{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T18:31:59Z","timestamp":1786991519551,"version":"build-2736575974"},"reference-count":426,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2022,11,1]],"date-time":"2022-11-01T00:00:00Z","timestamp":1667260800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,11,1]],"date-time":"2022-11-01T00:00:00Z","timestamp":1667260800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,9,24]],"date-time":"2022-09-24T00:00:00Z","timestamp":1663977600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100007812","name":"University of Washington","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007812","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001314","name":"Durham University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001314","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2022,11]]},"DOI":"10.1016\/j.jbc.2022.102537","type":"journal-article","created":{"date-parts":[[2022,9,26]],"date-time":"2022-09-26T21:40:22Z","timestamp":1664228422000},"page":"102537","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":40,"title":["Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens"],"prefix":"10.1016","volume":"298","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0644-4123","authenticated-orcid":false,"given":"Roy A.","family":"Quinlan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6651-5205","authenticated-orcid":false,"given":"John I.","family":"Clark","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2022.102537_bib1","series-title":"Albert and Jakobiec's Principles and Practice of Ophthalmology","first-page":"1","article-title":"Biology of the transparent lens and changes with age","author":"Clark","year":"2020"},{"key":"10.1016\/j.jbc.2022.102537_bib2","series-title":"Ophthalmology","first-page":"1528","article-title":"Basic science of the lens","author":"Dai","year":"2008"},{"key":"10.1016\/j.jbc.2022.102537_bib3","series-title":"Corneal Transparency","author":"Farrell","year":"2000"},{"key":"10.1016\/j.jbc.2022.102537_bib4","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1113\/jphysiol.1957.sp005758","article-title":"The structure and transparency of the cornea","volume":"136","author":"Maurice","year":"1957","journal-title":"J.\u00a0Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib5","first-page":"493","article-title":"The physical basis for transparency of the crystalline lens","volume":"1","author":"Trokel","year":"1962","journal-title":"Invest. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib6","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/j.exer.2003.10.008","article-title":"Order and disorder in the transparent media of the eye","volume":"78","author":"Clark","year":"2004","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib7","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1364\/AO.10.000459","article-title":"Theory of transparency of the eye","volume":"10","author":"Benedek","year":"1971","journal-title":"Appl. Opt."},{"key":"10.1016\/j.jbc.2022.102537_bib8","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1097\/00003226-200111000-00015","article-title":"Enigma of the abundant water-soluble cytoplasmic proteins of the cornea: the \"refracton\" hypothesis","volume":"20","author":"Piatigorsky","year":"2001","journal-title":"Cornea"},{"key":"10.1016\/j.jbc.2022.102537_bib9","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.semcdb.2007.09.015","article-title":"Corneal crystallins and the development of cellular transparency","volume":"19","author":"Jester","year":"2008","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib10","doi-asserted-by":"crossref","first-page":"18953","DOI":"10.1074\/jbc.M609275200","article-title":"Ubiquitous lens alpha-, beta-, and gamma-crystallins accumulate in anuran cornea as corneal crystallins","volume":"282","author":"Krishnan","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib11","doi-asserted-by":"crossref","DOI":"10.1088\/1361-648X\/aae000","article-title":"Protein refractive index increment is determined by conformation as well as composition","volume":"30","author":"Khago","year":"2018","journal-title":"J.\u00a0Phys. Condens Matter"},{"key":"10.1016\/j.jbc.2022.102537_bib12","doi-asserted-by":"crossref","first-page":"5195","DOI":"10.1038\/srep05195","article-title":"Primary sequence contribution to the optical function of the eye lens","volume":"4","author":"Mahendiran","year":"2014","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2022.102537_bib13","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1097\/00003226-200003000-00012","article-title":"The keratocyte network of human cornea: a three-dimensional study using confocal laser scanning fluorescence microscopy","volume":"19","author":"Hahnel","year":"2000","journal-title":"Cornea"},{"key":"10.1016\/j.jbc.2022.102537_bib14","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1016\/j.exer.2010.06.021","article-title":"The molecular basis of corneal transparency","volume":"91","author":"Hassell","year":"2010","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib15","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.preteyeres.2015.07.001","article-title":"Corneal structure and transparency","volume":"49","author":"Meek","year":"2015","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib16","doi-asserted-by":"crossref","DOI":"10.1098\/rsif.2013.0512","article-title":"Mechanisms of self-organization for the collagen fibril lattice in the human cornea","volume":"10","author":"Cheng","year":"2013","journal-title":"J.\u00a0R. Soc. Interf."},{"key":"10.1016\/j.jbc.2022.102537_bib17","doi-asserted-by":"crossref","first-page":"2205","DOI":"10.1016\/S0006-3495(03)74646-3","article-title":"Changes in the refractive index of the stroma and its extrafibrillar matrix when the cornea swells","volume":"85","author":"Meek","year":"2003","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102537_bib18","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1038\/sj.eye.6700574","article-title":"Transparency, swelling and scarring in the corneal stroma","volume":"17","author":"Meek","year":"2003","journal-title":"Eye (Lond)"},{"key":"10.1016\/j.jbc.2022.102537_bib19","series-title":"Noninvasive Diagnostic Techniques in Ophthalmology","first-page":"189","article-title":"Light scattering from cornea and corneal transparency","author":"McCally","year":"1990"},{"key":"10.1016\/j.jbc.2022.102537_bib20","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1007\/s002490050220","article-title":"Determination of corneal gel dynamics","volume":"28","author":"Matsuura","year":"1999","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.jbc.2022.102537_bib21","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.str.2009.11.013","article-title":"Structural interactions between collagen and proteoglycans are elucidated by three-dimensional electron tomography of bovine cornea","volume":"18","author":"Lewis","year":"2010","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2022.102537_bib22","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1002\/aja.1001910408","article-title":"A\u00a0quantitative evaluation of Fourier components in transparent and opaque calf cornea","volume":"191","author":"Gisselberg","year":"1991","journal-title":"Am. J. Anat."},{"key":"10.1016\/j.jbc.2022.102537_bib23","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/bs.pmbts.2015.05.001","article-title":"Lens development and crystallin gene expression","volume":"134","author":"Cvekl","year":"2015","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib24","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.1098\/rstb.2010.0175","article-title":"The lens: a classical model of embryonic induction providing new insights into cell determination in early development","volume":"366","author":"Gunhaga","year":"2011","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib25","series-title":"Early Lens Development","author":"Robinson","year":"2004"},{"key":"10.1016\/j.jbc.2022.102537_bib26","doi-asserted-by":"crossref","first-page":"4432","DOI":"10.1242\/dev.107953","article-title":"The cellular and molecular mechanisms of vertebrate lens development","volume":"141","author":"Cvekl","year":"2014","journal-title":"Development"},{"key":"10.1016\/j.jbc.2022.102537_bib27","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/S0070-2153(10)90010-0","article-title":"Eye development","volume":"90","author":"Graw","year":"2010","journal-title":"Curr. Top Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib28","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1167\/iovs.61.6.5","article-title":"Identification of a primary stroma and novel endothelial cell projections in the developing human cornea","volume":"61","author":"Feneck","year":"2020","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib29","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1016\/j.semcdb.2006.10.004","article-title":"Cell cycle regulation in the developing lens","volume":"17","author":"Griep","year":"2006","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib30","article-title":"Gradient moduli lens models: how material properties and application of forces can affect deformation and distributions of stress","volume":"6","author":"Wang","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2022.102537_bib31","series-title":"The Ocular Lens","author":"Maisel","year":"1985"},{"key":"10.1016\/j.jbc.2022.102537_bib32","first-page":"603","article-title":"CP49 and filensin intermediate filaments are essential for formation of cold cataract","volume":"26","author":"Li","year":"2020","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib33","doi-asserted-by":"crossref","first-page":"43259","DOI":"10.1074\/jbc.M111.264580","article-title":"The orchestration of mammalian tissue morphogenesis through a series of coherent feed-forward loops","volume":"286","author":"Xie","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib34","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/j.tig.2017.08.001","article-title":"Signaling and gene regulatory networks in mammalian lens development","volume":"33","author":"Cvekl","year":"2017","journal-title":"Trends Genet."},{"key":"10.1016\/j.jbc.2022.102537_bib35","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.exer.2015.11.006","article-title":"From eyeless to neurological diseases","volume":"156","author":"Graw","year":"2017","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib36","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1007\/s11064-016-2156-x","article-title":"Lens biology is a dimension of neurobiology","volume":"42","author":"Frederikse","year":"2017","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.jbc.2022.102537_bib37","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1038\/s41398-020-0791-0","article-title":"Polymorphisms in CRYBB2 encoding \u03b2B2-crystallin are associated with antisaccade performance and memory function","volume":"10","author":"Giegling","year":"2020","journal-title":"Transl. Psych."},{"key":"10.1016\/j.jbc.2022.102537_bib38","series-title":"Histology of the Human Eye; an Atlas and Textbook","author":"Hogan","year":"1971"},{"key":"10.1016\/j.jbc.2022.102537_bib39","series-title":"Structure of the Vertebrate Lens","author":"Kuszak","year":"2004"},{"key":"10.1016\/j.jbc.2022.102537_bib40","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1016\/j.exer.2003.09.016","article-title":"Fibre cell organization in crystalline lenses","volume":"78","author":"Kuszak","year":"2004","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib41","series-title":"Biology of the Lens: Lens Transparency as a Function of Embryology, Anatomy, and Physiology","author":"Kuszak","year":"2008"},{"key":"10.1016\/j.jbc.2022.102537_bib42","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1387\/ijdb.041880jk","article-title":"Development of lens sutures","volume":"48","author":"Kuszak","year":"2004","journal-title":"Int. J. Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib43","first-page":"251","article-title":"Computer modeling of secondary fiber development and growth: I. Nonprimate lenses","volume":"12","author":"Kuszak","year":"2006","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib44","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1006\/exer.1994.1138","article-title":"The interrelationship of lens anatomy and optical quality. II. Primate lenses","volume":"59","author":"Kuszak","year":"1994","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib45","doi-asserted-by":"crossref","first-page":"5822","DOI":"10.3390\/ijms21165822","article-title":"Connexin mutants compromise the lens circulation and cause cataracts through biomineralization","volume":"21","author":"Berthoud","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib46","doi-asserted-by":"crossref","first-page":"1418","DOI":"10.3390\/biom10101418","article-title":"Do connexin mutants cause cataracts by perturbing glutathione levels and redox metabolism in the lens?","volume":"10","author":"Jara","year":"2020","journal-title":"Biomolecules"},{"key":"10.1016\/j.jbc.2022.102537_bib47","doi-asserted-by":"crossref","first-page":"3821","DOI":"10.1167\/iovs.19-27302","article-title":"Lens connexin channels have differential permeability to the second messenger cAMP","volume":"60","author":"Valiunas","year":"2019","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib48","doi-asserted-by":"crossref","first-page":"R994","DOI":"10.1152\/ajpregu.00180.2018","article-title":"The lens internal microcirculation system delivers solutes to the lens core faster than would be predicted by passive diffusion","volume":"315","author":"Vaghefi","year":"2018","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib49","doi-asserted-by":"crossref","first-page":"5388","DOI":"10.1364\/BOE.401254","article-title":"In\u00a0vivo SS-OCT imaging of crystalline lens sutures","volume":"11","author":"Gupta","year":"2020","journal-title":"Biomed. Opt. Express"},{"key":"10.1016\/j.jbc.2022.102537_bib50","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/0304-4165(84)90090-4","article-title":"Spatial reorganization of low-molecular-weight proteins during cold cataract opacification","volume":"800","author":"Gulik-Krzywicki","year":"1984","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102537_bib51","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/j.exer.2007.11.018","article-title":"Analysis of nuclear fiber cell cytoplasmic texture in advanced cataractous lenses from Indian subjects using Debye-Bueche theory","volume":"86","author":"Metlapally","year":"2008","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib52","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1159\/000265057","article-title":"Scanning electron microscopy of opaque and transparent states in reversible calf lens cataracts","volume":"12","author":"Clark","year":"1980","journal-title":"Ophthal. Res."