{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T09:33:58Z","timestamp":1773308038394,"version":"3.50.1"},"reference-count":94,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,1,12]],"date-time":"2026-01-12T00:00:00Z","timestamp":1768176000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000009","name":"Foundation for the National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000009","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01GM144964"],"award-info":[{"award-number":["R01GM144964"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01EY021514"],"award-info":[{"award-number":["R01EY021514"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Reports"],"published-print":{"date-parts":[[2026,3]]},"DOI":"10.1016\/j.bpr.2026.100251","type":"journal-article","created":{"date-parts":[[2026,1,18]],"date-time":"2026-01-18T06:31:19Z","timestamp":1768717879000},"page":"100251","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Mimicking oxidative damage in \u03b3S-crystallin with site-specific incorporation of 5-hydroxytryptophan"],"prefix":"10.1016","volume":"6","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0451-9825","authenticated-orcid":false,"given":"Yeonseong","family":"Seo","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3795-5551","authenticated-orcid":false,"given":"Zane G.","family":"Long","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tsoler K.","family":"Demerdjian","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Acts A.","family":"Avenido","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7911-9834","authenticated-orcid":false,"given":"Carter T.","family":"Butts","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9996-7411","authenticated-orcid":false,"given":"Rachel W.","family":"Martin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpr.2026.100251_bib1","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.bpr.2026.100251_bib2","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1093\/hmg\/7.3.471","article-title":"Autosomal dominant congenital cataract associated with a missense mutation in the human \u03b1-crystallin gene CRYAA","volume":"7","author":"Litt","year":"1998","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bpr.2026.100251_bib3","first-page":"U95","article-title":"A novel mutation in the gene for a \u03b1-crystallin associated with autosomal dominant cataract linked to 21q","volume":"43","author":"Mackay","year":"2002","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.bpr.2026.100251_bib4","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1167\/iovs.05-1004","article-title":"A novel \u03b1B-crystallin mutation associated with autosomal dominant congenital lamellar cataract","volume":"47","author":"Liu","year":"2006","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.bpr.2026.100251_bib5","doi-asserted-by":"crossref","first-page":"1779","DOI":"10.1093\/hmg\/9.12.1779","article-title":"Link between a novel human \u03b3D-crystallin allele and a unique cataract phenotype explained by protein crystallography","volume":"9","author":"Kmoch","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bpr.2026.100251_bib6","doi-asserted-by":"crossref","first-page":"6116","DOI":"10.1073\/pnas.101124798","article-title":"Crystal cataracts: Human genetic cataract caused by protein crystallization","volume":"98","author":"Pande","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpr.2026.100251_bib7","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.1021\/bi0479611","article-title":"Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human \u03b3D-crystallin","volume":"44","author":"Pande","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpr.2026.100251_bib8","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1136\/jmg.2004.028274","article-title":"Gamma-S crystallin gene (CRYGS) mutation causes dominant progressive cortical cataract in humans","volume":"42","author":"Sun","year":"2005","journal-title":"J. Med. Genet."},{"key":"10.1016\/j.bpr.2026.100251_bib9","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.bbrc.2013.11.073","article-title":"The cataract-associated V41M mutant of human \u03b3S-crystallin shows specific structural changes that directly enhance local surface hydrophobicity","volume":"443","author":"Bharat","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bpr.2026.100251_bib10","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.bpr.2026.100251_bib11","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.bpr.2026.100251_bib12","doi-asserted-by":"crossref","first-page":"8638","DOI":"10.1021\/bi015924t","article-title":"Deamidation in human \u03b3S-crystallin from cataractous lenses is influenced by surface exposure","volume":"41","author":"Lapko","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpr.2026.100251_bib13","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1042\/bj20031367","article-title":"The identification of a reaction site of glutathione mixed-disulphide formation on \u03b3S-crystallin in human lens","volume":"379","author":"Craghill","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.bpr.2026.100251_bib14","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1016\/S1074-5521(97)90303-3","article-title":"Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer\u2019s disease amyloid-\u03b2 protein","volume":"4","author":"Harper","year":"1997","journal-title":"Chem. Biol."