{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,9]],"date-time":"2026-06-09T16:08:41Z","timestamp":1781021321297,"version":"3.54.1"},"reference-count":58,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,4,10]],"date-time":"2024-04-10T00:00:00Z","timestamp":1712707200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2024,4,10]],"date-time":"2024-04-10T00:00:00Z","timestamp":1712707200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100000691","name":"Academy of Medical Sciences","doi-asserted-by":"publisher","award":["SBF006044"],"award-info":[{"award-number":["SBF006044"]}],"id":[{"id":"10.13039\/501100000691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["EXC2056"],"award-info":[{"award-number":["EXC2056"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002347","name":"Bundesministerium f\u00fcr Bildung und Forschung","doi-asserted-by":"publisher","award":["05K19GU1"],"award-info":[{"award-number":["05K19GU1"]}],"id":[{"id":"10.13039\/501100002347","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002347","name":"Bundesministerium f\u00fcr Bildung und Forschung","doi-asserted-by":"publisher","award":["05K16GU1"],"award-info":[{"award-number":["05K16GU1"]}],"id":[{"id":"10.13039\/501100002347","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002347","name":"Bundesministerium f\u00fcr Bildung und Forschung","doi-asserted-by":"publisher","award":["05K22GU6"],"award-info":[{"award-number":["05K22GU6"]}],"id":[{"id":"10.13039\/501100002347","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009318","name":"Helmholtz Association","doi-asserted-by":"publisher","award":["VH-NG-19-02"],"award-info":[{"award-number":["VH-NG-19-02"]}],"id":[{"id":"10.13039\/501100009318","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Commun Chem"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Human gamma-D crystallin (HGD) is a major constituent of the eye lens. Aggregation of HGD contributes to cataract formation, the leading cause of blindness worldwide. It is unique in its longevity, maintaining its folded and soluble state for 50-60 years. One outstanding question is the structural basis of this longevity despite oxidative aging and environmental stressors including ultraviolet radiation (UV). Here we present crystallographic structures evidencing a UV-induced crystallin redox switch mechanism. The room-temperature serial synchrotron crystallographic (SSX) structure of freshly prepared crystallin mutant (R36S) shows no post-translational modifications. After aging for nine months in the absence of light, a thiol-adduct (dithiothreitol) modifying surface cysteines is observed by low-dose SSX. This is shown to be UV-labile in an acutely light-exposed structure. This suggests a mechanism by which a major source of crystallin damage, UV, may also act as a rescuing factor in a finely balanced redox system.<\/jats:p>","DOI":"10.1038\/s42004-024-01163-w","type":"journal-article","created":{"date-parts":[[2024,4,10]],"date-time":"2024-04-10T13:01:46Z","timestamp":1712754106000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["An ultraviolet-driven rescue pathway for oxidative stress to eye lens protein human gamma-D crystallin"],"prefix":"10.1038","volume":"7","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9984-3387","authenticated-orcid":false,"given":"Jake A.","family":"Hill","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yvonne","family":"Nyathi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6355-8640","authenticated-orcid":false,"given":"Sam","family":"Horrell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7906-9788","authenticated-orcid":false,"given":"David","family":"von