},{"key":"10.1016\/j.jbc.2022.102537_bib53","first-page":"61","article-title":"Untersuchung der Proteinsubstanzen in den leichtbrechenden Medien des Auges I","volume":"18","author":"M\u00f6rner","year":"1894","journal-title":"Hoppe-Seyl."},{"key":"10.1016\/j.jbc.2022.102537_bib54","first-page":"634","article-title":"Color and solubility of the proteins of human cataracts","volume":"7","author":"Pirie","year":"1968","journal-title":"Invest. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib55","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/S0014-4835(65)80043-4","article-title":"The problem of albuminoid","volume":"4","author":"Waley","year":"1965","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib56","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1001\/archopht.1956.00930030475003","article-title":"Changes in lens proteins of rats during aging","volume":"55","author":"Dische","year":"1956","journal-title":"AMA Arch. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib57","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/0014-4835(73)90118-8","article-title":"On the presence and mechanism of formation of heavy molecular weight aggregates in human normal and cataractous lenses","volume":"15","author":"Jedziniak","year":"1973","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib58","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/0002-9394(51)90013-X","article-title":"Studies on the oxidation of cysteine to cystine in lens proteins during cataract formation","volume":"34","author":"Dische","year":"1951","journal-title":"Am. J. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib59","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1016\/0014-4835(72)90111-X","article-title":"Biochemical and fine structure studies on the water-insoluble components of the calf lens","volume":"13","author":"Lasser","year":"1972","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib60","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0014-4835(76)90033-6","article-title":"Structural proteins of the mammalian lens: a review with emphasis on changes in development, aging and cataract","volume":"22","author":"Harding","year":"1976","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib61","first-page":"51","article-title":"Quantitative verification of the existence of high molecular weight protein aggregates in the intact normal human lens by light-scattering spectroscopy","volume":"17","author":"Jedziniak","year":"1978","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib62","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/S0006-3495(21)00384-2","article-title":"Identification of the scattering elements responsible for lens opacification in cold cataracts","volume":"37","author":"Delaye","year":"1982","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102537_bib63","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1038\/302415a0","article-title":"Short-range order of crystallin proteins accounts for eye lens transparency","volume":"302","author":"Delaye","year":"1983","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102537_bib64","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.jbc.2022.102537_bib65","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0006-3495(79)85237-6","article-title":"Light scattering of normal human lens I. Application of random density and orientation fluctuation theory","volume":"26","author":"Bettelheim","year":"1979","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102537_bib66","doi-asserted-by":"crossref","first-page":"1078","DOI":"10.1126\/science.252.5009.1078","article-title":"The recruitment of crystallins: new functions precede gene duplication","volume":"252","author":"Piatigorsky","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102537_bib67","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1111\/j.1749-6632.1998.tb09626.x","article-title":"Multifunctional lens crystallins and corneal enzymes. More than meets the eye","volume":"842","author":"Piatigorsky","year":"1998","journal-title":"Ann. N. Y Acad. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib68","first-page":"130","article-title":"The search for a solution to senile cataracts. Proctor lecture","volume":"25","author":"Spector","year":"1984","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib69","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1098\/rsta.1979.0100","article-title":"Light scattering & reversible cataracts in calf and human lenses","volume":"293","author":"Benedek","year":"1979","journal-title":"Phil. Trans. R. Soc. Lond. A."},{"key":"10.1016\/j.jbc.2022.102537_bib70","first-page":"175","article-title":"Dynamic light scattering in the intact rabbit lens. Its relation to protein concentration","volume":"28","author":"Latina","year":"1987","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib71","doi-asserted-by":"crossref","first-page":"5065","DOI":"10.1021\/bi00438a025","article-title":"Elucidation of intermediate (mobile) and slow (solidlike) protein motions in bovine lens homogenates by carbon-13 NMR spectroscopy","volume":"28","author":"Morgan","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102537_bib72","first-page":"1396","article-title":"Morphology of the normal human lens","volume":"37","author":"Taylor","year":"1996","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib73","first-page":"169","article-title":"Reorganisation of the microtubule cytoskeleton and centrosomal loss during lens fibre cell differentiation","volume":"299","author":"Millar","year":"1997","journal-title":"Nova Acta Leopoldiana"},{"key":"10.1016\/j.jbc.2022.102537_bib74","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/0014-4835(79)90130-1","article-title":"Syneresis and its possible role in cataractogenesis","volume":"28","author":"Bettelheim","year":"1979","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib75","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0006-3495(83)84402-6","article-title":"Effect of change in concentration upon lens turbidity as predicted by the random fluctuation theory","volume":"41","author":"Bettelheim","year":"1983","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102537_bib76","doi-asserted-by":"crossref","first-page":"1240","DOI":"10.1177\/1535370219867296","article-title":"Microtubules: evolving roles and critical cellular interactions","volume":"244","author":"Logan","year":"2019","journal-title":"Exp. Biol. Med. (Maywood, N.J.)"},{"key":"10.1016\/j.jbc.2022.102537_bib77","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.exer.2016.03.009","article-title":"The cause and consequence of fiber cell compaction in the vertebrate lens","volume":"156","author":"Bassnett","year":"2017","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib78","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1098\/rstb.2010.0302","article-title":"Biological glass: structural determinants of eye lens transparency","volume":"366","author":"Bassnett","year":"2011","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib79","first-page":"135","article-title":"In\u00a0vivo observation of protein diffusivity in rabbit lenses","volume":"16","author":"Tanaka","year":"1977","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib80","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1039\/dc9745700007","article-title":"Introductory lecture","volume":"57","author":"Flory","year":"1974","journal-title":"Faraday Discuss. Chem. Soc."},{"key":"10.1016\/j.jbc.2022.102537_bib81","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1038\/scientificamerican0181-124","article-title":"Gels","volume":"244","author":"Tanaka","year":"1981","journal-title":"Sci. Am."},{"key":"10.1016\/j.jbc.2022.102537_bib82","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1515\/BC.2006.064","article-title":"Protein aggregation in crowded environments","volume":"387","author":"Ellis","year":"2006","journal-title":"Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib83","doi-asserted-by":"crossref","first-page":"8341","DOI":"10.1021\/acs.jpcb.9b05467","article-title":"Proteins: \"Boil 'Em, mash 'Em, stick 'Em in a stew\"","volume":"123","author":"Boob","year":"2019","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.jbc.2022.102537_bib84","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1002\/jps.20417","article-title":"Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations","volume":"94","author":"Minton","year":"2005","journal-title":"J.\u00a0Pharm. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib85","doi-asserted-by":"crossref","first-page":"5593","DOI":"10.1016\/j.jmb.2020.08.011","article-title":"The aggregation of \u03b1b-crystallin under crowding conditions is prevented by \u03b1A-crystallin: implications for \u03b1-crystallin stability and lens transparency","volume":"432","author":"Grosas","year":"2020","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib86","doi-asserted-by":"crossref","first-page":"10649","DOI":"10.1021\/acs.jpcb.1c07093","article-title":"Virtual issue on protein crowding and stability","volume":"125","author":"Feig","year":"2021","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.jbc.2022.102537_bib87","first-page":"700","article-title":"Organophosphates of the crystalline lens: a nuclear magnetic resonance spectroscopic study","volume":"21","author":"Greiner","year":"1981","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib88","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0014-4835(86)80070-7","article-title":"The effect of prolonged elevated glucose levels on the phosphate metabolism of the rabbit lens in perfused organ culture","volume":"43","author":"Willis","year":"1986","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib89","first-page":"1339","article-title":"31P nuclear magnetic resonance and laser spectroscopic analyses of lens transparency during calcium-induced opacification","volume":"31","author":"Beaulieu","year":"1990","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib90","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1002\/pro.2229","article-title":"Evolution of crystallins for a role in the vertebrate eye lens","volume":"22","author":"Slingsby","year":"2013","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib91","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/S0959-440X(00)00172-X","article-title":"Macromolecular crowding: an important but neglected aspect of the intracellular environment","volume":"11","author":"Ellis","year":"2001","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib92","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S1350-9462(98)00023-8","article-title":"Theoretical and experimental basis for the inhibition of cataract","volume":"18","author":"Benedek","year":"1999","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib93","series-title":"Cataract: Biochemistry, Epidemiology and Pharmacology","author":"Harding","year":"1991"},{"key":"10.1016\/j.jbc.2022.102537_bib94","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108709","article-title":"Hallmarks of lens aging and cataractogenesis","volume":"210","author":"Wishart","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib95","series-title":"Ageing of the Lens: Proceedings of the Symposium on Ageing of the Lens","first-page":"29","author":"Regnault","year":"1980"},{"key":"10.1016\/j.jbc.2022.102537_bib96","series-title":"Age Related Cataract","author":"Young","year":"1991"},{"key":"10.1016\/j.jbc.2022.102537_bib97","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1016\/S0140-6736(05)70803-5","article-title":"Age-related cataract","volume":"365","author":"Asbell","year":"2005","journal-title":"Lancet"},{"key":"10.1016\/j.jbc.2022.102537_bib98","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1038\/eye.1999.119","article-title":"Epidemiology of age-related cataract","volume":"13","author":"Taylor","year":"1999","journal-title":"Eye (Lond)"},{"key":"10.1016\/j.jbc.2022.102537_bib99","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1159\/000055612","article-title":"Age-related nuclear cataract: a lens transport problem","volume":"32","author":"Truscott","year":"2000","journal-title":"Ophthal. Res."},{"key":"10.1016\/j.jbc.2022.102537_bib100","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"},{"key":"10.1016\/j.jbc.2022.102537_bib101","first-page":"463","article-title":"Carbon turnover in the water-soluble protein of the adult human lens","volume":"19","author":"Stewart","year":"2013","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib102","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1126\/science.aaf1703","article-title":"Eye lens radiocarbon reveals centuries of longevity in the Greenland shark (Somniosus microcephalus)","volume":"353","author":"Nielsen","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102537_bib103","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.50170","article-title":"Long-lived metabolic enzymes in the crystalline lens identified by pulse-labeling of mice and mass spectrometry","volume":"8","author":"Liu","year":"2019","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2022.102537_bib104","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.mrrev.2019.02.004","article-title":"Cataractogenic load - a concept to study the contribution of ionizing radiation to accelerated aging in the eye lens","volume":"779","author":"Uwineza","year":"2019","journal-title":"Mutat. Res."},{"key":"10.1016\/j.jbc.2022.102537_bib105","first-page":"78","article-title":"Early responses to low-dose ionizing radiation in cellular lens epithelial models","volume":"197","author":"Ahmadi","year":"2022","journal-title":"Radiat. Res."},{"key":"10.1016\/j.jbc.2022.102537_bib106","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2020.108230","article-title":"Status of oxidative stress markers, advanced glycation index, and polyol pathway in age-related cataract subjects with and without diabetes","volume":"200","author":"Chitra","year":"2020","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib107","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1006\/exer.2001.1033","article-title":"Age-related telomere shortening occurs in lens epithelium from old rats and is slowed by caloric restriction","volume":"73","author":"Pendergrass","year":"2001","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib108","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.mrrev.2016.07.010","article-title":"Ionizing radiation induced cataracts: recent biological and mechanistic developments and perspectives for future research","volume":"770","author":"Ainsbury","year":"2016","journal-title":"Mutat. Res."