{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T17:19:39Z","timestamp":1791825579428,"version":"4.3.4"},"reference-count":52,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,7,1]],"date-time":"2024-07-01T00:00:00Z","timestamp":1719792000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,7,1]],"date-time":"2024-07-01T00:00:00Z","timestamp":1719792000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2024,7]]},"DOI":"10.1016\/j.biochi.2024.03.004","type":"journal-article","created":{"date-parts":[[2024,3,15]],"date-time":"2024-03-15T17:24:22Z","timestamp":1710523462000},"page":"151-168","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"special_numbering":"C","title":["Unraveling the impact of the p.R107L mutation on the structure and function of human \u03b1B-Crystallin: Implications for cataract formation"],"prefix":"10.1016","volume":"222","author":[{"given":"Farid","family":"Nasiri","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Parisa","family":"Ebrahimi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammad Bagher","family":"Shahsavani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anis","family":"Barati","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Issa","family":"Zarei","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jun","family":"Hong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masaru","family":"Hoshino","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ali Akbar","family":"Moosavi-Movahedi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7396-7720","authenticated-orcid":false,"given":"Reza","family":"Yousefi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2024.03.004_bib1","doi-asserted-by":"crossref","first-page":"e489","DOI":"10.1016\/S2214-109X(20)30488-5","article-title":"Bourne, the lancet global health commission on global eye health: vision beyond 2020","volume":"9","author":"Burton","year":"2021","journal-title":"Lancet Global Health"},{"key":"10.1016\/j.biochi.2024.03.004_bib2","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1038\/s41433-020-0806-3","article-title":"Global and regional prevalence of age-related cataract: a comprehensive systematic review and meta-analysis","volume":"34","author":"Hashemi","year":"2020","journal-title":"Eye"},{"key":"10.1016\/j.biochi.2024.03.004_bib3","doi-asserted-by":"crossref","first-page":"e144","DOI":"10.1016\/S2214-109X(20)30489-7","article-title":"Causes of blindness and vision impairment in 2020 and trends over 30 years, and prevalence of avoidable blindness in relation to VISION 2020: the Right to Sight: an analysis for the Global Burden of Disease Study","volume":"9","author":"Steinmetz","year":"2021","journal-title":"Lancet Global Health"},{"key":"10.1016\/j.biochi.2024.03.004_bib4","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1146\/annurev-physchem-090419-121428","article-title":"\u03b1-Crystallins in the Vertebrate eye lens: complex oligomers and molecular chaperones","volume":"72","author":"Sprague-Piercy","year":"2020","journal-title":"Annu. Rev. Phys. Chem."},{"key":"10.1016\/j.biochi.2024.03.004_bib5","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.bbagen.2015.06.008","article-title":"Structure and function of \u03b1-crystallins: traversing from in\u00a0vitro to in\u00a0vivo","volume":"1860","author":"Haslbeck","year":"2016","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.biochi.2024.03.004_bib6","doi-asserted-by":"crossref","first-page":"11041","DOI":"10.1021\/acs.jpcb.0c07449","article-title":"A\u00a0perspective on biophysical studies of Crystallin aggregation and implications for Cataract formation","volume":"124","author":"Bari","year":"2020","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.biochi.2024.03.004_bib7","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1007\/s12192-019-00979-z","article-title":"Small Heat Shock Proteins: multifaceted proteins with important implications for life","volume":"24","author":"Carra","year":"2019","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/j.biochi.2024.03.004_bib8","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fmolb.2022.842149","article-title":"Insights on human small heat shock proteins and their alterations in diseases","volume":"9","author":"Tedesco","year":"2022","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.biochi.2024.03.004_bib9","doi-asserted-by":"crossref","first-page":"1142","DOI":"10.1016\/j.ijbiomac.2019.09.239","article-title":"Structural and functional characterization of D109H and R69C mutant versions of human \u03b1B-crystallin: the biochemical pathomechanism underlying cataract and myopathy development","volume":"146","author":"Ghahramani","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.biochi.2024.03.004_bib10","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1007\/s12192-020-01098-w","article-title":"The multifaceted nature of \u03b1B-Crystallin","volume":"25","author":"Hayashi","year":"2020","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/j.biochi.2024.03.004_bib11","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.bbagen.2015.06.004","article-title":"Differential role of arginine mutations on the structure and functions of \u03b1-crystallin","volume":"1860","author":"Panda","year":"2016","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.biochi.2024.03.004_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.124590","article-title":"Investigating the role of double mutations R12C\/P20R, and R12C\/R69C on structure, chaperone-like activity, and amyloidogenic properties of human \u03b1B-crystallin","volume":"242","author":"Khaleghinejad","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.biochi.2024.03.004_bib14","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1002\/humu.22948","article-title":"Sporadic and familial congenital Cataracts: mutational spectrum and new diagnoses using Next-Generation Sequencing","volume":"37","author":"Ma","year":"2016","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.biochi.2024.03.004_bib15","doi-asserted-by":"crossref","first-page":"20491","DOI":"10.1073\/pnas.1111014108","article-title":"Multiple