Stetten","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7694-8525","authenticated-orcid":false,"given":"Danny","family":"Axford","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2104-7057","authenticated-orcid":false,"given":"Robin L.","family":"Owen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Godfrey S.","family":"Beddard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8499-7490","authenticated-orcid":false,"given":"Arwen R.","family":"Pearson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7894-4939","authenticated-orcid":false,"given":"Helen M.","family":"Ginn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1868-8435","authenticated-orcid":false,"given":"Briony A.","family":"Yorke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,4,10]]},"reference":[{"key":"1163_CR1","doi-asserted-by":"publisher","first-page":"196","DOI":"10.1097\/ICL.0b013e31821e45a9","volume":"37","author":"RD Glickman","year":"2011","unstructured":"Glickman, R. D. Ultraviolet phototoxicity to the retina. Eye contact lens 37, 196\u2013205 (2011).","journal-title":"Eye contact lens"},{"key":"1163_CR2","doi-asserted-by":"publisher","first-page":"17997","DOI":"10.1074\/jbc.RA118.004551","volume":"293","author":"E Serebryany","year":"2018","unstructured":"Serebryany, E., Yu, S., Trauger, S. A., Budnik, B. & Shakhnovich, E. I. Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation. J. Biol. Chem. 293, 17997\u201318009 (2018).","journal-title":"J. Biol. Chem."},{"key":"1163_CR3","doi-asserted-by":"publisher","first-page":"4182","DOI":"10.1167\/iovs.10-7094","volume":"52","author":"S Su","year":"2011","unstructured":"Su, S. et al. Proteomic analysis of human age-related nuclear cataracts and normal lens nuclei. Investig. Ophthalmol. Vis. Sci. 52, 4182\u20134191 (2011).","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"1163_CR4","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1146\/annurev-physchem-090419-121428","volume":"72","author":"MA Sprague-Piercy","year":"2021","unstructured":"Sprague-Piercy, M. A., Rocha, M. A., Kwok, A. O. & Martin, R. W. \u03b1-crystallins in the vertebrate eye lens: Complex oligomers and molecular chaperones. Annu. Rev. Phys. Chem. 72, 143\u2013163 (2021).","journal-title":"Annu. Rev. Phys. Chem."},{"key":"1163_CR5","first-page":"1","volume":"1","author":"D Lam","year":"2015","unstructured":"Lam, D. et al. Cataract. Nat. Rev. Dis. Prim. 1, 1\u201315 (2015).","journal-title":"Nat. Rev. Dis. Prim."},{"key":"1163_CR6","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1042\/bj2300143","volume":"230","author":"C Slingsby","year":"1985","unstructured":"Slingsby, C. & Miller, L. The reaction of glutathione with the eye-lens protein gamma-crystallin. Biochem. J. 230, 143 (1985).","journal-title":"Biochem. J."},{"key":"1163_CR7","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1089\/jop.2000.16.121","volume":"16","author":"FJ Giblin","year":"2000","unstructured":"Giblin, F. J. Glutathione: a vital lens antioxidant. J. Ocul. Pharmacol. Therap. 16, 121\u2013135 (2000).","journal-title":"J. Ocul. Pharmacol. Therap."},{"key":"1163_CR8","doi-asserted-by":"publisher","first-page":"1516","DOI":"10.3390\/antiox11081516","volume":"11","author":"JC Lim","year":"2022","unstructured":"Lim, J. C., Suzuki-Kerr, H., Nguyen, T. X., Lim, C. J. & Poulsen, R. C. Redox homeostasis in ocular tissues: Circadian regulation of glutathione in the lens? Antioxidants 11, 1516 (2022).","journal-title":"Antioxidants"},{"key":"1163_CR9","doi-asserted-by":"publisher","first-page":"1973","DOI":"10.3390\/antiox11101973","volume":"11","author":"MF Lou","year":"2022","unstructured":"Lou, M. F. Glutathione and glutaredoxin in redox regulation and cell signaling of the lens. Antioxidants 11, 1973 (2022).","journal-title":"Antioxidants"},{"key":"1163_CR10","doi-asserted-by":"publisher","first-page":"3595","DOI":"10.1016\/j.bbadis.2018.08.021","volume":"1864","author":"S Ramkumar","year":"2018","unstructured":"Ramkumar, S., Fan, X., Wang, B., Yang, S. & Monnier, V. M. Reactive cysteine residues in the oxidative dimerization and cu2+ induced aggregation of human \u03b3d-crystallin: Implications for age-related cataract. Biochim. et. Biophys. Acta (BBA)-Mol. Basis Dis. 1864, 3595\u20133604 (2018).","journal-title":"Biochim. et. Biophys. Acta (BBA)-Mol. Basis Dis."