},{"key":"10.1016\/j.jbc.2022.102537_bib109","first-page":"372","article-title":"Experimental radiation cataract--its clinical relevance","volume":"59","author":"Merriam","year":"1983","journal-title":"Bull. New York Acad. Med."},{"key":"10.1016\/j.jbc.2022.102537_bib110","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.icrp.2012.06.018","article-title":"Radiation cataract","volume":"41","author":"Kleiman","year":"2012","journal-title":"Ann. ICRP"},{"key":"10.1016\/j.jbc.2022.102537_bib111","doi-asserted-by":"crossref","first-page":"887","DOI":"10.18632\/aging.100081","article-title":"Ionizing radiation and aging: rejuvenating an old idea","volume":"1","author":"Richardson","year":"2009","journal-title":"Aging"},{"key":"10.1016\/j.jbc.2022.102537_bib112","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1667\/RRXX19.1","article-title":"Radiation cataractogenesis: epidemiology and biology","volume":"173","author":"Blakely","year":"2010","journal-title":"Radiat. Res."},{"key":"10.1016\/j.jbc.2022.102537_bib113","first-page":"1496","article-title":"X-ray induced cataract is preceded by LEC loss, and coincident with accumulation of cortical DNA, and ROS; similarities with age-related cataracts","volume":"16","author":"Pendergrass","year":"2010","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib114","first-page":"186","article-title":"Phase separation of X-irradiated lenses of rabbit","volume":"22","author":"Clark","year":"1982","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib115","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1111\/bjh.13148","article-title":"Incidence and risk factors for cataract after haematopoietic stem cell transplantation for childhood leukaemia: an LEA study","volume":"168","author":"Horwitz","year":"2015","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.jbc.2022.102537_bib116","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108772","article-title":"Sensitivity and latency of ionising radiation-induced cataract","volume":"212","author":"Ainsbury","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib117","first-page":"1","article-title":"Introduction to the special LDLensRad focus issue","volume":"197","author":"Ainsbury","year":"2022","journal-title":"Radiat. Res."},{"key":"10.1016\/j.jbc.2022.102537_bib118","first-page":"92","article-title":"Lens epithelial cell proliferation in response to ionizing radiation","volume":"197","author":"Barnard","year":"2022","journal-title":"Radiat. Res."},{"key":"10.1016\/j.jbc.2022.102537_bib119","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.1080\/09553002.2020.1812759","article-title":"Etiology of posterior subcapsular cataracts based on a review of risk factors including aging, diabetes, and ionizing radiation","volume":"96","author":"Richardson","year":"2020","journal-title":"Int. J. Radiat. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib120","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1136\/bjophthalmol-2019-315282","article-title":"Inherited cataracts: molecular genetics, clinical features, disease mechanisms and novel therapeutic approaches","volume":"104","author":"Berry","year":"2020","journal-title":"Br. J. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib121","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1002\/prca.200800085","article-title":"Proteome analysis of human foetal, aged and advanced nuclear cataract lenses","volume":"2","author":"Hains","year":"2008","journal-title":"Proteomics Clin. Appl."},{"key":"10.1016\/j.jbc.2022.102537_bib122","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.jbc.2022.102537_bib123","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1006\/exer.1998.0530","article-title":"Deamidation and disulfide bonding in human lens gamma-crystallins","volume":"67","author":"Hanson","year":"1998","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib124","doi-asserted-by":"crossref","first-page":"1837","DOI":"10.1172\/JCI38277","article-title":"Functions of the intermediate filament cytoskeleton in the eye lens","volume":"119","author":"Song","year":"2009","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.jbc.2022.102537_bib125","series-title":"Encyclopedia of Biological Chemistry III","first-page":"639","article-title":"Structural proteins | crystallins of the mammalian eye lens","author":"Kalligeraki","year":"2021"},{"key":"10.1016\/j.jbc.2022.102537_bib126","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1006\/exer.1998.0482","article-title":"Age-related changes in human lens crystallins identified by HPLC and mass spectrometry","volume":"67","author":"Ma","year":"1998","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib127","series-title":"Vegetative Physiology and Biochemistry","first-page":"213","article-title":"The lens","author":"Van Heyningen","year":"1962"},{"key":"10.1016\/j.jbc.2022.102537_bib128","series-title":"The Vertebrate Eye and its Adaptive Radiation","author":"Walls","year":"1942"},{"key":"10.1016\/j.jbc.2022.102537_bib129","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.jbc.2022.102537_bib130","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.jbc.2022.102537_bib131","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1073\/pnas.75.3.1204","article-title":"Aspartic acid racemization in heavy molecular weight crystallins and water insoluble protein from normal human lenses and cataracts","volume":"75","author":"Masters","year":"1978","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102537_bib132","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1007\/s11357-010-9171-7","article-title":"Racemisation and human cataract. D-Ser, D-Asp\/Asn and D-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lenses","volume":"33","author":"Hooi","year":"2011","journal-title":"Age (Dordr)"},{"key":"10.1016\/j.jbc.2022.102537_bib133","article-title":"Deamidation of the human eye lens protein \u03b3S-crystallin accelerates oxidative aging","author":"Norton-Baker","year":"2021","journal-title":"bioRxiv"},{"key":"10.1016\/j.jbc.2022.102537_bib134","doi-asserted-by":"crossref","first-page":"2554","DOI":"10.1021\/pr050473a","article-title":"Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility?","volume":"5","author":"Wilmarth","year":"2006","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.jbc.2022.102537_bib135","doi-asserted-by":"crossref","first-page":"1945","DOI":"10.1002\/pro.3915","article-title":"Cumulative deamidations of the major lens protein \u03b3S-crystallin increase its aggregation during unfolding and oxidation","volume":"29","author":"Vetter","year":"2020","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib136","doi-asserted-by":"crossref","first-page":"3819","DOI":"10.1021\/pr070182x","article-title":"Reliable detection of deamidated peptides from lens crystallin proteins using changes in reversed-phase elution times and parent ion masses","volume":"6","author":"Dasari","year":"2007","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.jbc.2022.102537_bib137","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1016\/j.tibs.2016.06.004","article-title":"Old proteins in man: a field in its infancy","volume":"41","author":"Truscott","year":"2016","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib138","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.104557","article-title":"Research progress in biological activities of succinimide derivatives","volume":"108","author":"Zhao","year":"2021","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib139","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.jbc.2022.102537_bib140","doi-asserted-by":"crossref","first-page":"12409","DOI":"10.1073\/pnas.221463198","article-title":"Deamidation of human proteins","volume":"98","author":"Robinson","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102537_bib141","doi-asserted-by":"crossref","DOI":"10.1016\/j.preteyeres.2019.100802","article-title":"Spatiotemporal changes in the human lens proteome: critical insights into long-lived proteins","volume":"76","author":"Schey","year":"2020","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib142","first-page":"1","article-title":"Bowman lecture. The conquest of cataract: a global challenge","volume":"104","author":"Kupfer","year":"1985","journal-title":"Trans. Ophthalmol. Soc. U K"},{"key":"10.1016\/j.jbc.2022.102537_bib143","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.jbc.2022.102537_bib144","series-title":"Collagen: Structure and Mechanics","first-page":"359","article-title":"The cornea and sclera","author":"Meek","year":"2008"},{"key":"10.1016\/j.jbc.2022.102537_bib145","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1016\/j.exer.2008.08.018","article-title":"Protein-protein interactions and lens transparency","volume":"87","author":"Takemoto","year":"2008","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib146","first-page":"879","article-title":"Role of short-range protein interactions in lens opacifications","volume":"12","author":"Ponce","year":"2006","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib147","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1007\/s12192-020-01092-2","article-title":"Peeking from behind the veil of enigma: emerging insights on small heat shock protein structure and function","volume":"25","author":"Klevit","year":"2020","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/j.jbc.2022.102537_bib148","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1002\/pro.2191","article-title":"Age-dependent racemization of serine residues in a human chaperone protein","volume":"22","author":"Hooi","year":"2013","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib149","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1002\/pro.2095","article-title":"Age-dependent deamidation of glutamine residues in human \u03b3S crystallin: deamidation and unstructured regions","volume":"21","author":"Hooi","year":"2012","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib150","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/j.bbapap.2018.04.002","article-title":"Identification of isomeric aspartate residues in \u03b2B2-crystallin from aged human lens","volume":"1866","author":"Takata","year":"2018","journal-title":"Biochim. Biophys. Acta Proteins Proteom"},{"key":"10.1016\/j.jbc.2022.102537_bib151","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1021\/acs.biochem.8b01053","article-title":"Succinylation is a gain-of-function modification in human lens \u03b1b-crystallin","volume":"58","author":"Nandi","year":"2019","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102537_bib152","doi-asserted-by":"crossref","first-page":"3817","DOI":"10.1042\/BCJ20190743","article-title":"Mechanism of protein cleavage at asparagine leading to protein-protein cross-links","volume":"476","author":"Friedrich","year":"2019","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2022.102537_bib153","doi-asserted-by":"crossref","first-page":"12203","DOI":"10.1074\/jbc.RA119.009052","article-title":"The l-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation","volume":"294","author":"Warmack","year":"2019","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib154","first-page":"476","article-title":"Crystallins in water soluble-high molecular weight protein fractions and water insoluble protein fractions in aging and cataractous human lenses","volume":"10","author":"Harrington","year":"2004","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib155","first-page":"1680","article-title":"Proteomic analysis of water insoluble proteins from normal and cataractous human lenses","volume":"13","author":"Harrington","year":"2007","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib156","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":"Takemoto","year":"1996","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib157","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1016\/j.str.2022.03.002","article-title":"Deamidation of the human eye lens protein \u03b3S-crystallin accelerates oxidative aging","volume":"30","author":"Norton-Baker","year":"2022","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2022.102537_bib158","doi-asserted-by":"crossref","first-page":"2755","DOI":"10.1021\/jasms.1c00193","article-title":"Data-independent acquisition mass spectrometry of the human lens enhances spatiotemporal measurement of fiber cell aging","volume":"32","author":"Cantrell","year":"2021","journal-title":"J.\u00a0Am. Soc. Mass Spectrom."},{"key":"10.1016\/j.jbc.2022.102537_bib159","doi-asserted-by":"crossref","first-page":"1515","DOI":"10.1021\/acs.analchem.1c04322","article-title":"Native mass spectrometry and surface induced dissociation provide insight into the post-translational modifications of tetrameric AQP0 isolated from bovine eye lens","volume":"94","author":"Harvey","year":"2022","journal-title":"Anal. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib160","first-page":"232","article-title":"Morbidity profiles of centenarians: survivors, delayers, and escapers","volume":"58","author":"Evert","year":"2003","journal-title":"J.\u00a0Gerontology. Ser. A, Biol. Sci. Med. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib161","first-page":"1201","article-title":"Life at the extreme limit: phenotypic characteristics of supercentenarians in Okinawa","volume":"63","author":"Willcox","year":"2008","journal-title":"J.\u00a0Gerontology. Ser. A, Biol. Sci. Med. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib162","doi-asserted-by":"crossref","first-page":"2091","DOI":"10.1016\/j.ophtha.2013.03.032","article-title":"Long-term changes in visual acuity in an older population over a 15-year period: the blue mountains eye study","volume":"120","author":"Hong","year":"2013","journal-title":"Ophthalmology"},{"key":"10.1016\/j.jbc.2022.102537_bib163","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1016\/S0161-6420(90)32514-9","article-title":"Distribution of lens opacities in the Italian-American case-control study of age-related cataract. The Italian-American study group","volume":"97","author":"Maraini","year":"1990","journal-title":"Ophthalmology"},{"key":"10.1016\/j.jbc.2022.102537_bib164","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1007\/s00417-020-04770-0","article-title":"Frequency of cataract surgery and its impact on visual function-results from the German Gutenberg Health Study","volume":"258","author":"Schuster","year":"2020","journal-title":"Graefes Arch. Clin. Exp. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib165","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1016\/j.ophtha.2016.01.036","article-title":"Genetic and dietary factors influencing the progression of nuclear cataract","volume":"123","author":"Yonova-Doing","year":"2016","journal-title":"Ophthalmology"},{"key":"10.1016\/j.jbc.2022.102537_bib166","series-title":"Nutritional and Environmental Influences on the Eye","first-page":"53","article-title":"Nutritional and environmental influences on risk for cataract","author":"Taylor","year":"1999"},{"key":"10.1016\/j.jbc.2022.102537_bib167","doi-asserted-by":"crossref","first-page":"10604","DOI":"10.1073\/pnas.0500398102","article-title":"Epigenetic differences arise during the lifetime of monozygotic twins","volume":"102","author":"Fraga","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102537_bib168","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1111\/j.1474-9726.2012.00835.x","article-title":"Epigenetic variation during the adult lifespan: cross-sectional and longitudinal data on monozygotic twin pairs","volume":"11","author":"Talens","year":"2012","journal-title":"Aging cell"},{"key":"10.1016\/j.jbc.2022.102537_bib169","doi-asserted-by":"crossref","first-page":"347","DOI":"10.3390\/genes5020347","article-title":"Epigenetic variation in monozygotic twins: a genome-wide analysis of DNA methylation in buccal cells","volume":"5","author":"van Dongen","year":"2014","journal-title":"Genes (Basel)"},{"key":"10.1016\/j.jbc.2022.102537_bib170","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1038\/s41467-018-08008-w","article-title":"Multi-ancestry study of blood lipid levels identifies four loci interacting with physical activity","volume":"10","author":"Kilpel\u00e4inen","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2022.102537_bib171","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.39856","article-title":"Genomics of 1 million parent lifespans implicates novel pathways and common diseases and distinguishes survival chances","volume":"8","author":"Timmers","year":"2019","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2022.102537_bib172","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1038\/nature19329","article-title":"Restricted diet delays accelerated ageing and genomic stress in DNA-repair-deficient mice","volume":"537","author":"Vermeij","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102537_bib173","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.\u00a0Proteome Res."},{"key":"10.1016\/j.jbc.2022.102537_bib174","doi-asserted-by":"crossref","first-page":"3554","DOI":"10.1167\/iovs.11-9085","article-title":"Racemization of two proteins over our lifespan: deamidation of asparagine 76 in \u03b3S crystallin is greater in cataract than in normal lenses across the age range","volume":"53","author":"Hooi","year":"2012","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib175","first-page":"110","article-title":"Existence of deamidated alphaB-crystallin fragments in normal and cataractous human lenses","volume":"9","author":"Srivastava","year":"2003","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib176","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.jbc.2022.102537_bib177","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1076\/ceyr.17.3.247.5218","article-title":"Quantitation of asparagine-101 deamidation from alpha-A crystallin during aging of the human lens","volume":"17","author":"Takemoto","year":"1998","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib178","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/S0014-4835(03)00159-3","article-title":"Human beta-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate","volume":"77","author":"Zhang","year":"2003","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib179","first-page":"95","article-title":"Post-translational modifications of eye lens crystallins: crosslinking, phosphorylation and deamidation","volume":"231","author":"de Jong","year":"1988","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib180","doi-asserted-by":"crossref","first-page":"19020","DOI":"10.1016\/S0021-9258(18)37383-6","article-title":"Spontaneous peptide bond cleavage in aging alpha-crystallin through a succinimide intermediate","volume":"263","author":"Voorter","year":"1988","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib181","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1038\/258264a0","article-title":"Stepwise degradations and deamidation of the eye lens protein alpha-crystallin in ageing","volume":"258","author":"Van Kleef","year":"1975","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102537_bib182","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/0014-5793(90)81131-7","article-title":"Site-specific racemization in aging alpha A-crystallin","volume":"269","author":"Groenen","year":"1990","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2022.102537_bib183","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/0014-5793(87)80935-3","article-title":"Age-dependent deamidation of chicken alpha A-crystallin","volume":"221","author":"Voorter","year":"1987","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2022.102537_bib184","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1006\/bbrc.1999.1748","article-title":"Formation of four isomers at the asp-151 residue of aged human alphaA-crystallin by natural aging","volume":"265","author":"Fujii","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2022.102537_bib185","doi-asserted-by":"crossref","first-page":"8638","DOI":"10.1021\/bi015924t","article-title":"Deamidation in human gamma S-crystallin from cataractous lenses is influenced by surface exposure","volume":"41","author":"Lapko","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102537_bib186","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1006\/exer.1996.0160","article-title":"Modifications of the water-insoluble human lens alpha-crystallins","volume":"63","author":"Lund","year":"1996","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib187","first-page":"164","article-title":"Increased deamidation of asparagine during human senile cataractogenesis","volume":"6","author":"Takemoto","year":"2000","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib188","doi-asserted-by":"crossref","first-page":"3936","DOI":"10.1016\/j.febslet.2007.07.022","article-title":"Protein-protein interactions among human lens acidic and basic beta-crystallins","volume":"581","author":"Liu","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2022.102537_bib189","doi-asserted-by":"crossref","first-page":"5007","DOI":"10.1167\/iovs.19-27535","article-title":"Molecular processes implicated in human age-related nuclear cataract","volume":"60","author":"Truscott","year":"2019","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib190","doi-asserted-by":"crossref","first-page":"4890","DOI":"10.1021\/acs.biochem.5b00185","article-title":"Deamidation of human \u03b3s-crystallin increases attractive protein interactions: implications for cataract","volume":"54","author":"Pande","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102537_bib191","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.jbc.2022.102537_bib192","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1134\/S000629792203004X","article-title":"Protein aggregation and cataract: role of age-related modifications and mutations in \u03b1-crystallins","volume":"87","author":"Budnar","year":"2022","journal-title":"Biochemistry (Mosc)"},{"key":"10.1016\/j.jbc.2022.102537_bib193","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":"Truscott","year":"2005","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib194","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/0005-2795(77)90212-4","article-title":"Oxidative changes in human lens proteins during senile nuclear cataract formation","volume":"492","author":"Truscott","year":"1977","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102537_bib195","doi-asserted-by":"crossref","first-page":"3211","DOI":"10.1074\/mcp.M115.050948","article-title":"Evidence of highly conserved \u03b2-crystallin disulfidome that can be mimicked by in\u00a0vitro oxidation in age-related human cataract and glutathione depleted mouse lens","volume":"14","author":"Fan","year":"2015","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.jbc.2022.102537_bib196","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/j.exer.2004.05.009","article-title":"Sulfur in human crystallins","volume":"79","author":"Srikanthan","year":"2004","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib197","doi-asserted-by":"crossref","first-page":"108619","DOI":"10.1016\/j.exer.2021.108619","volume":"208","author":"Grosas","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib198","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1038\/s41594-020-00543-9","article-title":"Imbalances in the eye lens proteome are linked to cataract formation","volume":"28","author":"Schmid","year":"2021","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib199","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/0014-4835(91)90145-5","article-title":"Interaction and aggregation of lens crystallins","volume":"53","author":"Liang","year":"1991","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib200","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108705","article-title":"Protein posttranslational modification (PTM) by glycation: role in lens aging and age-related cataractogenesis","volume":"210","author":"Fan","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib201","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108707","article-title":"Redox chemistry of lens crystallins: a system of cysteines","volume":"211","author":"Serebryany","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib202","series-title":"Long-Lived Proteins in Human Aging and Disease","article-title":"Eye lens crystallins: remarkable long-lived proteins","author":"Grosas","year":"2021"},{"key":"10.1016\/j.jbc.2022.102537_bib203","series-title":"Long-lived Proteins in Human Aging and Disease","first-page":"59","article-title":"Eye lens crystallins: remarkable long-lived proteins","author":"Grosas","year":"2021"},{"key":"10.1016\/j.jbc.2022.102537_bib204","doi-asserted-by":"crossref","first-page":"18010","DOI":"10.1074\/jbc.H118.006240","article-title":"\u03b3-Crystallin redox-detox in the lens","volume":"293","author":"Quinlan","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib205","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2020.140446","article-title":"Asp isomerization increases aggregation of \u03b1-crystallin and decreases its chaperone activity in human lens of various ages","volume":"1868","author":"Fujii","year":"2020","journal-title":"Biochim. Biophys. Acta Proteins Proteom"},{"key":"10.1016\/j.jbc.2022.102537_bib206","doi-asserted-by":"crossref","first-page":"1797","DOI":"10.1021\/acs.jproteome.7b00073","article-title":"Identification of sequence similarities among isomerization hotspots in crystallin proteins","volume":"16","author":"Lyon","year":"2017","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.jbc.2022.102537_bib207","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/j.str.2020.11.006","article-title":"Assessing the structures and interactions of \u03b3d-crystallin deamidation variants","volume":"29","author":"Guseman","year":"2021","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2022.102537_bib208","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S0167-4838(01)00258-8","article-title":"Inversion and isomerization of Asp-58 residue in human alphaA-crystallin from normal aged lenses and cataractous lenses","volume":"1549","author":"Fujii","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102537_bib209","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/268071a0","article-title":"Aspartic acid racemisation in the human lens during ageing and in cataract formation","volume":"268","author":"Masters","year":"1977","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102537_bib210","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1002\/cbic.202000739","article-title":"Chemical properties determine solubility and stability in \u03b2\u03b3-crystallins of the eye lens","volume":"22","author":"Rocha","year":"2021","journal-title":"Chembiochem"},{"key":"10.1016\/j.jbc.2022.102537_bib211","doi-asserted-by":"crossref","first-page":"4415","DOI":"10.1038\/s41467-018-06902-x","article-title":"Measuring macromolecular size distributions and interactions at high concentrations by sedimentation velocity","volume":"9","author":"Chaturvedi","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2022.102537_bib212","doi-asserted-by":"crossref","first-page":"2990","DOI":"10.1021\/jacs.8b11371","article-title":"Measuring ultra-weak protein self-association by non-ideal sedimentation velocity","volume":"141","author":"Chaturvedi","year":"2019","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2022.102537_bib213","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1126\/science.aal2674","article-title":"Eye patches: protein assembly of index-gradient squid lenses","volume":"357","author":"Cai","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102537_bib214","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1111\/j.1474-9726.2007.00342.x","article-title":"Presbyopia and heat: changes associated with aging of the human lens suggest a functional role for the small heat shock protein, alpha-crystallin, in maintaining lens flexibility","volume":"6","author":"Heys","year":"2007","journal-title":"Aging Cell"},{"key":"10.1016\/j.jbc.2022.102537_bib215","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/0014-4835(78)90131-8","article-title":"Human insoluble lens protein. II. Isolation and characterization of a 9600 dalton polypeptide","volume":"26","author":"Roy","year":"1978","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib216","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/0014-4835(85)90183-6","article-title":"Spatial and temporal mapping of the age-related changes in human lens crystallins","volume":"41","author":"McFall-Ngai","year":"1985","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib217","doi-asserted-by":"crossref","first-page":"11579","DOI":"10.1074\/jbc.M110.148627","article-title":"The common modification in alphaA-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.jbc.2022.102537_bib218","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1111\/acel.12164","article-title":"Human protein aging: modification and crosslinking through dehydroalanine and dehydrobutyrine intermediates","volume":"13","author":"Wang","year":"2014","journal-title":"Aging Cell"},{"key":"10.1016\/j.jbc.2022.102537_bib219","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":"Moreau","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib220","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1016\/j.str.2017.05.015","article-title":"Crystal structure of chicken \u03b3s-crystallin reveals lattice contacts with implications for function in the lens and the evolution of the \u03b2\u03b3-crystallins","volume":"25","author":"Sagar","year":"2017","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2022.102537_bib221","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1006\/exer.1993.1123","article-title":"Suppression of phase separation in bovine gamma IV crystallin solutions: effect of modification by charged versus uncharged polar groups","volume":"57","author":"Pande","year":"1993","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib222","doi-asserted-by":"crossref","first-page":"731","DOI":"10.3389\/fcell.2020.00731","article-title":"Distribution and function of glycosaminoglycans and proteoglycans in the development, homeostasis and pathology of the ocular surface","volume":"8","author":"Puri","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib223","first-page":"449","article-title":"Observation of protein diffusivity in intact human and bovine lenses with application to cataract","volume":"14","author":"Tanaka","year":"1975","journal-title":"Invest. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib224","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/0014-4835(84)90115-5","article-title":"In\u00a0vivo observation of lens protein diffusivity in normal and X-irradiated rabbit lenses","volume":"39","author":"Nishio","year":"1984","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib225","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2022.108974","article-title":"Alzheimer's disease amyloid-\u03b2 pathology in the lens of the eye","volume":"221","author":"Moncaster","year":"2022","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib226","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1042\/bj20011512","article-title":"Effects of modifications of alpha-crystallin on its chaperone and other properties","volume":"364","author":"Derham","year":"2002","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2022.102537_bib227","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/S0014-4835(03)00156-8","article-title":"Expression of betaA2-crystallin in human lenses","volume":"77","author":"Lapko","year":"2003","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib228","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.bbadis.2011.11.011","article-title":"Acetylation of \u03b1A-crystallin in the human lens: effects on structure and chaperone function","volume":"1822","author":"Nagaraj","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102537_bib229","doi-asserted-by":"crossref","first-page":"7900","DOI":"10.1073\/pnas.122231399","article-title":"Shotgun identification of protein modifications from protein complexes and lens tissue","volume":"99","author":"MacCoss","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102537_bib230","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1167\/iovs.12-11168","article-title":"Proteomics and phosphoproteomics analysis of human lens fiber cell membranes","volume":"54","author":"Wang","year":"2013","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib231","doi-asserted-by":"crossref","first-page":"4127","DOI":"10.1007\/s00018-015-1996-x","article-title":"Regulation of \u03b1A- and \u03b1B-crystallins via phosphorylation in cellular homeostasis","volume":"72","author":"Thornell","year":"2015","journal-title":"Cell Mol. Life Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib232","doi-asserted-by":"crossref","first-page":"17997","DOI":"10.1074\/jbc.RA118.004551","article-title":"Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation","volume":"293","author":"Serebryany","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib233","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.jbc.2022.102537_bib234","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1002\/j.1460-2075.1994.tb06339.x","article-title":"Chaperone activity of alpha-crystallins modulates intermediate filament assembly","volume":"13","author":"Nicholl","year":"1994","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2022.102537_bib235","doi-asserted-by":"crossref","first-page":"1687","DOI":"10.1016\/j.biocel.2012.02.015","article-title":"sHSP in the eye lens: crystallin mutations, cataract and proteostasis","volume":"44","author":"Clark","year":"2012","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib236","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.bbagen.2015.08.014","article-title":"Functional sequences in human alphaB crystallin","volume":"1860","author":"Clark","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102537_bib237","first-page":"10","article-title":"Proctor Lecture. The function of alpha-crystallin","volume":"34","author":"Horwitz","year":"1993","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib238","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1042\/bj3280763","article-title":"Effect of aging on the chaperone-like function of human alpha-crystallin assessed by three methods","volume":"328","author":"Derham","year":"1997","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2022.102537_bib239","doi-asserted-by":"crossref","first-page":"817","DOI":"10.3109\/02713689209000754","article-title":"The ability of lens alpha crystallin to protect against heat-induced aggregation is age-dependent","volume":"11","author":"Horwitz","year":"1992","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib240","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1006\/bbrc.1995.1391","article-title":"Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications","volume":"208","author":"Cherian","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2022.102537_bib241","doi-asserted-by":"crossref","first-page":"4319","DOI":"10.1167\/iovs.09-3522","article-title":"Age-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry","volume":"50","author":"Grey","year":"2009","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib242","doi-asserted-by":"crossref","first-page":"44258","DOI":"10.1074\/jbc.M405648200","article-title":"Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin","volume":"279","author":"Gupta","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib243","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1111\/opo.12426","article-title":"Intraocular light scatter, reflections, fluorescence and absorption: what we see in the slit lamp","volume":"38","author":"van den Berg","year":"2018","journal-title":"Ophthalmic Physiol. Opt."},{"key":"10.1016\/j.jbc.2022.102537_bib244","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1080\/02713683.2017.1343852","article-title":"Natural course of posterior subcapsular cataract over a short time period","volume":"42","author":"Neumayer","year":"2017","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib245","doi-asserted-by":"crossref","first-page":"4986","DOI":"10.1167\/iovs.18-25067","article-title":"Lens epithelial cells initiate an inflammatory response following cataract surgery","volume":"59","author":"Jiang","year":"2018","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib246","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.trsl.2021.05.005","article-title":"Immune responses to injury and their links to eye disease","volume":"236","author":"Stepp","year":"2021","journal-title":"Transl Res."},{"key":"10.1016\/j.jbc.2022.102537_bib247","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1016\/j.it.2008.08.002","article-title":"Immune regulation and the eye","volume":"29","author":"Stein-Streilein","year":"2008","journal-title":"Trends Immunol."},{"key":"10.1016\/j.jbc.2022.102537_bib248","first-page":"1940","article-title":"Ocular immune privilege and the Faustian dilemma. The Proctor lecture","volume":"37","author":"Streilein","year":"1996","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib249","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1615\/CritRevImmunol.v22.i1.20","article-title":"Immune privilege in the anterior chamber of the eye","volume":"22","author":"Niederkorn","year":"2002","journal-title":"Crit. Rev. Immunol."},{"key":"10.1016\/j.jbc.2022.102537_bib250","series-title":"Lens Disorders: A Clinical Manual of Cataract Diagnosis","author":"Brown","year":"1996"},{"key":"10.1016\/j.jbc.2022.102537_bib251","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1016\/0014-4835(90)90097-E","article-title":"Intermediary metabolism of the lens: a historical perspective 1928-1989","volume":"50","author":"Chylack","year":"1990","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib252","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.exer.2012.05.007","article-title":"Osmotic stress, not aldose reductase activity, directly induces growth factors and MAPK signaling changes during sugar cataract formation","volume":"101","author":"Zhang","year":"2012","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib253","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/S0161-6420(84)34252-X","article-title":"Mechanisms of senile cataract formation","volume":"91","author":"Chylack","year":"1984","journal-title":"Ophthalmology"},{"key":"10.1016\/j.jbc.2022.102537_bib254","first-page":"619","article-title":"Pathways of glucose metabolism in the lens","volume":"4","author":"Kinoshita","year":"1965","journal-title":"Invest. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib255","first-page":"502","article-title":"Energy metabolism in the lens during aging","volume":"4","author":"Sippel","year":"1965","journal-title":"Invest. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib256","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/0014-4835(88)90027-9","article-title":"Phosphorus and proton magnetic resonance spectroscopic studies on the relationship between transparency and glucose metabolism in the rabbit lens","volume":"47","author":"Williams","year":"1988","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib257","doi-asserted-by":"crossref","first-page":"e76923","DOI":"10.7554\/eLife.76923","article-title":"A native chemical chaperone in the human eye lens","volume":"11","author":"Serebryany","year":"2022","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2022.102537_bib258","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1016\/S0006-3495(99)77013-X","article-title":"Swelling studies on the cornea and\u00a0sclera: the effects of pH and ionic strength","volume":"77","author":"Huang","year":"1999","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102537_bib259","first-page":"501","article-title":"Structural alterations affecting transparency in swollen human corneas","volume":"7","author":"Goldman","year":"1968","journal-title":"Invest. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib260","first-page":"574","article-title":"The relationship between morphology and transparency in the nonswelling corneal stroma of the shark","volume":"6","author":"Goldman","year":"1967","journal-title":"Invest. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib261","series-title":"The Ocular Lens: Structure, Function, and Pathology","first-page":"265","article-title":"Physical basis of lens transparency","author":"Bettelheim","year":"1985"},{"key":"10.1016\/j.jbc.2022.102537_bib262","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00232-007-9019-y","article-title":"The lens circulation","volume":"216","author":"Mathias","year":"2007","journal-title":"J.\u00a0Membr. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib263","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/0014-4835(80)90124-4","article-title":"Philly mouse: a new model of hereditary cataract","volume":"30","author":"Kador","year":"1980","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib264","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1001\/archopht.1968.03850040613022","article-title":"Experimental miotic cataract. II. Permeability, cation transport, and intermediary metabolism","volume":"79","author":"Michon","year":"1968","journal-title":"Arch. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib265","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1042\/bj0560372","article-title":"Changes in lens during the formation of x-ray cataract in rabbits. II","volume":"56","author":"Van Heyningen","year":"1954","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2022.102537_bib266","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1038\/216503a0","article-title":"Difference in swelling and opacity formation between young and old lenses","volume":"216","author":"Pirie","year":"1967","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102537_bib267","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1136\/bjo.73.7.522","article-title":"Dynamic nature of posterior subcapsular cataract","volume":"73","author":"Adrien Shun-Shin","year":"1989","journal-title":"Br. J. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib268","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/S0002-9394(14)73929-7","article-title":"Transient posterior subcapsular lens opacities in diabetes mellitus","volume":"115","author":"Dickey","year":"1993","journal-title":"Am. J. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib269","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.preteyeres.2016.04.006","article-title":"Aldose reductase, ocular diabetic complications and the development of topical Kinostat(\u00ae)","volume":"54","author":"Kador","year":"2016","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib270","doi-asserted-by":"crossref","first-page":"R263","DOI":"10.1152\/ajpregu.00309.2021","article-title":"Intracellular hydrostatic pressure regulation in the bovine lens: a role in the regulation of lens optics?","volume":"322","author":"Chen","year":"2022","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib271","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/j.bbrc.2015.04.138","article-title":"Role of Aquaporin 0 in lens biomechanics","volume":"462","author":"Kumari","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2022.102537_bib272","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0006-3495(79)85284-4","article-title":"Electrical properties of structural components of the crystalline lens","volume":"25","author":"Mathias","year":"1979","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102537_bib273","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1113\/jphysiol.1976.sp011596","article-title":"Current-voltage relationships in the crystalline lens","volume":"262","author":"Eisenberg","year":"1976","journal-title":"J.\u00a0Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib274","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1113\/jphysiol.1980.sp013461","article-title":"Characteristics of voltage-dependent conductance in the membranes of a non-excitable tissue: the amphibian lens","volume":"308","author":"Delamere","year":"1980","journal-title":"J.\u00a0Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib275","doi-asserted-by":"crossref","first-page":"2202","DOI":"10.1002\/jcp.26074","article-title":"Endogenous bioelectric currents promote differentiation of the mammalian lens","volume":"233","author":"Cao","year":"2018","journal-title":"J.