{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T04:01:21Z","timestamp":1784779281616,"version":"3.55.0"},"reference-count":40,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T00:00:00Z","timestamp":1677628800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T00:00:00Z","timestamp":1677628800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T00:00:00Z","timestamp":1677628800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T00:00:00Z","timestamp":1677628800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T00:00:00Z","timestamp":1677628800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T00:00:00Z","timestamp":1677628800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T00:00:00Z","timestamp":1677628800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100003443","name":"Ministry of Education and Science of the Russian Federation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003443","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Chemistry"],"published-print":{"date-parts":[[2023,3]]},"DOI":"10.1016\/j.bpc.2023.106963","type":"journal-article","created":{"date-parts":[[2023,1,26]],"date-time":"2023-01-26T02:58:26Z","timestamp":1674701906000},"page":"106963","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"special_numbering":"C","title":["Oxidative damage to \u03b2L-crystallin in vitro by iron compounds formed in physiological buffers"],"prefix":"10.1016","volume":"294","author":[{"given":"Nicolay B.","family":"Poliansky","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mikhail V.","family":"Motyakin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valery V.","family":"Kasparov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ivan A.","family":"Novikov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Konstantin O.","family":"Muranov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpc.2023.106963_bb0005","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1016\/j.bbagen.2010.02.005","article-title":"Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage","volume":"1800","author":"Arosio","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpc.2023.106963_bb0010","article-title":"Ferritin self-assembly, structure, function, and biotechnological applications","volume":"10","author":"Sudarev","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bpc.2023.106963_bb0015","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/j.cmet.2010.08.011","article-title":"Ferrit(in)ing out new mechanisms in iron homeostasis","volume":"12","author":"Andrews","year":"2010","journal-title":"Cell Metab."},{"key":"10.1016\/j.bpc.2023.106963_bb0020","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s10534-020-00232-6","article-title":"Iron-oxide minerals in the human tissues","volume":"33","author":"Svobodova","year":"2020","journal-title":"Biometals."},{"key":"10.1016\/j.bpc.2023.106963_bb0025","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1006\/exer.2000.0912","article-title":"Distribution of ferritin and redox-active transition metals in normal and cataractous human lenses","volume":"71","author":"Garner","year":"2000","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.bpc.2023.106963_bb0030","doi-asserted-by":"crossref","first-page":"728","DOI":"10.2471\/BLT.12.104034","article-title":"Global cost of correcting vision impairment from uncorrected refractive error","volume":"90","author":"Fricke","year":"2012","journal-title":"Bull. World Health Organ."},{"key":"10.1016\/j.bpc.2023.106963_bb0035","doi-asserted-by":"crossref","first-page":"63","DOI":"10.2471\/BLT.07.041210","article-title":"Global magnitude of visual impairment caused by uncorrected refractive errors in 2004","volume":"86","author":"Resnikoff","year":"2008","journal-title":"Bull. World Health Organ."},{"key":"10.1016\/j.bpc.2023.106963_bb0040","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1134\/S0006297922020031","article-title":"Biochemistry of eye Lens in the norm and in cataractogenesis","volume":"87","author":"Muranov","year":"2022","journal-title":"Biochem. Mosc."},{"key":"10.1016\/j.bpc.2023.106963_bb0045","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.bpc.2023.106963_bb0050","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.bpc.2023.106963_bb0055","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1021\/tx300372t","article-title":"Chemical modification of lysozyme, glucose 6-phosphate dehydrogenase, and bovine eye lens proteins induced by peroxyl radicals: role of oxidizable amino acid residues","volume":"26","author":"Arenas","year":"2013","journal-title":"Chem.Res.Toxicol."