},{"key":"1163_CR11","doi-asserted-by":"publisher","first-page":"108709","DOI":"10.1016\/j.exer.2021.108709","volume":"210","author":"TF Wishart","year":"2021","unstructured":"Wishart, T. F., Flokis, M., Shu, D. Y., Das, S. J. & Lovicu, F. J. Hallmarks of lens aging and cataractogenesis. Exp. Eye Res. 210, 108709 (2021).","journal-title":"Exp. Eye Res."},{"key":"1163_CR12","doi-asserted-by":"publisher","first-page":"1175","DOI":"10.1021\/tx800005u","volume":"21","author":"C Sch\u00f6neich","year":"2008","unstructured":"Sch\u00f6neich, C. Mechanisms of protein damage induced by cysteine thiyl radical formation. Chem. Res. Toxicol. 21, 1175\u20131179 (2008).","journal-title":"Chem. Res. Toxicol."},{"key":"1163_CR13","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1042\/EBC20190053","volume":"64","author":"L Turell","year":"2020","unstructured":"Turell, L., Zeida, A. & Trujillo, M. Mechanisms and consequences of protein cysteine oxidation: the role of the initial short-lived intermediates. Essays Biochem. 64, 55\u201366 (2020).","journal-title":"Essays Biochem."},{"key":"1163_CR14","doi-asserted-by":"publisher","first-page":"26497","DOI":"10.1074\/jbc.R113.461368","volume":"288","author":"CL Grek","year":"2013","unstructured":"Grek, C. L., Zhang, J., Manevich, Y., Townsend, D. M. & Tew, K. D. Causes and consequences of cysteine s-glutathionylation. J. Biol. Chem. 288, 26497\u201326504 (2013).","journal-title":"J. Biol. Chem."},{"key":"1163_CR15","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1016\/j.coph.2007.06.003","volume":"7","author":"MM Gallogly","year":"2007","unstructured":"Gallogly, M. M. & Mieyal, J. J. Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr. Opin. Pharmacol. 7, 381\u2013391 (2007).","journal-title":"Curr. Opin. Pharmacol."},{"key":"1163_CR16","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1016\/j.exer.2016.06.018","volume":"156","author":"X Fan","year":"2017","unstructured":"Fan, X., Monnier, V. M. & Whitson, J. Lens glutathione homeostasis: Discrepancies and gaps in knowledge standing in the way of novel therapeutic approaches. Exp. eye Res. 156, 103\u2013111 (2017).","journal-title":"Exp. eye Res."},{"key":"1163_CR17","doi-asserted-by":"publisher","first-page":"587","DOI":"10.1006\/exer.1998.0549","volume":"67","author":"MH Sweeney","year":"1998","unstructured":"Sweeney, M. H. & Truscott, R. J. An impediment to glutathione diffusion in older normal human lenses: a possible precondition for nuclear cataract. Exp. eye Res. 67, 587\u2013595 (1998).","journal-title":"Exp. eye Res."},{"key":"1163_CR18","doi-asserted-by":"publisher","first-page":"889","DOI":"10.1016\/0014-4835(92)90015-K","volume":"55","author":"MF Lou","year":"1992","unstructured":"Lou, M. F. & Dickerson Jr, J. E. Protein-thiol mixed disulfides in human lens. Exp. Eye Res. 55, 889\u2013896 (1992).","journal-title":"Exp. Eye Res."},{"key":"1163_CR19","doi-asserted-by":"publisher","first-page":"1106","DOI":"10.1111\/php.12096","volume":"89","author":"N Schafheimer","year":"2013","unstructured":"Schafheimer, N. & King, J. Tryptophan cluster protects human \u03b3d-crystallin from ultraviolet radiation-induced photoaggregation in vitro. Photochem. Photobiol. 89, 1106\u20131115 (2013).","journal-title":"Photochem. Photobiol."