{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T16:35:25Z","timestamp":1777566925539,"version":"3.51.4"},"reference-count":43,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,3,28]],"date-time":"2022-03-28T00:00:00Z","timestamp":1648425600000},"content-version":"vor","delay-in-days":86,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Research in Structural Biology"],"published-print":{"date-parts":[[2022]]},"DOI":"10.1016\/j.crstbi.2022.03.004","type":"journal-article","created":{"date-parts":[[2022,4,1]],"date-time":"2022-04-01T02:37:16Z","timestamp":1648780636000},"page":"87-95","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"C","title":["Crystal structure of plasmoredoxin, a redox-active protein unique for malaria parasites"],"prefix":"10.1016","volume":"4","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4422-6795","authenticated-orcid":false,"given":"Karin","family":"Fritz-Wolf","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jochen","family":"Bathke","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stefan","family":"Rahlfs","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Katja","family":"Becker","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.crstbi.2022.03.004_bib1","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.crstbi.2022.03.004_bib2","doi-asserted-by":"crossref","first-page":"25613","DOI":"10.1074\/jbc.274.36.25613","article-title":"The high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-I","volume":"274","author":"Alphey","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.crstbi.2022.03.004_bib3","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":"Arn\u00e9r","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.crstbi.2022.03.004_bib4","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1000541","article-title":"An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations","volume":"5","author":"Atkinson","year":"2009","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.crstbi.2022.03.004_bib5","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1046\/j.1432-1033.2003.03495.x","article-title":"Plasmoredoxin, a novel redox-active protein unique for malarial parasites","volume":"270","author":"Becker","year":"2003","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.crstbi.2022.03.004_bib6","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1111\/j.1365-2958.2006.05303.x","article-title":"Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum","volume":"61","author":"Boucher","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.crstbi.2022.03.004_bib7","doi-asserted-by":"crossref","first-page":"e2474","DOI":"10.1371\/journal.pone.0002474","article-title":"Depletion of Plasmodium berghei plasmoredoxin reveals a non-essential role for life cycle progression of the malaria parasite","volume":"3","author":"Buchholz","year":"2008","journal-title":"PLoS One"},{"key":"10.1016\/j.crstbi.2022.03.004_bib8","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1107\/S2059798317002066","article-title":"Is dimerization a common feature in thioredoxins? The case of thioredoxin from Litopenaeus vannamei","volume":"73","author":"Campos-Acevedo","year":"2017","journal-title":"Acta Crystallogr D Struct Biol"},{"key":"10.1016\/j.crstbi.2022.03.004_bib9","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.pbiomolbio.2005.06.012","article-title":"Similarities and differences in the thioredoxin superfamily","volume":"91","author":"Carvalho","year":"2006","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"10.1016\/j.crstbi.2022.03.004_bib10","first-page":"731","article-title":"Protein folding coupled to disulphide bond formation","volume":"378","author":"Creighton","year":"1997","journal-title":"Biol. Chem."},{"key":"10.1016\/j.crstbi.2022.03.004_bib11","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.crstbi.2022.03.004_bib12","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.crstbi.2022.03.004_bib13","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.crstbi.2022.03.004_bib14","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0001781","article-title":"The crystal structures of the tryparedoxin-tryparedoxin peroxidase couple unveil the structural determinants of Leishmania detoxification pathway","volume":"6","author":"Fiorillo","year":"2012","journal-title":"PLoS Neglected Trop. Dis."},{"key":"10.1016\/j.crstbi.2022.03.004_bib15","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1038\/ncomms1382","article-title":"Crystal structure of the human thioredoxin reductase-thioredoxin complex","volume":"2","author":"Fritz-Wolf","year":"2011","journal-title":"Nat. Commun."},{"key":"10.1016\/j.crstbi.2022.03.004_bib16","doi-asserted-by":"crossref","first-page":"3446","DOI":"10.1016\/j.jmb.2013.06.037","article-title":"Crystal structure of the Plasmodium falciparum thioredoxin reductase-thioredoxin complex","volume":"425","author":"Fritz-Wolf","year":"2013","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.crstbi.2022.03.004_bib17","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1002\/pro.3749","article-title":"DALI and the persistence of protein shape","volume":"29","author":"Holm","year":"2020","journal-title":"Protein Sci."},{"key":"10.1016\/j.crstbi.2022.03.004_bib18","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1089\/ars.2000.2.4-811","article-title":"Antioxidant function of thioredoxin and glutaredoxin systems","volume":"2","author":"Holmgren","year":"2000","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.crstbi.2022.03.004_bib19","doi-asserted-by":"crossref","first-page":"2305","DOI":"10.1073\/pnas.72.6.2305","article-title":"Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution","volume":"72","author":"Holmgren","year":"1975","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.crstbi.2022.03.004_bib20","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1002\/prot.22458","article-title":"Structure is three to ten times more conserved than sequence--a study of structural response in protein cores","volume":"77","author":"Illergard","year":"2009","journal-title":"Proteins"},{"key":"10.1016\/j.crstbi.2022.03.004_bib21","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.ijmm.2012.07.007","article-title":"Thioredoxin and glutathione systems in Plasmodium falciparum","volume":"302","author":"Jortzik","year":"2012","journal-title":"Int J Med Microbiol"},{"key":"10.1016\/j.crstbi.2022.03.004_bib22","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1107\/S0907444909047374","article-title":"Integration, scaling, space-group assignment and post-refinement","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.crstbi.2022.03.004_bib23","doi-asserted-by":"crossref","first-page":"10261","DOI":"10.1016\/S0021-9258(19)70458-X","article-title":"Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli","volume":"255","author":"Kallis","year":"1980","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.crstbi.2022.03.004_bib24","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 \u00c5 resolution","volume":"212","author":"Katti","year":"1990","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.crstbi.2022.03.004_bib25","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1515\/BC.2003.062","article-title":"The parasite-specific trypanothione metabolism of trypanosoma and leishmania","volume":"384","author":"Krauth-Siegel","year":"2003","journal-title":"Biol. Chem."