{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T06:07:19Z","timestamp":1761718039696},"reference-count":47,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2007,11,1]],"date-time":"2007-11-01T00:00:00Z","timestamp":1193875200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2007,11]]},"DOI":"10.1016\/j.jmb.2007.08.062","type":"journal-article","created":{"date-parts":[[2007,9,6]],"date-time":"2007-09-06T20:07:28Z","timestamp":1189109248000},"page":"1293-1304","source":"Crossref","is-referenced-by-count":15,"title":["Mixed Oligomer Formation between Human \u03b1A-Crystallin and its Cataract-causing G98R Mutant: Structural, Stability and Functional Differences"],"prefix":"10.1016","volume":"373","author":[{"given":"Devendra","family":"Singh","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bakthisaran","family":"Raman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tangirala","family":"Ramakrishna","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ch. Mohan","family":"Rao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2007.08.062_bib1","doi-asserted-by":"crossref","first-page":"5819","DOI":"10.1073\/pnas.82.17.5819","article-title":"Complete structure of the alpha B-crystallin gene: conservation of the exon-intron distribution in the two nonlinked alpha-crystallin genes","volume":"82","author":"Quax-Jeuken","year":"1985","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2007.08.062_bib2","doi-asserted-by":"crossref","first-page":"2360","DOI":"10.1073\/pnas.79.7.2360","article-title":"Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin","volume":"79","author":"Ingolia","year":"1982","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2007.08.062_bib3","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1177\/38.1.2294148","article-title":"Cellular distribution of alpha B-crystallin in non-lenticular tissues","volume":"38","author":"Iwaki","year":"1990","journal-title":"J. Histochem. Cytochem."},{"key":"10.1016\/j.jmb.2007.08.062_bib4","doi-asserted-by":"crossref","first-page":"23337","DOI":"10.1016\/S0021-9258(18)50096-X","article-title":"Alpha A-crystallin is expressed in non-ocular tissues","volume":"267","author":"Srinivasan","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib5","doi-asserted-by":"crossref","first-page":"31792","DOI":"10.1074\/jbc.M503182200","article-title":"Alpha-crystallin is a target gene of the farnesoid X-activated receptor in human livers","volume":"280","author":"Lee","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib6","doi-asserted-by":"crossref","first-page":"3652","DOI":"10.1073\/pnas.88.9.3652","article-title":"Alpha B-crystallin is a small heat shock protein","volume":"88","author":"Klemenz","year":"1991","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2007.08.062_bib7","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1159\/000016362","article-title":"Heat shock proteins and the cellular response to osmotic stress","volume":"10","author":"Beck","year":"2000","journal-title":"Cell. Physiol. Biochem."},{"key":"10.1016\/j.jmb.2007.08.062_bib8","doi-asserted-by":"crossref","first-page":"2613","DOI":"10.1111\/j.1742-4658.2005.04708.x","article-title":"The small heat shock proteins and their role in human disease","volume":"272","author":"Sun","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.jmb.2007.08.062_bib9","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/S0959-440X(99)00048-2","article-title":"Small heat-shock proteins and their potential role in human disease","volume":"10","author":"Clark","year":"2000","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jmb.2007.08.062_bib10","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. USA"},{"key":"10.1016\/j.jmb.2007.08.062_bib11","doi-asserted-by":"crossref","first-page":"6220","DOI":"10.1074\/jbc.272.10.6220","article-title":"Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin","volume":"272","author":"Sun","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib12","doi-asserted-by":"crossref","first-page":"34773","DOI":"10.1074\/jbc.274.49.34773","article-title":"Differential temperature-dependent chaperone-like activity of alphaA- and alphaB-crystallin homoaggregates","volume":"274","author":"Datta","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib13","doi-asserted-by":"crossref","first-page":"27264","DOI":"10.1016\/S0021-9258(18)46978-5","article-title":"Chaperone-like activity and quaternary structure of alpha-crystallin","volume":"269","author":"Raman","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib14","doi-asserted-by":"crossref","first-page":"24137","DOI":"10.1074\/jbc.274.34.24137","article-title":"Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins","volume":"274","author":"Kumar","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib15","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/S0014-5793(01)02451-6","article-title":"Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation","volume":"497","author":"Rajaraman","year":"2001","journal-title":"FEBS