},{"key":"10.1016\/j.bpr.2026.100251_bib15","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1016\/j.cell.2013.08.035","article-title":"Molecular structure of \u03b2-amyloid fibrils in alzheimer\u2019s disease brain tissue","volume":"154","author":"Lu","year":"2013","journal-title":"Cell"},{"key":"10.1016\/j.bpr.2026.100251_bib16","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1042\/BJ20150617","article-title":"Amyloid fibrils are the molecular trigger of inflammation in parkinson\u2019s disease","volume":"471","author":"Gustot","year":"2015","journal-title":"Biochem. J."},{"key":"10.1016\/j.bpr.2026.100251_bib17","doi-asserted-by":"crossref","first-page":"17963","DOI":"10.1073\/pnas.1906124116","article-title":"Parkinson\u2019s disease is a type of amyloidosis featuring accumulation of amyloid fibrils of \u03b1-synuclein","volume":"116","author":"Araki","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpr.2026.100251_bib18","doi-asserted-by":"crossref","first-page":"4604","DOI":"10.1073\/pnas.96.8.4604","article-title":"Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for huntington\u2019s disease pathology","volume":"96","author":"Scherzinger","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpr.2026.100251_bib19","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1038\/368756a0","article-title":"Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus","volume":"368","author":"Lorenzo","year":"1994","journal-title":"Nature"},{"key":"10.1016\/j.bpr.2026.100251_bib20","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1038\/s41594-020-0496-3","article-title":"Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly","volume":"27","author":"Gallardo","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpr.2026.100251_bib21","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0065-3233(08)60287-9","article-title":"Sickle cell hemoglobin polymerization","volume":"40","author":"Eaton","year":"1990","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.bpr.2026.100251_bib22","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1016\/j.ijbiomac.2016.09.073","article-title":"Sickle cell disease: Its molecular mechanism and the one drug that treats it","volume":"93","author":"Ferrone","year":"2016","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bpr.2026.100251_bib23","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms15137","article-title":"Cataract-associated P23T \u03b3D-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH","volume":"8","author":"Boatz","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bpr.2026.100251_bib24","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1074\/jbc.M112.416354","article-title":"The human W42R \u03b3D-crystallin mutant structure provides a link between congenital and age-related cataracts","volume":"288","author":"Ji","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpr.2026.100251_bib25","first-page":"771","article-title":"Structural study of the G57W mutant of human gamma-s-crystallin, associated with congenital cataract","volume":"22","author":"Khan","year":"2016","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bpr.2026.100251_bib26","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.126910","article-title":"Cataract-causing mutations S78F and S78P of \u03b3D-crystallin decrease protein conformational stability and drive aggregation","volume":"253","author":"Lin","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bpr.2026.100251_bib27","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.pathophys.2006.05.006","article-title":"Oxidative stress in cataracts","volume":"13","author":"Vinson","year":"2006","journal-title":"Pathophysiology"},{"key":"10.1016\/j.bpr.2026.100251_bib28","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1111\/j.1463-5224.2006.00498.x","article-title":"Oxidation, antioxidants and cataract formation: a literature review","volume":"9","author":"Williams","year":"2006","journal-title":"Vet. Ophthalmol."