},{"key":"1163_CR20","doi-asserted-by":"publisher","first-page":"11552","DOI":"10.1021\/bi060988v","volume":"45","author":"J Chen","year":"2006","unstructured":"Chen, J., Flaugh, S. L., Callis, P. R. & King, J. Mechanism of the highly efficient quenching of tryptophan fluorescence in human \u03b3d-crystallin. Biochemistry 45, 11552\u201311563 (2006).","journal-title":"Biochemistry"},{"key":"1163_CR21","doi-asserted-by":"publisher","first-page":"1779","DOI":"10.1093\/hmg\/9.12.1779","volume":"9","author":"S Kmoch","year":"2000","unstructured":"Kmoch, S. et al. Link between a novel human \u03b3d-crystallin allele and a unique cataract phenotype explained by protein crystallography. Hum. Mol. Genet. 9, 1779\u20131786 (2000).","journal-title":"Hum. Mol. Genet."},{"key":"1163_CR22","doi-asserted-by":"publisher","first-page":"6116","DOI":"10.1073\/pnas.101124798","volume":"98","author":"A Pande","year":"2001","unstructured":"Pande, A. et al. Crystal cataracts: human genetic cataract caused by protein crystallization. Proc. Natl Acad. Sci. 98, 6116\u20136120 (2001).","journal-title":"Proc. Natl Acad. Sci."},{"key":"1163_CR23","doi-asserted-by":"publisher","first-page":"1137","DOI":"10.1016\/S0022-2836(03)00375-9","volume":"328","author":"A Basak","year":"2003","unstructured":"Basak, A. et al. High-resolution x-ray crystal structures of human \u03b3d crystallin (1.25 \u00e5) and the r58h mutant (1.15 \u00e5) associated with aculeiform cataract. J. Mol. Biol. 328, 1137\u20131147 (2003).","journal-title":"J. Mol. Biol."},{"key":"1163_CR24","doi-asserted-by":"publisher","first-page":"930","DOI":"10.1016\/j.bpj.2019.07.019","volume":"117","author":"AR Khan","year":"2019","unstructured":"Khan, A. R. et al. Temperature-dependent non-covalent protein-protein interactions explain normal and inverted solubility in a mutant of human gamma d-crystallin. Biophys. J. 117, 930\u2013937 (2019).","journal-title":"Biophys. J."},{"key":"1163_CR25","doi-asserted-by":"publisher","first-page":"167252","DOI":"10.1016\/j.jmb.2021.167252","volume":"433","author":"A Strofaldi","year":"2021","unstructured":"Strofaldi, A., Khan, A. R. & McManus, J. J. Surface exposed free cysteine suppresses crystallization of human \u03b3d-crystallin. J. Mol. Biol. 433, 167252 (2021).","journal-title":"J. Mol. Biol."},{"key":"1163_CR26","doi-asserted-by":"publisher","first-page":"284","DOI":"10.1016\/j.str.2020.11.006","volume":"29","author":"AJ Guseman","year":"2021","unstructured":"Guseman, A. J. et al. Assessing the structures and interactions of \u03b3d-crystallin deamidation variants. Structure 29, 284\u2013291 (2021).","journal-title":"Structure"},{"key":"1163_CR27","doi-asserted-by":"publisher","first-page":"eabf1380","DOI":"10.1126\/sciadv.abf1380","volume":"7","author":"P Mehrabi","year":"2021","unstructured":"Mehrabi, P. et al. Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison. Sci. Adv. 7, eabf1380 (2021).","journal-title":"Sci. Adv."},{"key":"1163_CR28","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1002\/pro.3302","volume":"27","author":"CS Bury","year":"2018","unstructured":"Bury, C. S., Brooks-Bartlett, J. C., Walsh, S. P. & Garman, E. F. Estimate your dose: Raddose-3d. Protein Sci. 27, 217\u2013228 (2018).","journal-title":"Protein Sci."},{"key":"1163_CR29","doi-asserted-by":"publisher","first-page":"1225","DOI":"10.1107\/S0021889813011461","volume":"46","author":"OB Zeldin","year":"2013","unstructured":"Zeldin, O. B., Gerstel, M. & Garman, E. F. Raddose-3d: time-and space-resolved modelling of dose in macromolecular crystallography. J. Appl. Crystallogr. 46, 1225\u20131230 (2013).","journal-title":"J. Appl. Crystallogr."