{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T07:19:39Z","timestamp":1779347979428,"version":"3.51.4"},"reference-count":52,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100002701","name":"Korea Ministry of Education","doi-asserted-by":"publisher","award":["NRF-2018R1D1A3B07048635"],"award-info":[{"award-number":["NRF-2018R1D1A3B07048635"]}],"id":[{"id":"10.13039\/501100002701","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003716","name":"Korea Basic Science Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003716","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"published-print":{"date-parts":[[2026,1]]},"DOI":"10.1016\/j.bbapap.2025.141115","type":"journal-article","created":{"date-parts":[[2025,11,20]],"date-time":"2025-11-20T17:02:20Z","timestamp":1763658140000},"page":"141115","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["Flexibility in acidophilic thioredoxins: Insights from Asp43 substitutions in E. coli thioredoxin"],"prefix":"10.1016","volume":"1874","author":[{"given":"Oanh Mai","family":"Ho","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mohammed Shazaly A.","family":"Elhassan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Khang","family":"Nguyen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"ChangWoo","family":"Lee","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2025.141115_bb0005","doi-asserted-by":"crossref","first-page":"6102","DOI":"10.1046\/j.1432-1327.2000.01701.x","article-title":"Physiological functions of thioredoxin and thioredoxin reductase","volume":"267","author":"Arner","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbapap.2025.141115_bb0010","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1128\/JB.181.5.1375-1379.1999","article-title":"The thioredoxin superfamily: redundancy, specificity, and gray-area genomics","volume":"181","author":"Aslund","year":"1999","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0015","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1146\/annurev.bi.54.070185.001321","article-title":"Thioredoxin","volume":"54","author":"Holmgren","year":"1985","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbapap.2025.141115_bb0020","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/0022-2836(90)90313-B","article-title":"Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution","volume":"212","author":"Katti","year":"1990","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0025","doi-asserted-by":"crossref","first-page":"13963","DOI":"10.1016\/S0021-9258(18)71625-6","article-title":"Thioredoxin and glutaredoxin systems","volume":"264","author":"Holmgren","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2025.141115_bb0030","doi-asserted-by":"crossref","first-page":"6463","DOI":"10.1073\/pnas.97.12.6463","article-title":"Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase","volume":"97","author":"Lowther","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbapap.2025.141115_bb0035","first-page":"68","article-title":"Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase, world","volume":"5","author":"Sengupta","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2025.141115_bb0040","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1089\/ars.2010.3114","article-title":"Structure, function, and mechanism of thioredoxin proteins","volume":"13","author":"Collet","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.bbapap.2025.141115_bb0045","doi-asserted-by":"crossref","first-page":"1690","DOI":"10.1016\/j.str.2013.06.020","article-title":"Conservation of protein structure over four billion years","volume":"21","author":"Ingles-Prieto","year":"2013","journal-title":"Structure"},{"key":"10.1016\/j.bbapap.2025.141115_bb0050","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1093\/molbev\/msu312","article-title":"Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history","volume":"32","author":"Risso","year":"2015","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0055","doi-asserted-by":"crossref","first-page":"10812","DOI":"10.1021\/acsomega.3c09806","article-title":"Thr-to-Ala mutation leads to a larger aromatic pair and reduced packing density in \u03b11,\u03b13-helices during thioredoxin cold adaptation","volume":"9","author":"Nguyen","year":"2024","journal-title":"ACS Omega"},{"key":"10.1016\/j.bbapap.2025.141115_bb0060","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1038\/nsmb.2020","article-title":"Single-molecule paleoenzymology probes the chemistry of resurrected enzymes","volume":"18","author":"Perez-Jimenez","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0065","article-title":"Ancient thioredoxins evolved to modern-day stability-function requirement by altering native state ensemble","volume":"373","author":"Modi","year":"2018","journal-title":"Philos. Trans. R. Soc. Lond. Ser. B Biol. Sci."},{"key":"10.1016\/j.bbapap.2025.141115_bb0070","doi-asserted-by":"crossref","first-page":"1752","DOI":"10.1111\/febs.14767","article-title":"Loop size optimization induces a strong thermal stabilization of the thioredoxin fold","volume":"286","author":"Ruggiero","year":"2019","journal-title":"FEBS J."