},{"key":"10.1016\/j.bpr.2026.100251_bib29","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.mrgentox.2008.09.013","article-title":"Environmental-induced oxidative stress in neurodegenerative disorders and aging","volume":"674","author":"Migliore","year":"2009","journal-title":"Mutat. Res., Genet. Toxicol. Environ. Mutagen."},{"key":"10.1016\/j.bpr.2026.100251_bib30","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1038\/s42004-024-01163-w","article-title":"An ultraviolet-driven rescue pathway for oxidative stress to eye lens protein human gamma-D crystallin","volume":"7","author":"Hill","year":"2024","journal-title":"Commun. Chem."},{"key":"10.1016\/j.bpr.2026.100251_bib31","doi-asserted-by":"crossref","DOI":"10.1016\/j.exer.2025.110288","article-title":"Effect of lens crystallins aggregation on cataract formation","volume":"253","author":"Wang","year":"2025","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.bpr.2026.100251_bib32","doi-asserted-by":"crossref","first-page":"19020","DOI":"10.1016\/S0021-9258(18)37383-6","article-title":"Spontaneous peptide bond cleavage in aging \u03b1-crystallin through a succinimide intermediate","volume":"263","author":"Voorter","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpr.2026.100251_bib33","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1016\/S0731-7085(99)00230-7","article-title":"Isoaspartate in peptides and proteins: Formation, significance, and analysis","volume":"21","author":"Aswad","year":"2000","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.bpr.2026.100251_bib34","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/0014-5793(93)81113-E","article-title":"Age-dependent deamidation of alpha B-crystallin","volume":"322","author":"Groenen","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bpr.2026.100251_bib35","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.bpr.2026.100251_bib36","doi-asserted-by":"crossref","first-page":"7556","DOI":"10.1074\/jbc.H119.008716","article-title":"Isomerization as the secret Achilles\u2019 heel of long-lived proteins","volume":"294","author":"Guseman","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpr.2026.100251_bib37","doi-asserted-by":"crossref","first-page":"7546","DOI":"10.1074\/jbc.RA118.007052","article-title":"Structural and functional consequences of age-related isomerization in \u03b1-crystallins","volume":"294","author":"Lyon","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpr.2026.100251_bib38","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.bpr.2026.100251_bib39","doi-asserted-by":"crossref","first-page":"30782","DOI":"10.1074\/jbc.M603882200","article-title":"Glutamine deamidation destabilizes human \u03b3D-crystallin and lowers the kinetic barrier to unfolding","volume":"281","author":"Flaugh","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpr.2026.100251_bib40","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1110\/ps.035410.108","article-title":"Deamidation destabilizes and triggers aggregation of a lens protein, \u03b2A3-crystallin","volume":"17","author":"Takata","year":"2008","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpr.2026.100251_bib41","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.bpr.2026.100251_bib42","doi-asserted-by":"crossref","first-page":"4112","DOI":"10.1021\/acs.biochem.9b00593","article-title":"Altered protein dynamics and increased aggregation of human \u03b3S-crystallin due to cataract-associated deamidations","volume":"58","author":"Forsythe","year":"2019","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpr.2026.100251_bib43","doi-asserted-by":"crossref","first-page":"3146","DOI":"10.1021\/bi052051k","article-title":"Deamidation in human lens \u03b2B2-crystallin destabilizes the dimer","volume":"45","author":"Lampi","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpr.2026.100251_bib44","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/j.bbagen.2015.06.014","article-title":"Differences in solution dynamics between lens \u03b2-crystallin homodimers and heterodimers probed by hydrogen-deuterium exchange and deamidation","volume":"1860","author":"Lampi","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpr.2026.100251_bib45","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.bbagen.2015.08.015","article-title":"Deamidation of N76 in human \u03b3S-crystallin promotes dimer formation","volume":"1860","author":"Ray","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpr.2026.100251_bib46","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.bpr.2026.100251_bib47","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1021\/acs.biochem.3c00097","article-title":"Identification of the most impactful asparagine residues for \u03b3S-crystallin aggregation by