Letters"},{"key":"10.1016\/j.jmb.2007.08.062_bib16","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1111\/j.1432-1033.1997.00380.x","article-title":"Molecular chaperones protect catalase against thermal stress","volume":"247","author":"Hook","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jmb.2007.08.062_bib17","doi-asserted-by":"crossref","first-page":"32559","DOI":"10.1074\/jbc.M006133200","article-title":"Complete protection by alpha-crystallin of lens sorbitol dehydrogenase undergoing thermal stress","volume":"275","author":"Marini","year":"2000","journal-title":"J.Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib18","first-page":"29","article-title":"Protection of a restriction enzyme from heat inactivation by alpha-crystallin","volume":"4","author":"Hess","year":"1998","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jmb.2007.08.062_bib19","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1042\/0264-6021:3590547","article-title":"Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation","volume":"359","author":"Goenka","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.jmb.2007.08.062_bib20","doi-asserted-by":"crossref","first-page":"9415","DOI":"10.1074\/jbc.273.16.9415","article-title":"Interactions of chaperone alpha-crystallin with the molten globule state of xylose reductase. Implications for reconstitution of the active enzyme","volume":"273","author":"Rawat","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib21","doi-asserted-by":"crossref","first-page":"2727","DOI":"10.1110\/ps.0213802","article-title":"Alpha-crystallin and ATP facilitate the in vitro renaturation of xylanase: enhancement of refolding by metal ions","volume":"11","author":"Nath","year":"2002","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2007.08.062_bib22","first-page":"768","article-title":"Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family","volume":"12","author":"Santhiya","year":"2006","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jmb.2007.08.062_bib23","first-page":"1372","article-title":"The cataract-causing mutation G98R in human alphaA-crystallin leads to folding defects and loss of chaperone activity","volume":"12","author":"Singh","year":"2006","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jmb.2007.08.062_bib24","doi-asserted-by":"crossref","first-page":"3488","DOI":"10.1021\/bi00466a010","article-title":"A dynamic quaternary structure of bovine alpha-crystallin as indicated from intermolecular exchange of subunits","volume":"29","author":"van den Oetelaar","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2007.08.062_bib25","doi-asserted-by":"crossref","first-page":"29511","DOI":"10.1074\/jbc.272.47.29511","article-title":"Subunit exchange of alphaA-crystallin","volume":"272","author":"Bova","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib26","doi-asserted-by":"crossref","first-page":"41004","DOI":"10.1074\/jbc.M007686200","article-title":"Packing-induced conformational and functional changes in the subunits of alpha-crystallin","volume":"275","author":"Datta","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib27","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1074\/jbc.273.1.286","article-title":"Intermolecular exchange and stabilization of recombinant human alphaA- and alphaB-crystallin","volume":"273","author":"Sun","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib28","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/S0014-5793(98)00707-8","article-title":"Subunit exchange of lens alpha-crystallin: a fluorescence energy transfer study with the fluorescent labeled alphaA-crystallin mutant W9F as a probe","volume":"430","author":"Sun","year":"1998","journal-title":"FEBS Letters"},{"key":"10.1016\/j.jmb.2007.08.062_bib29","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1093\/hmg\/7.3.471","article-title":"Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA","volume":"7","author":"Litt","year":"1998","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jmb.2007.08.062_bib30","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1038\/1765","article-title":"A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy","volume":"20","author":"Vicart","year":"1998","journal-title":"Nature Genet."},{"key":"10.1016\/j.jmb.2007.08.062_bib31","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1038\/sj.ejhg.5201046","article-title":"Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q","volume":"11","author":"Mackay","year":"2003","journal-title":"Eur. J. Hum. Genet."