\u00a0Cell Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib276","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0014-4835(02)00257-9","article-title":"Bi-directional migration of lens epithelial cells in a physiological electrical field","volume":"76","author":"Wang","year":"2003","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib277","doi-asserted-by":"crossref","DOI":"10.3389\/fphys.2021.818649","article-title":"Physiological mechanisms regulating lens transport","volume":"12","author":"Giannone","year":"2021","journal-title":"Front. Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib278","doi-asserted-by":"crossref","DOI":"10.1098\/rsob.150011","article-title":"Nonlinear ionizing radiation-induced changes in eye lens cell proliferation, cyclin D1 expression and lens shape","volume":"5","author":"Markiewicz","year":"2015","journal-title":"Open Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib279","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.exer.2015.11.017","article-title":"Breakdown of interlocking domains may contribute to formation of membranous globules and lens opacity in ephrin-A5(-\/-) mice","volume":"145","author":"Biswas","year":"2016","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib280","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.exer.2014.07.020","article-title":"Regional changes of AQP0-dependent square array junction and gap junction associated with cortical cataract formation in the Emory mutant mouse","volume":"127","author":"Biswas","year":"2014","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib281","doi-asserted-by":"crossref","first-page":"e58149","DOI":"10.7554\/eLife.58149","article-title":"Keratins and the plakin family cytolinker proteins control the length of epithelial microridge protrusions","volume":"9","author":"Inaba","year":"2020","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2022.102537_bib282","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.201904144","article-title":"Cortical contraction drives the 3D patterning of epithelial cell surfaces","volume":"219","author":"van Loon","year":"2020","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib283","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1006\/dbio.1996.0328","article-title":"Lens-specific expression of PDGF-A alters lens growth and development","volume":"180","author":"Reneker","year":"1996","journal-title":"Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib284","doi-asserted-by":"crossref","first-page":"1573","DOI":"10.1242\/dev.081042","article-title":"MAPK1 is required for establishing the pattern of cell proliferation and for cell survival during lens development","volume":"140","author":"Upadhya","year":"2013","journal-title":"Development"},{"key":"10.1016\/j.jbc.2022.102537_bib285","doi-asserted-by":"crossref","DOI":"10.1098\/rsob.210265","article-title":"Jack of all trades, master of each: the diversity of fibroblast growth factor signalling in eye development","volume":"12","author":"Makrides","year":"2022","journal-title":"Open Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib286","doi-asserted-by":"crossref","DOI":"10.3389\/fphys.2020.608812","article-title":"Insights into the early gene regulatory network controlling neural crest and placode fate choices at the neural border","volume":"11","author":"Seal","year":"2020","journal-title":"Front. Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib287","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1242\/dev.115.1.123","article-title":"Regulation and role of PDGF receptor alpha-subunit expression during embryogenesis","volume":"115","author":"Schatteman","year":"1992","journal-title":"Development"},{"key":"10.1016\/j.jbc.2022.102537_bib288","first-page":"560","article-title":"Effect of age on cell division, 3H-thymidine incorporation, and diurnal rhythm in the lens epithelium of rats","volume":"5","author":"von Sallmann","year":"1966","journal-title":"Invest. Ophthalmol."},{"key":"10.1016\/j.jbc.2022.102537_bib289","doi-asserted-by":"crossref","first-page":"e1","DOI":"10.1016\/j.preteyeres.2016.09.002","article-title":"The physiological optics of the lens","volume":"56","author":"Donaldson","year":"2017","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib290","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/j.preteyeres.2012.03.001","article-title":"The gradient index lens of the eye: an opto-biological synchrony","volume":"31","author":"Pierscionek","year":"2012","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib291","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.exer.2014.05.009","article-title":"Optical properties of the lens: an explanation for the zones of discontinuity","volume":"124","author":"Bahrami","year":"2014","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib292","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.exer.2015.08.011","article-title":"Refractive index degeneration in older lenses: a potential functional correlate to structural changes that underlie cataract formation","volume":"140","author":"Bahrami","year":"2015","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib293","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.exer.2013.12.004","article-title":"A\u00a0gradient of matrix-bound FGF-2 and perlecan is available to lens epithelial cells","volume":"120","author":"Wu","year":"2014","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib294","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/0012-1606(92)90138-7","article-title":"Cell cycle synchrony in the developing chicken lens epithelium","volume":"152","author":"Brewitt","year":"1992","journal-title":"Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib295","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1002\/jcp.1041500320","article-title":"Periods of oscillatory growth in developing ocular lens correspond with cell cycle times","volume":"150","author":"Brewitt","year":"1992","journal-title":"J.\u00a0Cell Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib296","doi-asserted-by":"crossref","first-page":"6943","DOI":"10.3390\/ijms21186943","article-title":"Lens connexin channels show differential permeability to signaling molecules","volume":"21","author":"Brink","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib297","first-page":"410","article-title":"Growth of the eye lens: I. Weight accumulation in multiple species","volume":"20","author":"Augusteyn","year":"2014","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib298","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108564","article-title":"Crystallin gene expression: insights from studies of transcriptional bursting","volume":"207","author":"Cvekl","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib299","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1111\/j.1432-0436.1981.tb01141.x","article-title":"Lens differentiation in vertebrates. A review of cellular and molecular features","volume":"19","author":"Piatigorsky","year":"1981","journal-title":"Differentiation"},{"key":"10.1016\/j.jbc.2022.102537_bib300","doi-asserted-by":"crossref","DOI":"10.1098\/rsif.2015.0391","article-title":"A\u00a0dimensionless ordered pull-through model of the mammalian lens epithelium evidences scaling across species and explains the age-dependent changes in cell density in the human lens","volume":"12","author":"Wu","year":"2015","journal-title":"J.\u00a0R. Soc. Interf."},{"key":"10.1016\/j.jbc.2022.102537_bib301","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1016\/S0014-4835(62)80037-2","article-title":"Aspects of mitotic activity in relation to cell proliferation in the lens epithelium","volume":"1","author":"Von Sallmann","year":"1962","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib302","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1126\/science.3187521","article-title":"Growth and transparency in the lens, an epithelial tissue, stimulated by pulses of PDGF","volume":"242","author":"Brewitt","year":"1988","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102537_bib303","doi-asserted-by":"crossref","first-page":"2606","DOI":"10.3390\/cells10102606","article-title":"Mutation of the EPHA2 tyrosine-kinase domain dysregulates cell pattern formation and cytoskeletal gene expression in the lens","volume":"10","author":"Zhou","year":"2021","journal-title":"Cells"},{"key":"10.1016\/j.jbc.2022.102537_bib304","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108662","article-title":"Inherited cataracts: genetic mechanisms and pathways new and old","volume":"209","author":"Shiels","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib305","series-title":"On Growth and Form","author":"Thompson","year":"1917"},{"key":"10.1016\/j.jbc.2022.102537_bib306","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2113883119","article-title":"Symmetry and simplicity spontaneously emerge from the algorithmic nature of evolution","volume":"119","author":"Johnston","year":"2022","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102537_bib307","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1038\/s41588-021-00970-4","article-title":"Discovery of a genetic module essential for assigning left-right asymmetry in humans and ancestral vertebrates","volume":"54","author":"Szenker-Ravi","year":"2022","journal-title":"Nat. Genet."},{"key":"10.1016\/j.jbc.2022.102537_bib308","doi-asserted-by":"crossref","DOI":"10.3389\/fphys.2021.772276","article-title":"Eph-ephrin signaling affects eye lens fiber cell intracellular voltage and membrane conductance","volume":"12","author":"Cheng","year":"2021","journal-title":"Front. Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib309","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1016\/j.bpj.2019.02.007","article-title":"A\u00a0bidomain model for lens microcirculation","volume":"116","author":"Zhu","year":"2019","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102537_bib310","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1111\/j.1432-0436.1980.tb01091.x","article-title":"Induction of the eye lens","volume":"17","author":"McAvoy","year":"1980","journal-title":"Differentiation"},{"key":"10.1016\/j.jbc.2022.102537_bib311","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ydbio.2005.01.020","article-title":"Growth factor regulation of lens development","volume":"280","author":"Lovicu","year":"2005","journal-title":"Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib312","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1080\/07315724.1993.10718294","article-title":"Cataract: relationship between nutrition and oxidation","volume":"12","author":"Taylor","year":"1993","journal-title":"J.\u00a0Am. Coll. Nutr."},{"key":"10.1016\/j.jbc.2022.102537_bib313","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.preteyeres.2017.04.001","article-title":"The lens growth process","volume":"60","author":"Bassnett","year":"2017","journal-title":"Prog. Retin. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib314","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/S1043-4682(10)80007-8","article-title":"The crystalline lens. A system networked by gap junctional intercellular communication","volume":"3","author":"Goodenough","year":"1992","journal-title":"Sem. Cell Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib315","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1242\/jcs.045203","article-title":"The stratified syncytium of the vertebrate lens","volume":"122","author":"Shi","year":"2009","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib316","doi-asserted-by":"crossref","first-page":"4222","DOI":"10.1091\/mbc.e06-05-0416","article-title":"FGF-2 release from the lens capsule by MMP-2 maintains lens epithelial cell viability","volume":"18","author":"Tholozan","year":"2007","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.jbc.2022.102537_bib317","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108808","article-title":"The importance of the epithelial fibre cell interface to lens regeneration in an in\u00a0vivo rat model and in a human bag-in-the-lens (BiL) sample","volume":"213","author":"Wu","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib318","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1167\/iovs.14-16028","article-title":"The penny pusher: a cellular model of lens growth","volume":"56","author":"Shi","year":"2015","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib319","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1002\/jcp.1041070302","article-title":"Cell population kinetics of the mouse lens epithelium","volume":"107","author":"Rafferty","year":"1981","journal-title":"J.\u00a0Cell Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib320","doi-asserted-by":"crossref","first-page":"1830","DOI":"10.1016\/j.bpj.2015.09.018","article-title":"Feedback regulation of intracellular hydrostatic pressure in surface cells of the lens","volume":"109","author":"Gao","year":"2015","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102537_bib321","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1167\/iovs.61.6.58","article-title":"Signaling between TRPV1\/TRPV4 and intracellular hydrostatic pressure in the mouse lens","volume":"61","author":"Delamere","year":"2020","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib322","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.1194\/jlr.R004119","article-title":"Lipids and the ocular lens","volume":"51","author":"Borchman","year":"2010","journal-title":"J.\u00a0lipid Res."