deamidation","volume":"62","author":"Kato","year":"2023","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpr.2026.100251_bib48","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.bpr.2026.100251_bib49","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1021\/acs.jpcb.1c08157","article-title":"Human \u03b3S-crystallin resists unfolding despite extensive chemical modification from exposure to ionizing radiation","volume":"126","author":"Norton-Baker","year":"2022","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bpr.2026.100251_bib50","doi-asserted-by":"crossref","first-page":"16751","DOI":"10.1021\/ja904857t","article-title":"Femtosecond fluorescence spectra of tryptophan in human \u03b3-crystallin mutants: Site-dependent ultrafast quenching","volume":"131","author":"Xu","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bpr.2026.100251_bib51","doi-asserted-by":"crossref","first-page":"3708","DOI":"10.1021\/bi802177g","article-title":"Mechanism of the very efficient quenching of tryptophan fluorescence in human \u03b3D-and \u03b3S-crystallins: The \u03b3-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage","volume":"48","author":"Chen","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpr.2026.100251_bib52","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1002\/pro.2924","article-title":"Aggregation of Trp>Glu point mutants of human \u03b3D-crystallin provides a model for hereditary or UV-induced cataract","volume":"25","author":"Serebryany","year":"2016","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpr.2026.100251_bib53","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1016\/j.bpj.2010.12.3691","article-title":"Separating instability from aggregation propensity in \u03b3S-crystallin variants","volume":"100","author":"Brubaker","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpr.2026.100251_bib54","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1016\/j.bbrc.2015.09.075","article-title":"Site-specific oxidation of amino acid residues in rat lens \u03b3-crystallin induced by low-dose \u03b3-irradiation","volume":"466","author":"Kim","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bpr.2026.100251_bib55","doi-asserted-by":"crossref","first-page":"72391","DOI":"10.1002\/pro.5560071116","article-title":"Identification of tryptophan oxidation products in bovine \u03b1-crystallin","volume":"7","author":"Finley","year":"1998","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpr.2026.100251_bib56","doi-asserted-by":"crossref","first-page":"9666","DOI":"10.1021\/acs.analchem.0c00965","article-title":"Identification and quantification of oxidation products in full-length biotherapeutic antibodies by NMR spectroscopy","volume":"92","author":"Hinterholzer","year":"2020","journal-title":"Anal. Chem."},{"key":"10.1016\/j.bpr.2026.100251_bib57","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.bpr.2026.100251_bib58","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2019.101251","article-title":"Reductive modification of genetically encoded 3-nitrotyrosine sites in alpha synuclein expressed in E. coli","volume":"26","author":"Gerding","year":"2019","journal-title":"Redox Biol."},{"key":"10.1016\/j.bpr.2026.100251_bib59","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1002\/cbic.201900735","article-title":"Identification of human IDO1 enzyme activity by using genetically encoded nitrotyrosine","volume":"21","author":"Zheng","year":"2020","journal-title":"Chembiochem"},{"key":"10.1016\/j.bpr.2026.100251_bib60","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2021.167304","article-title":"A robust platform for unnatural amino acid mutagenesis in E. coli using the bacterial tryptophanyl-tRNA synthetase\/tRNA pair","volume":"434","author":"Ficaretta","year":"2022","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpr.2026.100251_bib61","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.pep.2005.01.016","article-title":"Protein production by auto-induction in high-density shaking cultures","volume":"41","author":"Studier","year":"2005","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.bpr.2026.100251_bib62","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s12104-011-9326-1","article-title":"1H, 13C, and 15N assignments of wild-type human \u03b3S-crystallin and its cataract-related variant \u03b3S-G18V","volume":"6","author":"Brubaker","year":"2012","journal-title":"Biomol. NMR Assign."