},{"key":"1163_CR30","doi-asserted-by":"publisher","first-page":"e4608","DOI":"10.1002\/pro.4608","volume":"32","author":"HM Ginn","year":"2023","unstructured":"Ginn, H. M. Torsion angles to map and visualize the conformational space of a protein. Protein Sci. 32, e4608 (2023).","journal-title":"Protein Sci."},{"key":"1163_CR31","doi-asserted-by":"publisher","first-page":"525","DOI":"10.1021\/ct100578z","volume":"7","author":"MH Olsson","year":"2011","unstructured":"Olsson, M. H., S\u00f8ndergaard, C. R., Rostkowski, M. & Jensen, J. H. Propka3: consistent treatment of internal and surface residues in empirical p k a predictions. J. Chem. Theory Comput. 7, 525\u2013537 (2011).","journal-title":"J. Chem. Theory Comput."},{"key":"1163_CR32","doi-asserted-by":"publisher","first-page":"4442","DOI":"10.1021\/acs.jcim.0c00718","volume":"60","author":"PB Reis","year":"2020","unstructured":"Reis, P. B., Vila-Vicosa, D., Rocchia, W. & Machuqueiro, M. Pypka: A flexible python module for poisson\u2013boltzmann-based p k a calculations. J. Chem. Inf. model 60, 4442\u20134448 (2020).","journal-title":"J. Chem. Inf. model"},{"key":"1163_CR33","doi-asserted-by":"publisher","first-page":"3931","DOI":"10.1021\/acs.jpcb.0c02272","volume":"124","author":"HR Kilgore","year":"2020","unstructured":"Kilgore, H. R. & Raines, R. T. Disulfide chromophores arise from stereoelectronic effects. J. Phys. Chem. B 124, 3931\u20133935 (2020).","journal-title":"J. Phys. Chem. B"},{"key":"1163_CR34","doi-asserted-by":"publisher","first-page":"6554","DOI":"10.1021\/jacs.7b13455","volume":"140","author":"M Ochmann","year":"2018","unstructured":"Ochmann, M. et al. Uv-photochemistry of the disulfide bond: Evolution of early photoproducts from picosecond x-ray absorption spectroscopy at the sulfur k-edge. J. Am. Chem. Soc. 140, 6554\u20136561 (2018).","journal-title":"J. Am. Chem. Soc."},{"key":"1163_CR35","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1111\/php.12862","volume":"94","author":"M Taniguchi","year":"2018","unstructured":"Taniguchi, M., Du, H. & Lindsey, J. S. Photochemcad 3: diverse modules for photophysical calculations with multiple spectral databases. Photochem. Photobiol. 94, 277\u2013289 (2018).","journal-title":"Photochem. Photobiol."},{"key":"1163_CR36","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1016\/0005-2795(67)90379-0","volume":"140","author":"RW Cowgill","year":"1967","unstructured":"Cowgill, R. W. Fluorescence and protein structure: Xi. fluorescence quenching by disulfide and sulfhydryl groups. Biochim. et. Biophys. Acta (BBA)-Protein Struct. 140, 37\u201344 (1967).","journal-title":"Biochim. et. Biophys. Acta (BBA)-Protein Struct."},{"key":"1163_CR37","doi-asserted-by":"publisher","first-page":"6751","DOI":"10.1021\/acs.jpcb.2c02441","volume":"126","author":"I L\u00f3pez-Pe na","year":"2022","unstructured":"L\u00f3pez-Pe na, I., Lee, C. T., Rivera, J. J. & Kim, J. E. Role of the triplet state and protein dynamics in the formation and stability of the tryptophan radical in an apoazurin mutant. J. Phys. Chem. B 126, 6751\u20136761 (2022).","journal-title":"J. Phys. Chem. B"},{"key":"1163_CR38","doi-asserted-by":"publisher","first-page":"1115","DOI":"10.1002\/pro.2924","volume":"25","author":"E Serebryany","year":"2016","unstructured":"Serebryany, E. et al. Aggregation of trp> glu point mutants of human gamma-d crystallin provides a model for hereditary or uv-induced cataract. Protein Sci. 25, 1115\u20131128 (2016).","journal-title":"Protein Sci."},{"key":"1163_CR39","doi-asserted-by":"publisher","first-page":"3935","DOI":"10.1021\/pr070138h","volume":"6","author":"PG Hains","year":"2007","unstructured":"Hains, P. G. & Truscott, R. J. Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. J. proteome Res. 6, 3935\u20133943 (2007).","journal-title":"J. proteome Res."