molecular architectures of the eye lens chaperone \u03b1B-crystallin elucidated by a triple hybrid approach","volume":"108","author":"Braun","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.biochi.2024.03.004_bib16","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1038\/nsmb.1891","article-title":"Solid-state NMR and SAXS studies provide a structural basis for the activation of \u03b1B-crystallin oligomers","volume":"17","author":"Jehle","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.biochi.2024.03.004_bib17","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 (Moscow)"},{"key":"10.1016\/j.biochi.2024.03.004_bib18","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pone.0260306","article-title":"Structural and functional studies of D109A human \u03b1B-crystallin contributing to the development of cataract and cardiomyopathy diseases","volume":"16","author":"Hafizi","year":"2021","journal-title":"PLoS One"},{"key":"10.1016\/j.biochi.2024.03.004_bib19","series-title":"Native Mass Spectrometry: towards High-Throughput Structural Proteomics BT - Structural Proteomics: High-Throughput Methods","first-page":"349","author":"Kondrat","year":"2015"},{"key":"10.1016\/j.biochi.2024.03.004_bib20","doi-asserted-by":"crossref","first-page":"10611","DOI":"10.1073\/pnas.1932958100","article-title":"Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in \u03b1B-crystallin","volume":"100","author":"Aquilina","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.biochi.2024.03.004_bib21","doi-asserted-by":"crossref","first-page":"W90","DOI":"10.1093\/nar\/gkac345","article-title":"BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy","volume":"50","author":"Micsonai","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.biochi.2024.03.004_bib22","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.biochi.2021.06.019","article-title":"The biochemical association between R157H mutation in human \u03b1B-crystallin and development of cardiomyopathy: structural and functional analyses of the mutant protein","volume":"190","author":"Nasiri","year":"2021","journal-title":"Biochimie"},{"key":"10.1016\/j.biochi.2024.03.004_bib23","doi-asserted-by":"crossref","DOI":"10.1016\/j.bpc.2021.106744","article-title":"Myopathy-associated G154S mutation causes important changes in the conformational stability, amyloidogenic properties, and chaperone-like activity of human \u03b1B-crystallin","volume":"282","author":"Khoshaman","year":"2022","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.biochi.2024.03.004_bib24","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-021-82250-z","article-title":"Elucidation of the mechanism of subunit exchange in \u03b1B crystallin oligomers","volume":"11","author":"Inoue","year":"2021","journal-title":"Sci. Rep."},{"key":"10.1016\/j.biochi.2024.03.004_bib25","doi-asserted-by":"crossref","first-page":"1606","DOI":"10.1016\/S0006-3495(00)76713-0","article-title":"Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling","volume":"78","author":"Schuck","year":"2000","journal-title":"Biophys. J."},{"key":"10.1016\/j.biochi.2024.03.004_bib26","doi-asserted-by":"crossref","first-page":"4651","DOI":"10.1529\/biophysj.106.081372","article-title":"Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation","volume":"90","author":"Brown","year":"2006","journal-title":"Biophys. J."},{"key":"10.1016\/j.biochi.2024.03.004_bib27","doi-asserted-by":"crossref","first-page":"8063","DOI":"10.1021\/bi00421a014","article-title":"Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl .alpha.-chymotrypsin using different denaturants","volume":"27","author":"Santoro","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2024.03.004_bib28","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1016\/j.ijbiomac.2020.05.059","article-title":"Effects of natural mutations (L94I and L94V) on the stability and mechanism of folding of horse cytochrome c: a combined in\u00a0vitro and molecular dynamics simulations approach","volume":"159","author":"Khan","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.biochi.2024.03.004_bib29","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1007\/978-1-59745-367-7_2","article-title":"Determining the conformational stability of a protein using urea denaturation curves","volume":"490","author":"Shaw","year":"2009","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.biochi.2024.03.004_bib30","series-title":"Using Intrinsic Fluorescence to Measure Protein Stability upon Thermal and Chemical Denaturation BT - Plant Proteostasis: Methods and Protocols","first-page":"229","author":"Varej\u00e3o","year":"2023"},{"key":"10.1016\/j.biochi.2024.03.004_bib31","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1074\/jbc.M308203200","article-title":"Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation","volume":"279","author":"Meehan","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2024.03.004_bib32","article-title":"Unveiling the structural and functional consequences of the p.D109G pathogenic mutation in human \u03b1B-Crystallin responsible for restrictive cardiomyopathy and skeletal myopathy","author":"Jafari","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.biochi.2024.03.004_bib33","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1002\/jcc.24030","article-title":"Best bang for your buck: GPU nodes for GROMACS biomolecular simulations","volume":"36","author":"Kutzner","year":"2015","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.biochi.2024.03.004_bib34","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1002\/jcc.20291","article-title":"GROMACS: fast, flexible, and free","volume":"26","author":"Van Der Spoel","year":"2005","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.biochi.2024.03.004_bib35","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1002\/jcc.21367","article-title":"CHARMM general force field: a force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields","volume":"31","author":"Vanommeslaeghe","year":"2010","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.biochi.2024.03.004_bib36","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: an N\u22c5log(N) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.biochi.2024.03.004_bib37","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.