},{"key":"10.1016\/j.bpr.2026.100251_bib63","doi-asserted-by":"crossref","DOI":"10.1002\/pro.70049","article-title":"An improved variant of tobacco etch virus (tev) protease that does not need reducing agents","volume":"34","author":"Davis","year":"2025","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpr.2026.100251_bib64","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.bpj.2019.06.006","article-title":"Kinetic stability of long-lived human lens \u03b3S-crystallins and their isolated double Greek key domains","volume":"117","author":"Mills-Henry","year":"2019","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpr.2026.100251_bib65","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbagen.2019.129502","article-title":"Human \u03b1B-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein","volume":"1864","author":"Sprague-Piercy","year":"2020","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.bpr.2026.100251_bib66","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1080\/10543406.2014.920345","article-title":"Nonlinear calibration model choice between the four and five-parameter logistic models","volume":"25","author":"Cumberland","year":"2015","journal-title":"J. Biopharm. Stat."},{"key":"10.1016\/j.bpr.2026.100251_bib67","doi-asserted-by":"crossref","first-page":"5388","DOI":"10.1016\/S0021-9258(20)79739-5","article-title":"Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, \u03b1-chymotrypsin, and \u03b2-lactoglobulin","volume":"249","author":"Greene","year":"1974","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpr.2026.100251_bib68","doi-asserted-by":"crossref","first-page":"2221","DOI":"10.1016\/j.str.2013.09.017","article-title":"Preferential and specific binding of human \u03b1B-crystallin to a cataract-related variant of \u03b3S-crystallin","volume":"21","author":"Kingsley","year":"2013","journal-title":"Structure"},{"key":"10.1016\/j.bpr.2026.100251_bib69","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simulating liquid water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bpr.2026.100251_bib70","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1021\/ct100578z","article-title":"Propka3: Consistent treatment of internal and surface residues in empirical pKa predictions","volume":"7","author":"Olsson","year":"2011","journal-title":"J. Chem. Theor. Comput."},{"key":"10.1016\/j.bpr.2026.100251_bib71","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: Visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."},{"key":"10.1016\/j.bpr.2026.100251_bib72","doi-asserted-by":"crossref","DOI":"10.1063\/5.0014475","article-title":"Scalable molecular dynamics on CPU and GPU architectures with NAMD","volume":"153","author":"Phillips","year":"2020","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bpr.2026.100251_bib73","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/nmeth.4067","article-title":"CHARMM36m: An improved force field for folded and intrinsically disordered proteins","volume":"14","author":"Huang","year":"2017","journal-title":"Nat. Methods"},{"key":"10.1016\/j.bpr.2026.100251_bib74","author":"Dashti"},{"key":"10.1016\/j.bpr.2026.100251_bib75","doi-asserted-by":"crossref","first-page":"4177","DOI":"10.1063\/1.467468","article-title":"Constant pressure molecular dynamics algorithms","volume":"101","author":"Martyna","year":"1994","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bpr.2026.100251_bib76","doi-asserted-by":"crossref","first-page":"4613","DOI":"10.1063\/1.470648","article-title":"Constant pressure molecular dynamics simulation: The Langevin piston method","volume":"103","author":"Feller","year":"1995","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bpr.2026.100251_bib77","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1002\/pro.3923","article-title":"The bio3D packages for structural bioinformatics","volume":"30","author":"Grant","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpr.2026.100251_bib78","doi-asserted-by":"crossref","first-page":"1","DOI":"10.18637\/jss.v024.i06","article-title":"Social network analysis with sna","volume":"24","author":"Butts","year":"2008","journal-title":"J. Stat. Software"},{"key":"10.1016\/j.bpr.2026.100251_bib79","doi-asserted-by":"crossref","DOI":"10.18637\/jss.v024.i02","article-title":"Network: A package for managing relational data in R","volume":"24","author":"Butts","year":"2008","journal-title":"J. Stat. Software"},{"key":"10.1016\/j.bpr.2026.100251_bib80","series-title":"R: A Language and Environment for Statistical Computing","year":"2022"},{"key":"10.1016\/j.bpr.2026.100251_bib81","author":"Murdoch"},{"key":"10.1016\/j.bpr.2026.100251_bib82","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/s10858-016-0060-y","article-title":"Ccpnmr analysisassign: a flexible platform for integrated NMR analysis","volume":"66","author":"Skinner","year":"2016","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.bpr.2026.100251_bib85","doi-asserted-by":"crossref","first-page":"14521","DOI":"10.1021\/jp9071108","article-title":"Calculating the fluorescence of 5-hydroxytryptophan in