},{"key":"10.1016\/j.crstbi.2022.03.004_bib26","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1107\/S0907444904026460","article-title":"Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions","volume":"60","author":"Krissinel","year":"2004","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.crstbi.2022.03.004_bib27","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/S0014-5793(98)00793-5","article-title":"Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes","volume":"431","author":"L\u00fcdemann","year":"1998","journal-title":"FEBS (Fed. Eur. Biochem. Soc.) Lett."},{"key":"10.1016\/j.crstbi.2022.03.004_bib28","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/S0969-2126(01)00154-X","article-title":"Thioredoxin \u2014a fold for all reasons","volume":"3","author":"Martin","year":"1995","journal-title":"Structure"},{"key":"10.1016\/j.crstbi.2022.03.004_bib29","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1042\/bj3590065","article-title":"Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism","volume":"359","author":"Menchise","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.crstbi.2022.03.004_bib30","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1515\/BC.2005.129","article-title":"Plasmodium falciparum 2-Cys peroxiredoxin reacts with plasmoredoxin and peroxynitrite","volume":"386","author":"Nickel","year":"2005","journal-title":"Biol. Chem."},{"key":"10.1016\/j.crstbi.2022.03.004_bib31","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1089\/ars.2006.8.1227","article-title":"Thioredoxin networks in the malarial parasite Plasmodium falciparum","volume":"8","author":"Nickel","year":"2006","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.crstbi.2022.03.004_bib32","doi-asserted-by":"crossref","first-page":"21645","DOI":"10.1074\/jbc.274.31.21645","article-title":"Identification of thioredoxin-binding protein-2\/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression","volume":"274","author":"Nishiyama","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.crstbi.2022.03.004_bib33","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.\u00a0Comput. Chem."},{"key":"10.1016\/j.crstbi.2022.03.004_bib34","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1007\/s00018-002-8484-9","article-title":"The thioredoxin system of Plasmodium falciparum and other parasites","volume":"59","author":"Rahlfs","year":"2002","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.crstbi.2022.03.004_bib35","doi-asserted-by":"crossref","first-page":"9701","DOI":"10.1021\/bi00088a023","article-title":"Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione","volume":"32","author":"Ren","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.crstbi.2022.03.004_bib36","doi-asserted-by":"crossref","first-page":"2596","DOI":"10.1093\/emboj\/17.9.2596","article-title":"Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1","volume":"17","author":"Saitoh","year":"1998","journal-title":"EMBO J."},{"key":"10.1016\/j.crstbi.2022.03.004_bib37","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega","volume":"7","author":"Sievers","year":"2011","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.crstbi.2022.03.004_bib38","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1110\/ps.051632905","article-title":"Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2","volume":"14","author":"Smeets","year":"2005","journal-title":"Protein Sci."},{"key":"10.1016\/j.crstbi.2022.03.004_bib39","doi-asserted-by":"crossref","first-page":"35809","DOI":"10.1074\/jbc.274.50.35809","article-title":"Thioredoxin-dependent redox regulation of p53-mediated p21 activation","volume":"274","author":"Ueno","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.crstbi.2022.03.004_bib40","doi-asserted-by":"crossref","first-page":"3640","DOI":"10.1002\/anie.201810470","article-title":"Inhibitor-induced dimerization of an essential oxidoreductase from African trypanosomes","volume":"58","author":"Wagner","year":"2019","journal-title":"Angew Chem. Int. Ed. Engl."},{"key":"10.1016\/j.crstbi.2022.03.004_bib41","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1016\/S0969-2126(96)00079-2","article-title":"Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer","volume":"4","author":"Weichsel","year":"1996","journal-title":"Structure"},{"key":"10.1016\/j.crstbi.2022.03.004_bib42","series-title":"World Malaria Report 2019","author":"WHO","year":"2019"},{"key":"10.1016\/j.crstbi.2022.03.004_bib43","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1107\/S1399004713025285","article-title":"Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins","volume":"70","author":"Yogavel","year":"2014","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."}],"container-title":["Current Research in Structural Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2665928X22000083?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2665928X22000083?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,12]],"date-time":"2025-11-12T09:35:37Z","timestamp":1762940137000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2665928X22000083"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022]]},"references-count":43,"alternative-id":["S2665928X22000083"],"URL":"https:\/\/doi.org\/10.1016\/j.crstbi.2022.03.004","relation":{},"ISSN":["2665-928X"],"issn-type":[{"value":"2665-928X","type":"print"}],"subject":[],"published":{"date-parts":[[2022]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Crystal structure of plasmoredoxin, a redox-active protein unique for malaria parasites","name":"articletitle","label":"Article Title"},{"value":"Current Research in Structural Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.crstbi.2022.03.004","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}