\u00a0Mol. Graph."},{"key":"10.1016\/j.biochi.2024.03.004_bib38","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1002\/(SICI)1521-3773(19990115)38:1\/2<236::AID-ANIE236>3.0.CO;2-M","article-title":"Peptide folding: when simulation meets experiment","volume":"38","author":"Daura","year":"1999","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.biochi.2024.03.004_bib39","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.124590","article-title":"Investigating the role of double mutations R12C\/P20R, and R12C\/R69C on structure, chaperone-like activity, and amyloidogenic properties of human \u03b1B-crystallin","volume":"242","author":"Khaleghinejad","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.biochi.2024.03.004_bib40","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1111\/j.1747-0285.2009.00847.x","article-title":"Circular dichroism techniques: biomolecular and nanostructural analyses- A review","volume":"74","author":"Ranjbar","year":"2009","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.biochi.2024.03.004_bib41","first-page":"10","article-title":"Peak fitting applied to fourier transform infrared and Raman spectroscopic analysis of proteins","author":"Sadat","year":"2020","journal-title":"Appl. Sci."},{"key":"10.1016\/j.biochi.2024.03.004_bib42","doi-asserted-by":"crossref","DOI":"10.1016\/j.saa.2021.119712","article-title":"Potential of Raman spectroscopic techniques to study proteins","volume":"258","author":"Kuhar","year":"2021","journal-title":"Spectrochim. Acta Mol. Biomol. Spectrosc."},{"key":"10.1016\/j.biochi.2024.03.004_bib43","doi-asserted-by":"crossref","first-page":"3932","DOI":"10.1021\/acs.biochem.5b00442","article-title":"Mimicking and understanding the agglutination effect of the antimicrobial peptide thanatin using model phospholipid vesicles","volume":"54","author":"Robert","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2024.03.004_bib44","doi-asserted-by":"crossref","first-page":"11473","DOI":"10.1021\/jacs.1c03392","article-title":"Different folding states from the same protein sequence determine reversible vs irreversible amyloid fate","volume":"143","author":"Cao","year":"2021","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.biochi.2024.03.004_bib45","first-page":"2197","article-title":"Mutation analysis of 12 genes in Chinese families with congenital Cataracts","volume":"17","author":"Sun","year":"2011","journal-title":"Mol. Vis."},{"key":"10.1016\/j.biochi.2024.03.004_bib13","article-title":"A\u00a0novel dominant mutation in CRYAB gene leading to a severe phenotype with childhood onset","volume":"8","author":"Marcos","year":"2020","journal-title":"Mol. Genet. Genom. Med."},{"key":"10.1016\/j.biochi.2024.03.004_bib46","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1021\/bi061323w","article-title":"Paradoxical effects of substitution and deletion mutation of Arg56 on the structure and chaperone function of human \u03b1B-crystallin","volume":"46","author":"Biswas","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2024.03.004_bib47","doi-asserted-by":"crossref","first-page":"6137","DOI":"10.1073\/pnas.96.11.6137","article-title":"Mutation R120G in \u03b1B-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function","volume":"96","author":"Bova","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.biochi.2024.03.004_bib48","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7554\/eLife.07304","article-title":"A\u00a0conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress related acidosis","volume":"4","author":"Rajagopal","year":"2015","journal-title":"Elife"},{"key":"10.1016\/j.biochi.2024.03.004_bib49","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1167\/iovs.05-1004","article-title":"A\u00a0novel \u03b1B-Crystallin mutation associated with autosomal dominant congenital lamellar Cataract","volume":"47","author":"Liu","year":"2006","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.biochi.2024.03.004_bib50","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 Gen. Subj."},{"key":"10.1016\/j.biochi.2024.03.004_bib51","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1111\/j.1742-4658.2004.04507.x","article-title":"R120G \u03b1B-crystallin promotes the unfolding of reduced \u03b1-lactalbumin and is inherently unstable","volume":"272","author":"Treweek","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.biochi.2024.03.004_bib52","doi-asserted-by":"crossref","first-page":"6409","DOI":"10.1073\/pnas.1014656108","article-title":"N-terminal domain of \u03b1B-crystallin provides a conformational switch for multimerization and structural heterogeneity","volume":"108","author":"Jehle","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A."}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908424000543?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908424000543?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,6,8]],"date-time":"2024-06-08T14:11:25Z","timestamp":1717855885000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908424000543"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,7]]},"references-count":52,"alternative-id":["S0300908424000543"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2024.03.004","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2024,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Unraveling the impact of the p.R107L mutation on the structure and function of human \u03b1B-Crystallin: Implications for cataract formation","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2024.03.004","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier B.V. and Soci\u00e9t\u00e9 Fran\u00e7aise de Biochimie et Biologie Mol\u00e9culaire (SFBBM). All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}