},{"key":"10.1016\/j.bbapap.2025.141115_bb0075","doi-asserted-by":"crossref","first-page":"14105","DOI":"10.1074\/jbc.RA119.009718","article-title":"Functional analyses of ancestral thioredoxins provide insights into their evolutionary history","volume":"294","author":"Napolitano","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2025.141115_bb0080","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1016\/j.cbpa.2006.08.011","article-title":"Enzyme promiscuity: evolutionary and mechanistic aspects","volume":"10","author":"Khersonsky","year":"2006","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0085","doi-asserted-by":"crossref","first-page":"3611","DOI":"10.1042\/BCJ20160532","article-title":"Engineering ancestral protein hyperstability","volume":"473","author":"Romero-Romero","year":"2016","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2025.141115_bb0090","doi-asserted-by":"crossref","first-page":"4346","DOI":"10.1128\/JB.187.13.4346-4352.2005","article-title":"Acetobacter aceti possesses a proton motive force-dependent efflux system for acetic acid","volume":"187","author":"Matsushita","year":"2005","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0095","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1110\/ps.062519707","article-title":"Atomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter aceti","volume":"16","author":"Starks","year":"2007","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbapap.2025.141115_bb0100","doi-asserted-by":"crossref","first-page":"8931","DOI":"10.1021\/bi00028a001","article-title":"Aspartic acid 26 in reduced Escherichia coli thioredoxin has a pKa > 9","volume":"34","author":"Wilson","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2025.141115_bb0105","doi-asserted-by":"crossref","first-page":"2622","DOI":"10.1021\/bi961801a","article-title":"Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: structural and functional characterization of mutants of Asp 26 and Lys 57","volume":"36","author":"Dyson","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2025.141115_bb0110","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2022.906437","article-title":"AlphaFold 2 and NMR spectroscopy: partners to understand protein structure, dynamics and function","volume":"9","author":"Laurents","year":"2022","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.bbapap.2025.141115_bb0115","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.bbapap.2025.141115_bb0120","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera--a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bbapap.2025.141115_bb0125","doi-asserted-by":"crossref","first-page":"2722","DOI":"10.1093\/bioinformatics\/btt473","article-title":"lDDT: a local superposition-free score for comparing protein structures and models using distance difference tests","volume":"29","author":"Mariani","year":"2013","journal-title":"Bioinformatics"},{"key":"10.1016\/j.bbapap.2025.141115_bb0130","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1007\/978-1-62703-646-7_6","article-title":"Clustal omega, accurate alignment of very large numbers of sequences","volume":"1079","author":"Sievers","year":"2014","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0135","doi-asserted-by":"crossref","first-page":"W306","DOI":"10.1093\/nar\/gkae337","article-title":"RING 4.0: faster residue interaction networks with novel interaction types across over 35,000 different chemical structures","volume":"52","author":"Del Conte","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbapap.2025.141115_bb0140","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1002\/0471140864.ps2809s79","article-title":"Analysis of protein stability and ligand interactions by thermal shift assay","volume":"79","author":"Huynh","year":"2015","journal-title":"Curr Protoc Protein Sci"},{"key":"10.1016\/j.bbapap.2025.141115_bb0145","doi-asserted-by":"crossref","first-page":"13386","DOI":"10.1021\/bi020371n","article-title":"Protein stabilization by urea and guanidine hydrochloride","volume":"41","author":"Bhuyan","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2025.141115_bb0150","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1111\/j.1751-1097.1989.tb09183.x","article-title":"Acrylamide quenching of tryptophan photochemistry and photophysics","volume":"49","author":"Tallmadge","year":"1989","journal-title":"Photochem. Photobiol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0155","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.bbapap.2025.141115_bb0160","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1038\/nsb0902-646","article-title":"Molecular dynamics simulations of biomolecules","volume":"9","author":"Karplus","year":"2002","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0165","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.3390\/molecules28041771","article-title":"Identification of novel natural dual HDAC and Hsp90 inhibitors for metastatic TNBC using e-pharmacophore modeling, molecular docking, and molecular dynamics studies","volume":"28","author":"AbdElmoniem","year":"2023","journal-title":"Molecules"},{"key":"10.1016\/j.bbapap.2025.141115_bb0170","doi-asserted-by":"crossref","first-page":"4291","DOI":"10.1021\/acs.jctc.1c00302","article-title":"OPLS4: improving force field accuracy on challenging regimes of chemical space","volume":"17","author":"Lu","year":"2021","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.bbapap.2025.141115_bb0175","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0261123","article-title":"Essential roles of buried phenylalanine in the structural stability of thioredoxin from a psychrophilic Arctic bacterium Sphingomonas sp","volume":"16","author":"Nguyen","year":"2021","journal-title":"PLoS One"},{"key":"10.1016\/j.bbapap.2025.141115_bb0180","doi-asserted-by":"crossref","first-page":"E1627","DOI":"10.1073\/pnas.1613892114","article-title":"Evidence for the principle of minimal frustration in the evolution of protein folding