},{"key":"10.1016\/j.jmb.2007.08.062_bib32","doi-asserted-by":"crossref","first-page":"1141","DOI":"10.1086\/324158","article-title":"Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans","volume":"69","author":"Berry","year":"2001","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.jmb.2007.08.062_bib33","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1167\/iovs.05-1004","article-title":"A novel alphaB-crystallin mutation associated with autosomal dominant congenital lamellar cataract","volume":"47","author":"Liu","year":"2006","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jmb.2007.08.062_bib34","doi-asserted-by":"crossref","first-page":"9460","DOI":"10.1021\/bi010582c","article-title":"Protein interactions leading to conformational changes monitored by limited proteolysis: apo form and fragments of horse cytochrome c","volume":"40","author":"Spolaore","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2007.08.062_bib35","doi-asserted-by":"crossref","first-page":"50380","DOI":"10.1074\/jbc.M204898200","article-title":"Apolipoprotein E4 forms a molten globule. A potential basis for its association with disease","volume":"277","author":"Morrow","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib36","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/S0165-022X(99)00021-4","article-title":"Detection and assay of proteases using calf lens beta-crystallin aggregate as substrate","volume":"40","author":"Trivedi","year":"1999","journal-title":"J. Biochem. Biophys. Methods"},{"key":"10.1016\/j.jmb.2007.08.062_bib37","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1021\/bi991656b","article-title":"Mutation of R116C results in highly oligomerized alpha A-crystallin with modified structure and defective chaperone-like function","volume":"39","author":"Shroff","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2007.08.062_bib38","doi-asserted-by":"crossref","first-page":"6137","DOI":"10.1073\/pnas.96.11.6137","article-title":"Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function","volume":"96","author":"Bova","year":"1999","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2007.08.062_bib39","doi-asserted-by":"crossref","first-page":"33235","DOI":"10.1074\/jbc.274.47.33235","article-title":"The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro","volume":"274","author":"Perng","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.08.062_bib40","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":"Biswas","year":"2004","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.jmb.2007.08.062_bib41","first-page":"155","article-title":"Expression of the alpha-crystallin\/small heat-shock protein\/molecular chaperone genes in the lens and other tissues","volume":"69","author":"Sax","year":"1994","journal-title":"Adv. Enzymol. Relat. Areas Mol. Biol."},{"key":"10.1016\/j.jmb.2007.08.062_bib42","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/S0167-7799(02)02047-4","article-title":"Preparative protein refolding","volume":"20","author":"Middelberg","year":"2002","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.jmb.2007.08.062_bib43","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.pep.2006.07.011","article-title":"On-column refolding and purification of transglutaminase from Streptomyces fradiae expressed as inclusion bodies in Escherichia coli","volume":"51","author":"Liu","year":"2007","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.jmb.2007.08.062_bib44","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1038\/nbt0396-329","article-title":"Improved refolding of an immobilised fusion protein","volume":"14","author":"Stempfer","year":"1996","journal-title":"Nature Biotechnol."},{"key":"10.1016\/j.jmb.2007.08.062_bib45","doi-asserted-by":"crossref","first-page":"2411","DOI":"10.1002\/pro.5560041120","article-title":"How to measure and predict the molar absorption coefficient of a protein","volume":"4","author":"Pace","year":"1995","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2007.08.062_bib46","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1002\/bip.20630","article-title":"Differential recognition of natural and non-natural substrate by molecular chaperone alpha-crystallin-A subunit exchange study","volume":"85","author":"Biswas","year":"2007","journal-title":"Biopolymers"},{"key":"10.1016\/j.jmb.2007.08.062_bib47","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 Letters"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283607011448?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283607011448?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,8,22]],"date-time":"2021-08-22T22:07:21Z","timestamp":1629670041000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283607011448"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,11]]},"references-count":47,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2007,11]]}},"alternative-id":["S0022283607011448"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2007.08.062","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2007,11]]}}}