},{"key":"10.1016\/j.jbc.2022.102537_bib323","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108536","article-title":"Differences in the properties of porcine cortical and nuclear fiber cell plasma membranes revealed by saturation recovery EPR spin labeling measurements","volume":"206","author":"Stein","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib324","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/j.bbamem.2017.10.020","article-title":"Is the cholesterol bilayer domain a barrier to oxygen transport into the eye lens?","volume":"1860","author":"Plesnar","year":"2018","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102537_bib325","doi-asserted-by":"crossref","first-page":"533","DOI":"10.3109\/02713689609000764","article-title":"Fiber cell morphology and cytoplasmic texture in cataractous and normal human lens nuclei","volume":"15","author":"al-Ghoul","year":"1996","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib326","doi-asserted-by":"crossref","first-page":"30532","DOI":"10.18632\/oncotarget.5762","article-title":"The eye lens: age-related trends and individual variations in refractive index and shape parameters","volume":"6","author":"Pierscionek","year":"2015","journal-title":"Oncotarget"},{"key":"10.1016\/j.jbc.2022.102537_bib327","doi-asserted-by":"crossref","first-page":"C115","DOI":"10.1152\/ajpcell.00111.2015","article-title":"Ankyrin-B directs membrane tethering of periaxin and is required for maintenance of lens fiber cell hexagonal shape and mechanics","volume":"310","author":"Maddala","year":"2016","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"10.1016\/j.jbc.2022.102537_bib328","doi-asserted-by":"crossref","first-page":"3437","DOI":"10.1242\/jcs.202168","article-title":"A\u00a0rim-and-spoke hypothesis to explain the biomechanical roles for cytoplasmic intermediate filament networks","volume":"130","author":"Quinlan","year":"2017","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib329","doi-asserted-by":"crossref","first-page":"801","DOI":"10.3109\/02713689209000753","article-title":"Selective association of crystallins with lens 'native' membrane during dynamic cataractogenesis","volume":"11","author":"Cenedella","year":"1992","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib330","doi-asserted-by":"crossref","first-page":"8349","DOI":"10.1167\/iovs.15-18273","article-title":"Proteomic analysis of lipid Raft-like detergent-resistant membranes of lens fiber cells","volume":"56","author":"Wang","year":"2015","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib331","doi-asserted-by":"crossref","first-page":"3484","DOI":"10.1073\/pnas.73.10.3484","article-title":"Absence of low-molecular-weight alpha crystallin in nuclear region of old human lenses","volume":"73","author":"Roy","year":"1976","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102537_bib332","doi-asserted-by":"crossref","first-page":"2763","DOI":"10.1016\/j.bbamem.2016.06.026","article-title":"The lipidation profile of aquaporin-0 correlates with the acyl composition of phosphoethanolamine lipids in lens membranes","volume":"1858","author":"Ismail","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102537_bib333","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1006\/exer.1996.0130","article-title":"Binding capacity of alpha-crystallin to bovine lens lipids","volume":"63","author":"Borchman","year":"1996","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib334","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1080\/02713683.2020.1786131","article-title":"Interaction of alpha-crystallin with phospholipid membranes","volume":"46","author":"Mainali","year":"2021","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib335","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1167\/iovs.62.12.25","article-title":"Spatially resolved proteomic analysis of the lens extracellular diffusion barrier","volume":"62","author":"Wang","year":"2021","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib336","doi-asserted-by":"crossref","first-page":"1202","DOI":"10.1167\/iovs.13-13379","article-title":"Aquaporin-0 targets interlocking domains to control the integrity and transparency of the eye lens","volume":"55","author":"Lo","year":"2014","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib337","doi-asserted-by":"crossref","first-page":"4021","DOI":"10.1167\/iovs.18-26270","article-title":"Connexin 50 and AQP0 are essential in maintaining organization and integrity of lens fibers","volume":"60","author":"Gu","year":"2019","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib338","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/S0014-4835(03)00192-1","article-title":"Insertion of MP20 into lens fibre cell plasma membranes correlates with the formation of an extracellular diffusion barrier","volume":"77","author":"Grey","year":"2003","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib339","doi-asserted-by":"crossref","DOI":"10.1194\/jlr.TR120000874","article-title":"Lipid conformational order and the etiology of cataract and dry eye","volume":"62","author":"Borchman","year":"2021","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.jbc.2022.102537_bib340","doi-asserted-by":"crossref","first-page":"2289","DOI":"10.1194\/jlr.M079368","article-title":"Whales, lifespan, phospholipids, and cataracts","volume":"58","author":"Borchman","year":"2017","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.jbc.2022.102537_bib341","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.exer.2012.01.012","article-title":"Properties of fiber cell plasma membranes isolated from the cortex and nucleus of the porcine eye lens","volume":"97","author":"Mainali","year":"2012","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib342","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1007\/978-3-319-55231-6_5","article-title":"Factors determining the oxygen permeability of biological membranes: oxygen transport across eye lens fiber-cell plasma membranes","volume":"977","author":"Subczynski","year":"2017","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib343","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1007\/s00232-011-9412-4","article-title":"Functions of cholesterol and the cholesterol bilayer domain specific to the fiber-cell plasma membrane of the eye lens","volume":"245","author":"Subczynski","year":"2012","journal-title":"J.\u00a0Membr. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib344","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/0014-4835(72)90136-4","article-title":"Electron microscope observations on some structural proteins of the chick lens","volume":"14","author":"Maisel","year":"1972","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib345","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.3109\/02713688809033228","article-title":"Immunochemical characterization of a Mr 115 lens fiber cell-specific extrinsic membrane protein","volume":"7","author":"FitzGerald","year":"1988","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib346","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.ydbio.2011.06.036","article-title":"Periaxin is required for hexagonal geometry and membrane organization of mature lens fibers","volume":"357","author":"Maddala","year":"2011","journal-title":"Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib347","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/j.ydbio.2010.10.009","article-title":"Modulation of N-cadherin junctions and their role as epicenters of differentiation-specific actin regulation in the developing lens","volume":"349","author":"Leonard","year":"2011","journal-title":"Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib348","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/S0014-5793(03)00711-7","article-title":"Tropomodulin binds to filensin intermediate filaments","volume":"547","author":"Fischer","year":"2003","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2022.102537_bib349","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.exer.2016.03.005","article-title":"The lens actin filament cytoskeleton: diverse structures for complex functions","volume":"156","author":"Cheng","year":"2017","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib350","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1016\/j.ydbio.2006.03.056","article-title":"Actin filament organization regulates the induction of lens cell differentiation and survival","volume":"295","author":"Weber","year":"2006","journal-title":"Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib351","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1073\/pnas.52.4.1091","article-title":"Oriented microtubules in elongating cells of the developing lens rudiment after induction","volume":"52","author":"Byers","year":"1964","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102537_bib352","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1016\/S0022-5320(66)80080-1","article-title":"On the occurrence of microtubules in the developing lens of the squid Loligo pealii","volume":"14","author":"Arnold","year":"1966","journal-title":"J.\u00a0Ultrastruct. Res."},{"key":"10.1016\/j.jbc.2022.102537_bib353","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1083\/jcb.55.1.82","article-title":"Cell elongation in the cultured embryonic chick lens epithelium with and without protein synthesis","volume":"55","author":"Piatigorsky","year":"1972","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib354","series-title":"Principles of Biomolecular Organization","article-title":"Cytoplasmic microtubules and their function","author":"Porter","year":"1966"},{"key":"10.1016\/j.jbc.2022.102537_bib355","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1126\/science.493982","article-title":"Lens epithelial cell elongation in the absence of microtubules: evidence for a new effect of colchicine","volume":"206","author":"Beebe","year":"1979","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102537_bib356","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1016\/j.exer.2005.04.009","article-title":"Three-dimensional reconstruction of cells in the living lens: the relationship between cell length and volume","volume":"81","author":"Bassnett","year":"2005","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib357","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/S0014-4835(03)00176-3","article-title":"Microtubule configuration and membranous vesicle transport in elongating fiber cells of the rat lens","volume":"77","author":"Lo","year":"2003","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib358","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.exer.2016.03.016","article-title":"The molecular mechanisms underlying lens fiber elongation","volume":"156","author":"Audette","year":"2017","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib359","doi-asserted-by":"crossref","first-page":"10446","DOI":"10.1073\/pnas.162055899","article-title":"Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells","volume":"99","author":"Lauf","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102537_bib360","doi-asserted-by":"crossref","first-page":"85","DOI":"10.3390\/genes7100085","article-title":"Congenital cataracts and gut dysmotility in a DYNC1H1 dyneinopathy patient","volume":"7","author":"Gelineau-Morel","year":"2016","journal-title":"Genes (Basel)"},{"key":"10.1016\/j.jbc.2022.102537_bib361","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.32586","article-title":"Crk proteins transduce FGF signaling to promote lens fiber cell elongation","volume":"7","author":"Collins","year":"2018","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2022.102537_bib362","doi-asserted-by":"crossref","first-page":"4976","DOI":"10.1073\/pnas.72.12.4976","article-title":"Membrane-microtubule interactions: concanavalin A capping induced redistribution of cytoplasmic microtubules and colchicine binding proteins","volume":"72","author":"Albertini","year":"1975","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102537_bib363","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2019.02.001","article-title":"BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability","volume":"185","author":"Tapodi","year":"2019","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib364","doi-asserted-by":"crossref","first-page":"6006","DOI":"10.1167\/iovs.17-22153","article-title":"Aquaporin 0 modulates lens gap junctions in the presence of lens-specific beaded filament proteins","volume":"58","author":"Kumari","year":"2017","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib365","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108645","article-title":"Deletion of beaded filament proteins or the C-terminal end of Aquaporin 0 causes analogous abnormal distortion aberrations in mouse lens","volume":"209","author":"Varadaraj","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib366","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.yexcr.2004.11.021","article-title":"Seeing is believing! the optical properties of the eye lens are dependent upon a functional intermediate filament cytoskeleton","volume":"305","author":"Perng","year":"2005","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.jbc.2022.102537_bib367","doi-asserted-by":"crossref","first-page":"801","DOI":"10.3109\/02713688909000870","article-title":"The Mr 115 kd fiber cell-specific protein is a component of the lens cytoskeleton","volume":"8","author":"FitzGerald","year":"1989","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib368","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0014-4835(95)80009-3","article-title":"In\u00a0vitro studies on the assembly properties of the lens beaded filament proteins: co-assembly with a-crystallin but not with vimentin","volume":"60","author":"Carter","year":"1995","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib369","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/S0014-4835(02)00330-5","article-title":"Knockout of the intermediate filament protein CP49 destabilises the lens fibre cell cytoskeleton and decreases lens optical quality, but does not induce cataract","volume":"76","author":"Sandilands","year":"2003","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib370","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-020-73625-9","article-title":"Three-dimensional data capture and analysis of intact eye lenses evidences emmetropia-associated changes in epithelial cell organization","volume":"10","author":"Kalligeraki","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2022.102537_bib371","first-page":"970","article-title":"Expression of the type VI intermediate filament proteins CP49 and filensin in the mouse lens epithelium","volume":"22","author":"FitzGerald","year":"2016","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib372","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1002\/cm.970090104","article-title":"Actin filament patterns in mouse lens epithelium: a study of the effects of aging, injury, and genetics","volume":"9","author":"Liou","year":"1988","journal-title":"Cell Motil. Cytoskeleton"},{"key":"10.1016\/j.jbc.2022.102537_bib373","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1038\/eye.1999.116","article-title":"Lens cytoskeleton and transparency: a model","volume":"13","author":"Clark","year":"1999","journal-title":"Eye (Lond)"},{"key":"10.1016\/j.jbc.2022.102537_bib374","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1006\/exer.1996.0220","article-title":"Loss of cytoskeletal proteins and lens cell opacification in the selenite cataract model","volume":"64","author":"Matsushima","year":"1997","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib375","series-title":"Cytoskeletal Competence Requires Protein Chaperones","author":"Quinlan","year":"2002"},{"key":"10.1016\/j.jbc.2022.102537_bib376","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2020.618733","article-title":"Complex interactions between membrane-bound organelles, biomolecular condensates and the