landscapes","volume":"114","author":"Tzul","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbapap.2025.141115_bb0185","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.tim.2007.02.005","article-title":"Life in acid: pH homeostasis in acidophiles","volume":"15","author":"Baker-Austin","year":"2007","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0190","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1016\/j.biochi.2010.07.003","article-title":"Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum","volume":"92","author":"Michaux","year":"2010","journal-title":"Biochimie"},{"key":"10.1016\/j.bbapap.2025.141115_bb0195","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00792-011-0402-3","article-title":"Acidophilic bacteria and archaea: acid stable biocatalysts and their potential applications","volume":"16","author":"Sharma","year":"2012","journal-title":"Extremophiles"},{"key":"10.1016\/j.bbapap.2025.141115_bb0200","doi-asserted-by":"crossref","first-page":"6163","DOI":"10.1007\/s00253-023-12702-1","article-title":"Acid-resistant enzymes: the acquisition strategies and applications","volume":"107","author":"Zhang","year":"2023","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0205","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2022.970109","article-title":"A dynamical view of protein-protein complexes: studies by molecular dynamics simulations","volume":"9","author":"Martin","year":"2022","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.bbapap.2025.141115_bb0210","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1001870","article-title":"Protein flexibility facilitates quaternary structure assembly and evolution","volume":"12","author":"Marsh","year":"2014","journal-title":"PLoS Biol."},{"key":"10.1016\/j.bbapap.2025.141115_bb0215","series-title":"Structural adaptations of bacterial Grx3 to temperature: Pro29 is essential for cold adaptation in Sphingomonas sp. Grx3","first-page":"23848","volume":"10","author":"Vu","year":"2025"},{"key":"10.1016\/j.bbapap.2025.141115_bb0220","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.freeradbiomed.2014.11.013","article-title":"The basics of thiols and cysteines in redox biology and chemistry","volume":"80","author":"Poole","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.bbapap.2025.141115_bb0225","doi-asserted-by":"crossref","first-page":"32241","DOI":"10.1074\/jbc.M113.495150","article-title":"Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system","volume":"288","author":"Du","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2025.141115_bb0230","doi-asserted-by":"crossref","first-page":"3381","DOI":"10.1021\/cr4006654","article-title":"Biochemistry and theory of proton-coupled electron transfer","volume":"114","author":"Migliore","year":"2014","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bbapap.2025.141115_bb0235","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1002\/prot.340110103","article-title":"Structural and functional relations among thioredoxins of different species","volume":"11","author":"Eklund","year":"1991","journal-title":"Proteins"},{"key":"10.1016\/j.bbapap.2025.141115_bb0240","doi-asserted-by":"crossref","first-page":"7603","DOI":"10.1021\/bi00244a032","article-title":"The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability","volume":"30","author":"Langsetmo","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2025.141115_bb0245","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1007\/BF00179349","article-title":"Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin","volume":"4","author":"Chandrasekhar","year":"1994","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.bbapap.2025.141115_bb0250","doi-asserted-by":"crossref","first-page":"4056","DOI":"10.1016\/S0021-9258(20)64285-5","article-title":"Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis","volume":"266","author":"Krause","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2025.141115_bb0255","doi-asserted-by":"crossref","first-page":"3091","DOI":"10.1074\/jbc.271.6.3091","article-title":"Replacement of Trp28 in Escherichia coli thioredoxin by site-directed mutagenesis affects thermodynamic stability but not function","volume":"271","author":"Slaby","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2025.141115_bb0260","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1093\/protein\/10.12.1425","article-title":"Structural and functional roles of a conserved proline residue in the \u03b12 helix of Escherichia coli thioredoxin","volume":"10","author":"de Lamotte-Guery","year":"1997","journal-title":"Protein Eng."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963925000536?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963925000536?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,12,19]],"date-time":"2025-12-19T14:21:06Z","timestamp":1766154066000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963925000536"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1]]},"references-count":52,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2026,1]]}},"alternative-id":["S1570963925000536"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2025.141115","relation":{},"ISSN":["1570-9639"],"issn-type":[{"value":"1570-9639","type":"print"}],"subject":[],"published":{"date-parts":[[2026,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Flexibility in acidophilic thioredoxins: Insights from Asp43 substitutions in E. coli thioredoxin","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbapap.2025.141115","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier B.V. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"141115"}}