{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,3]],"date-time":"2026-03-03T03:15:55Z","timestamp":1772507755416,"version":"3.50.1"},"reference-count":74,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2014,11,1]],"date-time":"2014-11-01T00:00:00Z","timestamp":1414800000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2015,11,1]],"date-time":"2015-11-01T00:00:00Z","timestamp":1446336000000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"name":"Ministry of Science and Technology of China","award":["2010CB912402"],"award-info":[{"award-number":["2010CB912402"]}]},{"DOI":"10.13039\/501100011230","name":"State Key Laboratory of Biomembrane and Membrane Biotechnology","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100011230","id-type":"DOI","asserted-by":"crossref"}]}],"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":[[2014,11]]},"DOI":"10.1016\/j.bbadis.2014.07.022","type":"journal-article","created":{"date-parts":[[2014,7,30]],"date-time":"2014-07-30T18:49:37Z","timestamp":1406746177000},"page":"2216-2229","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"title":["Cataract-causing mutation R233H affects the stabilities of \u03b2B1- and \u03b2A3\/\u03b2B1-crystallins with different pH-dependence"],"prefix":"10.1016","volume":"1842","author":[{"given":"Yi-Bo","family":"Xi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wei-Jie","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiao-Tong","family":"Zuo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Harry Christianto","family":"Tjondro","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jing","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"An-Bang","family":"Dai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sha","family":"Wang","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.2014.07.022_bb0005","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.ceb.2013.12.006","article-title":"Sorting out the trash: the spatial nature of eukaryotic protein quality control","volume":"26","author":"Sontag","year":"2014","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0010","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"Dobson","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0015","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1007\/s00109-003-0464-5","article-title":"Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution","volume":"81","author":"Stefani","year":"2003","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0020","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."},{"key":"10.1016\/j.bbadis.2014.07.022_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."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0030","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":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0035","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.2014.07.022_bb0040","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1111\/cge.12182","article-title":"Genetics of human cataract","volume":"84","author":"Shiels","year":"2013","journal-title":"Clin. Genet."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0045","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1038\/nrg1202","article-title":"The genetic and molecular basis of congenital eye defects","volume":"4","author":"Graw","year":"2003","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0050","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/0002-9394(61)91117-5","article-title":"Syndromes with congenital cataract","volume":"52","author":"Francois","year":"1961","journal-title":"Am J. Ophthalmol."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0055","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.2014.07.022_bb0060","doi-asserted-by":"crossref","first-page":"2052","DOI":"10.1016\/S0161-6420(02)01249-6","article-title":"Incidence of age-related cataract over a 10-year interval: the Beaver Dam Eye Study","volume":"109","author":"Klein","year":"2002","journal-title":"Ophthalmology"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0065","doi-asserted-by":"crossref","first-page":"1786","DOI":"10.1056\/NEJM200006153422404","article-title":"Genetic and environmental factors in age-related nuclear cataracts in monozygotic and dizygotic twins","volume":"342","author":"Hammond","year":"2000","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0070","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.2014.07.022_bb0075","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.2014.07.022_bb0080","doi-asserted-by":"crossref","first-page":"1933","DOI":"10.1096\/fasebj.3.8.2656357","article-title":"Lens crystallins and their genes: diversity and tissue-specific expression","volume":"3","author":"Piatigorsky","year":"1989","journal-title":"FASEB J."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0085","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.2014.07.022_bb0090","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.2014.07.022_bb0095","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.2014.07.022_bb0100","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1016\/j.preteyeres.2012.06.001","article-title":"Novel roles for \u03b1-crystallins in retinal function and disease","volume":"31","author":"Kannan","year":"2012","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0105","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.2174\/156652412803306747","article-title":"Alpha-crystallins and tumorigenesis","volume":"12","author":"Chen","year":"2012","journal-title":"Curr. Mol. Med."