cytoskeleton","volume":"8","author":"Koppers","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib377","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1042\/ETLS20190174","article-title":"Drops and fibers - how biomolecular condensates and cytoskeletal filaments influence each other","volume":"4","author":"Wiegand","year":"2020","journal-title":"Emerg. Top Life Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib378","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1038\/nrm3753","article-title":"Post-translational modifications of intermediate filament proteins: mechanisms and functions","volume":"15","author":"Snider","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib379","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2021.102014","article-title":"Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress","volume":"44","author":"Griesser","year":"2021","journal-title":"Redox Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib380","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2022.864191","article-title":"Post-translational modification of lamins: mechanisms and functions","volume":"10","author":"Zheng","year":"2022","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib381","doi-asserted-by":"crossref","first-page":"3860","DOI":"10.1167\/iovs.10-6231","article-title":"Intermediate filaments regulate tissue size and stiffness in the murine lens","volume":"52","author":"Fudge","year":"2011","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib382","doi-asserted-by":"crossref","first-page":"4985","DOI":"10.1242\/jcs.00815","article-title":"A\u00a0novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells","volume":"116","author":"Straub","year":"2003","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib383","first-page":"301","article-title":"Plakoglobin is a component of the filamentous subplasmalemmal coat of lens cells","volume":"43","author":"Franke","year":"1987","journal-title":"Eur. J. Cell Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib384","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/0014-4827(80)90437-1","article-title":"Identification of the cytoskeletal proteins in lens-forming cells, a special epitheloid cell type","volume":"127","author":"Ramaekers","year":"1980","journal-title":"Exp. Cell Res,"},{"key":"10.1016\/j.jbc.2022.102537_bib385","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1016\/j.tcb.2020.03.005","article-title":"Actin cell cortex: structure and molecular organization","volume":"30","author":"Svitkina","year":"2020","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.jbc.2022.102537_bib386","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.exer.2017.02.012","article-title":"Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin","volume":"159","author":"Wang","year":"2017","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib387","doi-asserted-by":"crossref","first-page":"1562","DOI":"10.1167\/iovs.05-1313","article-title":"The C terminus of lens aquaporin 0 interacts with the cytoskeletal proteins filensin and CP49","volume":"47","author":"Lindsey Rose","year":"2006","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib388","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."},{"key":"10.1016\/j.jbc.2022.102537_bib389","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.jbc.2022.102537_bib390","doi-asserted-by":"crossref","first-page":"3595","DOI":"10.1038\/s41467-021-23873-8","article-title":"A\u00a0large multiethnic GWAS meta-analysis of cataract identifies new risk loci and sex-specific effects","volume":"12","author":"Choquet","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2022.102537_bib391","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1080\/13816810.2021.1998556","article-title":"Pathogenic variants in the CYP21A2 gene cause isolated autosomal dominant congenital posterior polar cataracts","volume":"43","author":"Berry","year":"2021","journal-title":"Ophthal. Genet."},{"key":"10.1016\/j.jbc.2022.102537_bib392","first-page":"601","article-title":"The heritability of age-related cortical cataract: the twin eye study","volume":"42","author":"Hammond","year":"2001","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib393","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1167\/iovs.08-2385","article-title":"Estimating heritability and shared environmental effects for refractive error in twin and family studies","volume":"50","author":"Lopes","year":"2009","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib394","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1016\/S0047-6374(01)00419-5","article-title":"Evolution of ageing","volume":"123","author":"Kirkwood","year":"2002","journal-title":"Mech. ageing Dev."},{"key":"10.1016\/j.jbc.2022.102537_bib395","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2102088118","article-title":"Aging as a consequence of selection to reduce the environmental risk of dying","volume":"118","author":"Omholt","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102537_bib396","doi-asserted-by":"crossref","DOI":"10.1098\/rsfs.2015.0079","article-title":"Understanding the physiology of the ageing individual: computational modelling of changes in metabolism and endurance","volume":"6","author":"van Beek","year":"2016","journal-title":"Interf. Focus"},{"key":"10.1016\/j.jbc.2022.102537_bib397","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1186\/s13072-022-00440-z","article-title":"Changes in DNA methylation hallmark alterations in chromatin accessibility and gene expression for eye lens differentiation","volume":"15","author":"Disatham","year":"2022","journal-title":"Epigenetics Chromatin"},{"key":"10.1016\/j.jbc.2022.102537_bib398","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108889","article-title":"RNA-binding proteins and post-transcriptional regulation in lens biology and cataract: mediating spatiotemporal expression of key factors that control the cell cycle, transcription, cytoskeleton and transparency","volume":"214","author":"Lachke","year":"2022","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib399","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1186\/s12920-019-0560-1","article-title":"Analysis of genetic networks regulating refractive eye development in collaborative cross progenitor strain mice reveals new genes and pathways underlying human myopia","volume":"12","author":"Tkatchenko","year":"2019","journal-title":"BMC Med. Genomics"},{"key":"10.1016\/j.jbc.2022.102537_bib400","doi-asserted-by":"crossref","first-page":"2780","DOI":"10.1016\/j.ygeno.2021.06.021","article-title":"Genetic network regulating visual acuity makes limited contribution to visually guided eye emmetropization","volume":"113","author":"Tkatchenko","year":"2021","journal-title":"Genomics"},{"key":"10.1016\/j.jbc.2022.102537_bib401","doi-asserted-by":"crossref","DOI":"10.1016\/j.dib.2020.106657","article-title":"Single cell RNA-sequencing data generated from human pluripotent stem cell-derived lens epithelial cells","volume":"34","author":"Shparberg","year":"2021","journal-title":"Data Brief"},{"key":"10.1016\/j.jbc.2022.102537_bib402","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.68490","article-title":"Correlative all-optical quantification of mass density and mechanics of subcellular compartments with fluorescence specificity","volume":"11","author":"Schl\u00fc\u00dfler","year":"2022","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2022.102537_bib403","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1002\/jbio.201500273","article-title":"Cell nuclei have lower refractive index and mass density than cytoplasm","volume":"9","author":"Sch\u00fcrmann","year":"2016","journal-title":"J.\u00a0Biophotonics"},{"key":"10.1016\/j.jbc.2022.102537_bib404","first-page":"2294","article-title":"A\u00a0method for determining cell number in the undisturbed epithelium of the mouse lens","volume":"16","author":"Bassnett","year":"2010","journal-title":"Mol. Vis."},{"key":"10.1016\/j.jbc.2022.102537_bib405","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1038\/s41586-022-04618-z","article-title":"Somatic mutation rates scale with lifespan across mammals","volume":"604","author":"Cagan","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102537_bib406","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2021.108535","article-title":"Single cell transcriptomics of the developing zebrafish lens and identification of putative controllers of lens development","volume":"206","author":"Farnsworth","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib407","doi-asserted-by":"crossref","first-page":"13530","DOI":"10.1074\/jbc.RA119.008853","article-title":"Transcriptional profiling of single fiber cells in a transgenic paradigm of an inherited childhood cataract reveals absence of molecular heterogeneity","volume":"294","author":"Bhat","year":"2019","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102537_bib408","article-title":"The aging mouse lens transcriptome","volume":"209","author":"Faranda","year":"2021","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.jbc.2022.102537_bib409","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1016\/j.cell.2016.07.050","article-title":"Epigenetic mechanisms of longevity and aging","volume":"166","author":"Sen","year":"2016","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2022.102537_bib410","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.1007\/s00439-013-1342-z","article-title":"Genetics of healthy aging and longevity","volume":"132","author":"Brooks-Wilson","year":"2013","journal-title":"Hum. Genet."},{"key":"10.1016\/j.jbc.2022.102537_bib411","doi-asserted-by":"crossref","first-page":"917","DOI":"10.3390\/cells11050917","article-title":"A\u00a0mechanistic theory of development-aging continuity in humans and other mammals","volume":"11","author":"Walker","year":"2022","journal-title":"Cells"},{"key":"10.1016\/j.jbc.2022.102537_bib412","first-page":"736","article-title":"Protective effects of familial longevity decrease with age and become negligible for centenarians","volume":"77","author":"Gavrilova","year":"2022","journal-title":"J.\u00a0Gerontol. Ser. A, Biol. Sci. Med. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib413","doi-asserted-by":"crossref","first-page":"7398","DOI":"10.1167\/iovs.15-18117","article-title":"MALDI imaging mass spectrometry spatially maps age-related deamidation and truncation of human lens aquaporin-0","volume":"56","author":"Wenke","year":"2015","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.jbc.2022.102537_bib414","doi-asserted-by":"crossref","first-page":"3241","DOI":"10.1038\/s41467-021-23461-w","article-title":"Automated annotation and visualisation of high-resolution spatial proteomic mass spectrometry imaging data using HIT-MAP","volume":"12","author":"Guo","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2022.102537_bib415","doi-asserted-by":"crossref","first-page":"e4473","DOI":"10.1002\/jms.4473","article-title":"MALDI imaging mass spectrometry of \u03b2- and \u03b3-crystallins in the ocular lens","volume":"55","author":"Anderson","year":"2020","journal-title":"J.\u00a0Mass Spectrom."},{"key":"10.1016\/j.jbc.2022.102537_bib416","doi-asserted-by":"crossref","first-page":"4462","DOI":"10.1364\/BOE.10.004462","article-title":"Development of an in\u00a0vivo magnetic resonance imaging and computer modelling platform to investigate the physiological optics of the crystalline lens","volume":"10","author":"Pan","year":"2019","journal-title":"Biomed. Opt. Express"},{"key":"10.1016\/j.jbc.2022.102537_bib417","doi-asserted-by":"crossref","first-page":"2851","DOI":"10.1167\/iovs.15-18413","article-title":"Protein disulfide levels and lens elasticity modulation: applications for presbyopia","volume":"57","author":"Garner","year":"2016","journal-title":"Invest Ophthalmol Vis Sci"},{"key":"10.1016\/j.jbc.2022.102537_bib418","doi-asserted-by":"crossref","first-page":"102417","DOI":"10.1016\/j.jbc.2022.102417","article-title":"\u03b1-Crystallin chaperone mimetic drugs inhibit lens \u03b3-crystallin aggregation: Potential role for cataract prevention","volume":"298","author":"Islam","year":"2022","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jbc.2022.102537_bib419","series-title":"Albert and Jakobiec's Principles and Practice of Ophthalmology","article-title":"Biology of the transparent lens and changes with age","author":"Clark","year":"2021"},{"key":"10.1016\/j.jbc.2022.102537_bib420","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1038\/scientificamerican0788-92","article-title":"How the human eye focuses","volume":"259","author":"JF Koretz","year":"1988","journal-title":"Sci. Am."},{"key":"10.1016\/j.jbc.2022.102537_bib421","first-page":"88","article-title":"The effect of age on the radiosensitivity of rat lenses","volume":"71","author":"Merriam","year":"1973","journal-title":"Trans. Am. Ophthalmol. Soc."},{"key":"10.1016\/j.jbc.2022.102537_bib422","first-page":"372","article-title":"Experimental radiation cataract--its clinical relevance","volume":"59","author":"Merriam","year":"1983","journal-title":"Bull N. Y Acad. Med."},{"key":"10.1016\/j.jbc.2022.102537_bib423","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1159\/000266570","article-title":"Characterization of the equatorial current of the lens","volume":"20","author":"Patterson","year":"1988","journal-title":"Ophthalmic Res."},{"key":"10.1016\/j.jbc.2022.102537_bib424","doi-asserted-by":"crossref","first-page":"e4159","DOI":"10.1371\/journal.pone.0004159","article-title":"Identification of pax6-dependent gene regulatory networks in the mouse lens","volume":"4","author":"Wolf","year":"2009","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2022.102537_bib425","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.3390\/nu11051186","article-title":"Nutritional strategies to prevent lens cataract: current status and future strategies","volume":"11","author":"Braakhuis","year":"2009","journal-title":"Nutrients"},{"key":"10.1016\/j.jbc.2022.102537_bib426","article-title":"Morphology of the Lens in Molecular and Cellular Biology of the Eye Lens.","author":"Maisel","year":"1981"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925822009802?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925822009802?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T00:26:31Z","timestamp":1758241591000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925822009802"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,11]]},"references-count":426,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2022,11]]}},"alternative-id":["S0021925822009802"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2022.102537","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2022,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2022.102537","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"102537"}}