10.1016\/j.bbadis.2020.166018_bb0205","doi-asserted-by":"crossref","first-page":"1939","DOI":"10.1016\/j.febslet.2007.04.005","article-title":"Specificity of alphaA-crystallin binding to destabilized mutants of betaB1-crystallin","volume":"581","author":"McHaourab","year":"2007","journal-title":"FEBS Lett."},{"issue":"1","key":"10.1016\/j.bbadis.2020.166018_bb0210","doi-asserted-by":"crossref","first-page":"8459","DOI":"10.1038\/s41598-019-44676-4","article-title":"Failure of oxysterols such as lanosterol to restore lens clarity from cataracts","volume":"9","author":"Daszynski","year":"2019","journal-title":"Sci. Rep."},{"issue":"27","key":"10.1016\/j.bbadis.2020.166018_bb0215","doi-asserted-by":"crossref","first-page":"8479","DOI":"10.1021\/jacs.8b03065","article-title":"Lanosterol disrupts aggregation of human \u03b3D-crystallin by binding to the hydrophobic dimerization interface","volume":"140","author":"Kang","year":"2018","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbadis.2020.166018_bb0220","doi-asserted-by":"crossref","unstructured":"Hu LD, Wang J, Chen XJ, Yan YB. Lanosterol modulates proteostasis via dissolving cytosolic sequestosomes\/aggresome-like induced structures. Biochimica et Biophysica Acta - Molecular Cell Research. 2020;1867(2).","DOI":"10.1016\/j.bbamcr.2019.118617"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443920303665?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443920303665?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,14]],"date-time":"2025-10-14T05:00:06Z","timestamp":1760418006000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0925443920303665"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,2]]},"references-count":44,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2021,2]]}},"alternative-id":["S0925443920303665"],"URL":"https:\/\/doi.org\/10.1016\/j.bbadis.2020.166018","relation":{},"ISSN":["0925-4439"],"issn-type":[{"value":"0925-4439","type":"print"}],"subject":[],"published":{"date-parts":[[2021,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"\u03b2B2 W151R mutant is prone to degradation, aggregation and exposes the hydrophobic side chains in the fourth Greek Key motif","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbadis.2020.166018","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"166018"}}