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0110","doi-asserted-by":"crossref","first-page":"e49730","DOI":"10.1371\/journal.pone.0049730","article-title":"Crystallins are regulated biomarkers for monitoring topical therapy of glaucomatous optic neuropathy","volume":"8","author":"Prokosch","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0115","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.2014.07.022_bb0120","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.2014.07.022_bb0125","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.2014.07.022_bb0130","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.2014.07.022_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.2014.07.022_bb0140","doi-asserted-by":"crossref","first-page":"2464","DOI":"10.1021\/bi500146d","article-title":"The N-terminal extension of \u03b2B1-crystallin chaperones \u03b2-crystallin folding and cooperates with \u03b1A-crystallin","volume":"53","author":"Leng","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0145","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1146\/annurev.bi.58.070189.004001","article-title":"Mutational effects on protein stability","volume":"58","author":"Alber","year":"1989","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0150","doi-asserted-by":"crossref","first-page":"e70336","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"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0155","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/j.jmb.2004.08.050","article-title":"The P23T cataract mutation causes loss of solubility of folded \u03b3D-crystallin","volume":"343","author":"Evans","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0160","doi-asserted-by":"crossref","first-page":"6122","DOI":"10.1021\/bi100664s","article-title":"Increase in surface hydrophobicity of the cataract-associated P23T mutant of human \u03b3D-crystallin is responsible for its dramatically lower, retrograde solubility","volume":"49","author":"Pande","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0165","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1016\/S0022-2836(03)00375-9","article-title":"High-resolution X-ray crystal structures of human \u03b3D crystallin (1.25\u00c5) and the R58H mutant (1.15\u00c5) associated with aculeiform cataract","volume":"328","author":"Basak","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0170","doi-asserted-by":"crossref","first-page":"16856","DOI":"10.1073\/pnas.0707412104","article-title":"Altered phase diagram due to a single point mutation in human \u03b3D-crystallin","volume":"104","author":"McManus","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0175","doi-asserted-by":"crossref","first-page":"e217","DOI":"10.1038\/cddis.2011.100","article-title":"\u03b2A3\/A1-Crystallin controls anoikis-mediated cell death in astrocytes by modulating PI3K\/AKT\/mTOR and ERK survival pathways through the PKD\/Bit1-signaling axis","volume":"2","author":"Ma","year":"2011","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0180","doi-asserted-by":"crossref","first-page":"1629","DOI":"10.1038\/ncomms2624","article-title":"Impaired endolysosomal function disrupts Notch signalling in optic nerve astrocytes","volume":"4","author":"Valapala","year":"2013","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0185","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1074\/mcp.M600245-MCP200","article-title":"Elongation of axons during regeneration involves retinal crystallin \u03b2B2 (crybb2)","volume":"6","author":"Liedtke","year":"2007","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0190","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.bbadis.2013.10.001","article-title":"The importance of the last strand at the C-terminus in \u03b2B2-crystallin stability and assembly","volume":"1842","author":"Zhang","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0195","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1093\/hmg\/ddh110","article-title":"Characterization of the G91del CRYBA1\/3-crystallin protein: a cause of human inherited cataract","volume":"13","author":"Reddy","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0200","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.bbrc.2014.03.119","article-title":"Cataract-linked mutation R188H promotes \u03b2B2-crystallin aggregation and fibrillization during acid denaturation","volume":"447","author":"Xi","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0205","first-page":"321","article-title":"Interaction and biophysical properties of human lens Q155* \u03b2B2-crystallin mutant","volume":"11","author":"Liu","year":"2005","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0210","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.2014.07.022_bb0215","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.2014.07.022_bb0220","doi-asserted-by":"crossref","first-page":"e51200","DOI":"10.1371\/journal.pone.0051200","article-title":"The congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of \u03b2B2-crystallin","volume":"7","author":"Xu","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0225","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1016\/j.bbadis.2012.11.005","article-title":"Increasing \u03b2B1-crystallin sensitivity to proteolysis caused by the congenital cataract-microcornea syndrome mutation S129R","volume":"1832","author":"Wang","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0230","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1038\/nrg1672","article-title":"Missense meanderings in sequence space: a biophysical view of protein evolution","volume":"6","author":"DePristo","year":"2005","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0235","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1001\/archophthalmol.2011.11","article-title":"Novel \u03b2-crystallin gene mutations in Chinese families with nuclear cataracts","volume":"129","author":"Wang","year":"2011","journal-title":"Arch. Ophthalmol."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0240","doi-asserted-by":"crossref","first-page":"2606","DOI":"10.1110\/ps.03265903","article-title":"Crystal structure of truncated human \u03b2B1-crystallin","volume":"12","author":"Montfort","year":"2003","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0245","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.2014.07.022_bb0250","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.2014.07.022_bb0255","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.2014.07.022_bb0260","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":"Biochem. Mosc."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0265","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0270","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."