},{"key":"10.1016\/j.bpc.2023.106963_bb0060","first-page":"183","article-title":"Oxidative modification of rat eye lens proteins by peroxyl radicals in vitro: protection by the chain-breaking antioxidants stobadine and Trolox","volume":"30-6-2005","author":"Stefek","year":"1741","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpc.2023.106963_bb0065","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/S0014-4835(89)80072-7","article-title":"Oxidative modifications to crystallins induced in calf lenses in vitro by hydrogen peroxide","volume":"48","author":"Siezen","year":"1989","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.bpc.2023.106963_bb0070","doi-asserted-by":"crossref","first-page":"103","DOI":"10.3109\/10715769709097789","article-title":"Identification of hydrogen peroxide oxidation sites of alpha A- and alpha B-crystallins","volume":"26","author":"Smith","year":"1997","journal-title":"Free Radic. Res."},{"key":"10.1016\/j.bpc.2023.106963_bb0075","doi-asserted-by":"crossref","first-page":"771","DOI":"10.3109\/02713688909000867","article-title":"Purification of a 43,000 Dalton aggregate generated from alpha-crystallin","volume":"8","author":"McDermott","year":"1989","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.bpc.2023.106963_bb0080","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/j.freeradbiomed.2015.09.013","article-title":"The impact of hydrogen peroxide on structure, stability and functional properties of human R12C mutant alphaA-crystallin: the imperative insights into pathomechanism of the associated congenital cataract incidence","volume":"89","author":"Khoshaman","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.bpc.2023.106963_bb0085","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1016\/j.chemosphere.2017.05.039","article-title":"Hydroxyl radical yields in the Fenton process under various pH, ligand concentrations and hydrogen peroxide\/Fe(II) ratios","volume":"182","author":"Fischbacher","year":"2017","journal-title":"Chemosphere."},{"key":"10.1016\/j.bpc.2023.106963_bb0090","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/0169-7722(93)90042-Q","article-title":"Kinetics of ferric oxyhydroxide precipitation","volume":"14","author":"Grundl","year":"1993","journal-title":"J. Contam. Hydrol."},{"key":"10.1016\/j.bpc.2023.106963_bb0095","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/0021-9797(76)90253-8","article-title":"Characterization of partially neutralized ferric nitrate solutions","volume":"56","author":"Murphy","year":"1976","journal-title":"J. Coll. Interf. Sci."},{"key":"10.1016\/j.bpc.2023.106963_bb0100","doi-asserted-by":"crossref","first-page":"1417","DOI":"10.1021\/es970648k","article-title":"Catalytic decomposition of hydrogen peroxide on Iron oxide: kinetics, mechanism, and implications","volume":"32","author":"Lin","year":"1998","journal-title":"Environ. Sci. Technol."},{"key":"10.1016\/j.bpc.2023.106963_bb0105","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.chemosphere.2015.05.066","article-title":"Quantitative characterization of hydroxyl radical generation in a goethite-catalyzed Fenton-like reaction","volume":"141","author":"Lin","year":"2015","journal-title":"Chemosphere."},{"key":"10.1016\/j.bpc.2023.106963_bb0110","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/S0003-2670(00)87341-9","article-title":"Reaction between ferric and thiocyanate ions","volume":"3","author":"Ovenston","year":"1949","journal-title":"Anal. Chim. Acta"},{"key":"10.1016\/j.bpc.2023.106963_bb0115","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1021\/ja01198a026","article-title":"The stability and light absorption of the complex ion FeSCN++","volume":"69","author":"Frank","year":"1947","journal-title":"J. Amer. Chem. Soc"},{"key":"10.1016\/j.bpc.2023.106963_bb0120","series-title":"Zetasizer Nano User Manual","author":"Zetasizer","year":"2013"},{"key":"10.1016\/j.bpc.2023.106963_bb0125","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1111\/j.1399-3011.1979.tb01900.x","article-title":"Isolation and physical characterization of bovine lens crystallins","volume":"13","author":"Chiou","year":"1979","journal-title":"Int. J. Pept. Protein Res."},{"key":"10.1016\/j.bpc.2023.106963_bb0130","doi-asserted-by":"crossref","first-page":"13747","DOI":"10.1074\/jbc.M208157200","article-title":"Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin towards beta LOW- and individual gamma-crystallins","volume":"278","author":"Putilina","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2023.106963_bb0135","doi-asserted-by":"crossref","DOI":"10.3390\/ijms21062039","article-title":"Effect of arginine on chaperone-like activity of HspB6 and monomeric 14-3-3z","volume":"21","author":"Mikhaylova","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bpc.2023.106963_bb0140","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/0003-2697(64)90200-3","article-title":"A