proteins","volume":"113","author":"Robinson","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bpr.2026.100251_bib83","doi-asserted-by":"crossref","first-page":"2876","DOI":"10.1038\/nprot.2006.202","article-title":"Using circular dichroism spectra to estimate protein secondary structure","volume":"1","author":"Greenfield","year":"2006","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.bpr.2026.100251_bib84","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1110\/ps.04627004","article-title":"Probing folding and fluorescence quenching in human \u03b3D crystallin Greek key domains using triple tryptophan mutant proteins","volume":"13","author":"Kosinski-Collins","year":"2004","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpr.2026.100251_bib86","doi-asserted-by":"crossref","first-page":"7334","DOI":"10.1021\/bi900467a","article-title":"The G18V CRYGS mutation associated with human cataracts increases \u03b3S-crystallin sensitivity to thermal and chemical stress","volume":"48","author":"Ma","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpr.2026.100251_bib87","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1023\/A:1012911329730","article-title":"Amide proton temperature coefficients as hydrogen bond indicators in proteins","volume":"21","author":"Cierpicki","year":"2001","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.bpr.2026.100251_bib88","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.bbagen.2015.09.022","article-title":"Increased hydrophobic surface exposure in the cataract-related G18V variant of human \u03b3S-crystallin","volume":"1860","author":"Khago","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpr.2026.100251_bib89","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1002\/prot.24321","article-title":"Crystal structure of the cataract-causing P23T \u03b3D-crystallin mutant. Proteins - Structure","volume":"81","author":"Ji","year":"2013","journal-title":"Proteins"},{"key":"10.1016\/j.bpr.2026.100251_bib90","doi-asserted-by":"crossref","first-page":"5212","DOI":"10.1167\/iovs.06-0427","article-title":"Mutation causing self-aggregation in human \u03b3C-crystallin leading to congenital cataract","volume":"47","author":"Talla","year":"2006","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.bpr.2026.100251_bib91","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbrc.2024.150585","article-title":"A novel cataract-related mutation R10P in \u03b3A-crystallin increases susceptibility to thermal shock and ultraviolet radiation of \u03b3A-crystallin","volume":"739","author":"Xu","year":"2024","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bpr.2026.100251_bib92","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/j.jmb.2018.12.005","article-title":"The structure and stability of the disulfide-linked \u03b3S-crystallin dimer provide insight into oxidation products associated with lens cataract formation","volume":"431","author":"Thorn","year":"2019","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpr.2026.100251_bib93","doi-asserted-by":"crossref","first-page":"1993","DOI":"10.1073\/pnas.040554397","article-title":"Molecular basis of a progressive juvenile-onset hereditary cataract","volume":"97","author":"Pande","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpr.2026.100251_bib94","first-page":"438","article-title":"Different tools to study interaction potentials in \u03b3-crystallin solutions: Relevance to crystal growth","volume":"D53","author":"Bonnet\u00e9","year":"1997","journal-title":"Acta Crystallogr."}],"container-title":["Biophysical Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2667074726000042?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2667074726000042?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T15:13:41Z","timestamp":1773242021000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2667074726000042"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3]]},"references-count":94,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2026,3]]}},"alternative-id":["S2667074726000042"],"URL":"https:\/\/doi.org\/10.1016\/j.bpr.2026.100251","relation":{},"ISSN":["2667-0747"],"issn-type":[{"value":"2667-0747","type":"print"}],"subject":[],"published":{"date-parts":[[2026,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mimicking oxidative damage in \u03b3S-crystallin with site-specific incorporation of 5-hydroxytryptophan","name":"articletitle","label":"Article Title"},{"value":"Biophysical Reports","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpr.2026.100251","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Author(s). Published by Elsevier Inc. on behalf of Biophysical Society.","name":"copyright","label":"Copyright"}],"article-number":"100251"}}