},{"key":"1163_CR40","doi-asserted-by":"publisher","first-page":"6751","DOI":"10.1021\/jp101508b","volume":"114","author":"O Mozziconacci","year":"2010","unstructured":"Mozziconacci, O., Kerwin, B. A. & Sch\u00f6neich, C. Reversible hydrogen transfer between cysteine thiyl radical and glycine and alanine in model peptides: covalent h\/d exchange, radical- radical reactions, and l-to d-ala conversion. J. Phys. Chem. B 114, 6751\u20136762 (2010).","journal-title":"J. Phys. Chem. B"},{"key":"1163_CR41","doi-asserted-by":"crossref","unstructured":"Winterbourn, C. C. Radical scavenging by thiols and the fate of thiyl radicals in Oxidative stress and redox regulation (ed. Jakob, U. & Reichmann, D.) 43\u201358 (Springer, 2013).","DOI":"10.1007\/978-94-007-5787-5_2"},{"key":"1163_CR42","doi-asserted-by":"publisher","first-page":"108707","DOI":"10.1016\/j.exer.2021.108707","volume":"211","author":"E Serebryany","year":"2021","unstructured":"Serebryany, E., Thorn, D. C. & Quintanar, L. Redox chemistry of lens crystallins: A system of cysteines. Exp. Eye Res. 211, 108707 (2021).","journal-title":"Exp. Eye Res."},{"key":"1163_CR43","doi-asserted-by":"publisher","first-page":"885","DOI":"10.3390\/antiox11050885","volume":"11","author":"B Moosmann","year":"2022","unstructured":"Moosmann, B. & Hajieva, P. Probing the role of cysteine thiyl radicals in biology: eminently dangerous, difficult to scavenge. Antioxidants 11, 885 (2022).","journal-title":"Antioxidants"},{"key":"1163_CR44","first-page":"3145","volume":"32","author":"RF Brubaker","year":"1991","unstructured":"Brubaker, R. F. Flow of aqueous humor in humans [the friedenwald lecture]. Investig. Ophthalmol. Vis. Sci. 32, 3145\u20133166 (1991).","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"1163_CR45","doi-asserted-by":"publisher","first-page":"1598","DOI":"10.1021\/acs.molpharmaceut.7b01128","volume":"15","author":"AT Wecksler","year":"2018","unstructured":"Wecksler, A. T. et al. Photodisruption of the structurally conserved cys-cys-trp triads leads to reduction-resistant scrambled intrachain disulfides in an igg1 monoclonal antibody. Mol. Pharma. 15, 1598\u20131606 (2018).","journal-title":"Mol. Pharma."},{"key":"1163_CR46","doi-asserted-by":"publisher","first-page":"6900","DOI":"10.1021\/acs.jafc.0c01760","volume":"68","author":"Z Zhao","year":"2020","unstructured":"Zhao, Z., Poojary, M. M., Skibsted, L. H. & Lund, M. N. Cleavage of disulfide bonds in cystine by uv-b illumination mediated by tryptophan or tyrosine as photosensitizers. J. Agric. Food Chem. 68, 6900\u20136909 (2020).","journal-title":"J. Agric. Food Chem."},{"key":"1163_CR47","doi-asserted-by":"publisher","first-page":"9602","DOI":"10.1039\/C6CP00865H","volume":"18","author":"RM Abaskharon","year":"2016","unstructured":"Abaskharon, R. M. & Gai, F. Direct measurement of the tryptophan-mediated photocleavage kinetics of a protein disulfide bond. Phys. Chem. Chem. Phys. 18, 9602\u20139607 (2016).","journal-title":"Phys. Chem. Chem. Phys."},{"key":"1163_CR48","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1016\/j.str.2022.03.002","volume":"30","author":"B Norton-Baker","year":"2022","unstructured":"Norton-Baker, B. et al. Deamidation of the human eye lens protein \u03b3s-crystallin accelerates oxidative aging. Structure 30, 763\u2013776 (2022).","journal-title":"Structure"},{"key":"1163_CR49","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1107\/S2059798317002996","volume":"73","author":"RL Owen","year":"2017","unstructured":"Owen, R. L. et al. Low-dose fixed-target serial synchrotron crystallography. Acta Crystallogr. Sect. D: Struct. Biol. 73, 373\u2013378 (2017).","journal-title":"Acta Crystallogr. Sect. D: Struct. Biol."},{"key":"1163_CR50","first-page":"e62200","volume":"e62200","author":"S Horrell","year":"2021","unstructured":"Horrell, S. et al. Fixed target serial data collection at diamond light source. JoVE (J. Visualized Exp.) e62200, e62200 (2021).","journal-title":"JoVE (J. Visualized Exp.)"