micro-biuret method for estimating proteins","volume":"9","author":"Itzhaki","year":"1964","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bpc.2023.106963_bb0145","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/S0076-6879(94)33040-9","article-title":"Carbonyl assays for determination of oxidatively modified proteins","volume":"233","author":"Levine","year":"1994","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bpc.2023.106963_bb0150","series-title":"Reactive Species Detection in Biology. From Fluorescence to Electron Paramagnetic Resonance Spectroscopy","author":"Villamena","year":"2016"},{"key":"10.1016\/j.bpc.2023.106963_bb0155","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.ymeth.2016.05.013","article-title":"Detection and characterisation of radicals using electron paramagnetic resonance (EPR) spin trapping and related methods","volume":"109","author":"Davies","year":"2016","journal-title":"Methods."},{"key":"10.1016\/j.bpc.2023.106963_bb0160","doi-asserted-by":"crossref","first-page":"3669","DOI":"10.1016\/S0021-9258(18)34832-4","article-title":"The horseradish peroxidase-catalyzed oxidation of 3,5,3\u2032,5\u2032-tetramethylbenzidine. Free radical and charge-transfer complex intermediates","volume":"257","author":"Josephy","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2023.106963_bb0165","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1385\/BTER:90:1-3:15","article-title":"Increased content of zinc and iron in human cataractous lenses","volume":"90","author":"Dawczynski","year":"2002","journal-title":"Biol. Trace Elem. Res."},{"key":"10.1016\/j.bpc.2023.106963_bb0170","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1159\/000055555","article-title":"Nickel, chromium, manganese, iron and aluminum levels in human cataractous and normal lenses","volume":"31","author":"Cekic","year":"1999","journal-title":"Ophthalmic Res."},{"key":"10.1016\/j.bpc.2023.106963_bb0175","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1006\/exer.1999.0754","article-title":"Formation of hydroxyl radicals in the human lens is related to the severity of nuclear cataract","volume":"70","author":"Garner","year":"2000","journal-title":"Exp. Eye Res."},{"issue":"Suppl. 1","key":"10.1016\/j.bpc.2023.106963_bb0180","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1159\/000267837","article-title":"H2O2 determination in rat lens: chemiluminescent versus radioisotopic methods","volume":"27","author":"Devamanoharan","year":"1995","journal-title":"Ophthalmic Res."},{"key":"10.1016\/j.bpc.2023.106963_bb0185","doi-asserted-by":"crossref","first-page":"831","DOI":"10.3109\/02713689109013879","article-title":"Hydrogen peroxide in the eye lens: radioisotopic determination","volume":"10","author":"Devamanoharan","year":"1991","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.bpc.2023.106963_bb0190","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.exer.2010.11.005","article-title":"Mechanism of aggregation of UV-irradiated betaL-crystallin","volume":"92","author":"Muranov","year":"2011","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.bpc.2023.106963_bb0195","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.bpc.2012.02.001","article-title":"Kinetics of aggregation of UV-irradiated glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle. Effect of agents possessing chaperone-like activity","volume":"163-164","author":"Maloletkina","year":"2012","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2023.106963_bb0200","doi-asserted-by":"crossref","first-page":"19683","DOI":"10.1074\/jbc.REV119.006217","article-title":"Detection, identification, and quantification of oxidative protein modifications","volume":"294","author":"Hawkins","year":"2019","journal-title":"J. Biol. Chem."}],"container-title":["Biophysical Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462223000145?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462223000145?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T07:59:40Z","timestamp":1759564780000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0301462223000145"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,3]]},"references-count":40,"alternative-id":["S0301462223000145"],"URL":"https:\/\/doi.org\/10.1016\/j.bpc.2023.106963","relation":{},"ISSN":["0301-4622"],"issn-type":[{"value":"0301-4622","type":"print"}],"subject":[],"published":{"date-parts":[[2023,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Oxidative damage to \u03b2L-crystallin in vitro by iron compounds formed in physiological buffers","name":"articletitle","label":"Article Title"},{"value":"Biophysical Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpc.2023.106963","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"106963"}}