},{"issue":"Pt 2","key":"10.1016\/j.bbadis.2014.07.022_bb0275","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1042\/bj2820589","article-title":"Spectrofluorimetric assessment of the surface hydrophobicity of proteins","volume":"282","author":"Cardamone","year":"1992","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0280","doi-asserted-by":"crossref","first-page":"e15035","DOI":"10.1371\/journal.pone.0015035","article-title":"Differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: molten globule state and aggregates","volume":"5","author":"Povarova","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0285","doi-asserted-by":"crossref","first-page":"2403","DOI":"10.1021\/bi00461a025","article-title":"pH-Induced denaturation of proteins: a single salt bridge contributes 3\u20135kcal\/mol to the free energy of folding of T4 lysozyme","volume":"29","author":"Anderson","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0290","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3109\/10409237509102551","article-title":"The stability of globular proteins","volume":"3","author":"Pace","year":"1975","journal-title":"Crit. Rev. Biochem."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0295","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1038\/nrg2808","article-title":"Mutational effects and the evolution of new protein functions","volume":"11","author":"Soskine","year":"2010","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0300","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":"Chiti","year":"2009","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0305","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1006\/jmbi.1999.3218","article-title":"Salt bridge stability in monomeric proteins","volume":"293","author":"Kumar","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0310","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.2014.07.022_bb0315","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1093\/protein\/10.11.1347","article-title":"Association properties of betaB2- and betaA3-crystallin: ability to form dimers","volume":"10","author":"Hejtmancik","year":"1997","journal-title":"Protein Eng."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0320","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1021\/bi034617f","article-title":"Energetics of domain-domain interactions and entropy driven association of \u03b2-crystallins","volume":"43","author":"Sergeev","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0325","doi-asserted-by":"crossref","first-page":"6592","DOI":"10.1021\/bi00480a007","article-title":"Quaternary interactions in eye lens \u03b2-crystallins: basic and acidic subunits of \u03b2-crystallins favor heterologous association","volume":"29","author":"Slingsby","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbadis.2014.07.022_bb0330","doi-asserted-by":"crossref","first-page":"3936","DOI":"10.1016\/j.febslet.2007.07.022","article-title":"Protein\u2013protein interactions among human lens acidic and basic beta-crystallins","volume":"581","author":"Liu","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0335","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1016\/j.bpj.2010.12.3691","article-title":"Separating instability from aggregation propensity in \u03b3S-crystallin variants","volume":"100","author":"Brubaker","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0340","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1002\/pro.2422","article-title":"An alternative structural isoform in amyloid-like aggregates formed from thermally denatured human \u03b3D-crystallin","volume":"23","author":"Moran","year":"2014","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0345","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1023\/A:1025771421906","article-title":"Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation","volume":"20","author":"Chi","year":"2003","journal-title":"Pharm. Res."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0350","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1085\/jgp.98.6.1085","article-title":"Cell to cell communication and pH in the frog lens","volume":"98","author":"Mathias","year":"1991","journal-title":"J. Gen. Physiol."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0355","doi-asserted-by":"crossref","first-page":"1981","DOI":"10.1002\/cphy.c110051","article-title":"Gap junctions","volume":"2","author":"Nielsen","year":"2012","journal-title":"Compr. Physiol."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0360","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1002\/humu.20724","article-title":"A novel mutation in AlphaA-crystallin (CRYAA) caused autosomal dominant congenital cataract in a large Chinese family","volume":"29","author":"Gu","year":"2008","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0365","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1086\/302619","article-title":"The \u03b3-crystallins and human cataracts: a puzzle made clearer","volume":"65","author":"H\u00e9on","year":"1999","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2014.07.022_bb0370","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1007\/s10541-005-0070-y","article-title":"Biochemical effects of molecular crowding","volume":"69","author":"Chebotareva","year":"2004","journal-title":"Biochemistry (Mosc)"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443914002348?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443914002348?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T04:32:27Z","timestamp":1649824347000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0925443914002348"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,11]]},"references-count":74,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2014,11]]}},"alternative-id":["S0925443914002348"],"URL":"https:\/\/doi.org\/10.1016\/j.bbadis.2014.07.022","relation":{},"ISSN":["0925-4439"],"issn-type":[{"value":"0925-4439","type":"print"}],"subject":[],"published":{"date-parts":[[2014,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Cataract-causing mutation R233H affects the stabilities of \u03b2B1- and \u03b2A3\/\u03b2B1-crystallins with different pH-dependence","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.2014.07.022","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}