},{"key":"1163_CR51","first-page":"C589","volume":"70","author":"C Betzel","year":"2017","unstructured":"Betzel, C., Schneider, T., Chapman, H., Redeckec, L. & IUCr, J. Serial synchrotron crystallography at embl petra iii beamline p14. Found. Crystallogr. 70, C589 (2017).","journal-title":"Found. Crystallogr."},{"key":"1163_CR52","doi-asserted-by":"publisher","first-page":"680","DOI":"10.1107\/S1600576716004751","volume":"49","author":"TA White","year":"2016","unstructured":"White, T. A. et al. Recent developments in crystfel. J. Appl. Crystallogr. 49, 680\u2013689 (2016).","journal-title":"J. Appl. Crystallogr."},{"key":"1163_CR53","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1107\/S0021889807021206","volume":"40","author":"AJ McCoy","year":"2007","unstructured":"McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658\u2013674 (2007).","journal-title":"J. Appl. Crystallogr."},{"key":"1163_CR54","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1107\/S2059798323003595","volume":"79","author":"J Agirre","year":"2023","unstructured":"Agirre, J. et al. The ccp4 suite: integrative software for macromolecular crystallography. Acta Crystallogr. Sect. D: Struct. Biol. 79, 449\u2013461 (2023).","journal-title":"Acta Crystallogr. Sect. D: Struct. Biol."},{"key":"1163_CR55","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1107\/S0907444911001314","volume":"67","author":"GN Murshudov","year":"2011","unstructured":"Murshudov, G. N. et al. Refmac5 for the refinement of macromolecular crystal structures. Acta Crystallogr. Sect. D: Biol. Crystallogr. 67, 355\u2013367 (2011).","journal-title":"Acta Crystallogr. Sect. D: Biol. Crystallogr."},{"key":"1163_CR56","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of coot. Acta Crystallogr. Sect. D. - Biol. Crystallogr. 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr. Sect. D. - Biol. Crystallogr."},{"key":"1163_CR57","doi-asserted-by":"publisher","first-page":"861","DOI":"10.1107\/S2059798319011471","volume":"75","author":"D Liebschner","year":"2019","unstructured":"Liebschner, D. et al. Macromolecular structure determination using x-rays, neutrons and electrons: recent developments in phenix. Acta Crystallogr. Sect. D: Struct. Biol. 75, 861\u2013877 (2019).","journal-title":"Acta Crystallogr. Sect. D: Struct. Biol."},{"key":"1163_CR58","first-page":"76","volume":"1","author":"E Krissinel","year":"2012","unstructured":"Krissinel, E. Enhanced fold recognition using efficient short fragment clustering. J. Mol. Biochem. 1, 76 (2012).","journal-title":"J. Mol. Biochem."}],"container-title":["Communications Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s42004-024-01163-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s42004-024-01163-w","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s42004-024-01163-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,4,10]],"date-time":"2024-04-10T14:07:37Z","timestamp":1712758057000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s42004-024-01163-w"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4,10]]},"references-count":58,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["1163"],"URL":"https:\/\/doi.org\/10.1038\/s42004-024-01163-w","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2023.08.25.554810","asserted-by":"object"}]},"ISSN":["2399-3669"],"issn-type":[{"value":"2399-3669","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,4,10]]},"assertion":[{"value":"4 October 2023","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 March 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"10 April 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"81"}}