{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T06:22:13Z","timestamp":1779344533262,"version":"3.51.4"},"reference-count":43,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[1997,4,1]],"date-time":"1997-04-01T00:00:00Z","timestamp":859852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":5951,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Current Biology"],"published-print":{"date-parts":[[1997,4]]},"DOI":"10.1016\/s0960-9822(06)00119-9","type":"journal-article","created":{"date-parts":[[2004,4,13]],"date-time":"2004-04-13T05:30:59Z","timestamp":1081834259000},"page":"239-245","source":"Crossref","is-referenced-by-count":186,"title":["The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules"],"prefix":"10.1016","volume":"7","author":[{"given":"Johan","family":"Kemmink","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nigel J","family":"Darby","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Klaas","family":"Dijkstra","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Nilges","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thomas E","family":"Creighton","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S0960-9822(06)00119-9_BIB1","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1016\/S0021-9258(18)81309-6","article-title":"Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver","volume":"238","author":"Goldberger","year":"1963","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB2","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/0926-6569(63)90223-2","article-title":"The enzymatic reactivation of reduced ribonuclease","volume":"67","author":"Venetianer","year":"1963","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB3","series-title":"Protein Folding","first-page":"455","article-title":"Protein folding in the cell","author":"Freedman","year":"1992"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB4","doi-asserted-by":"crossref","first-page":"3553","DOI":"10.1016\/S0021-9258(19)50556-7","article-title":"Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum","volume":"267","author":"Novia","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB5","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/317267a0","article-title":"Sequence of protein disulfide isomerase and implications of its relationship to thioredoxin","volume":"317","author":"Edman","year":"1985","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB6","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/S0969-2126(01)00154-X","article-title":"Thioredoxin \u2013 a fold for all reasons","volume":"3","author":"Martin","year":"1995","journal-title":"Structure"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB7","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/S0969-2126(01)00153-8","article-title":"Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide","volume":"3","author":"Holmgren","year":"1995","journal-title":"Structure"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB8","doi-asserted-by":"crossref","first-page":"8342","DOI":"10.1021\/bi960465v","article-title":"On the reactivity and ionization of the active-site cysteine residues of Escherichia coli thioredoxin","volume":"35","author":"Takahashi","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB9","doi-asserted-by":"crossref","first-page":"5083","DOI":"10.1021\/bi00070a016","article-title":"The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo","volume":"32","author":"Zapun","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB10","doi-asserted-by":"crossref","first-page":"16770","DOI":"10.1021\/bi00051a027","article-title":"Characterization of the active-site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase","volume":"34","author":"Darby","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB11","doi-asserted-by":"crossref","first-page":"5974","DOI":"10.1021\/bi00185a039","article-title":"Reactivity and ionization of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo","volume":"33","author":"Nelson","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB12","doi-asserted-by":"crossref","first-page":"3576","DOI":"10.1021\/bi00011a012","article-title":"Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase","volume":"34","author":"Darby","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB13","doi-asserted-by":"crossref","first-page":"10517","DOI":"10.1021\/bi960763s","article-title":"Identifying and characterizing a structural domain of protein disulfide isomerase","volume":"35","author":"Darby","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB14","doi-asserted-by":"crossref","first-page":"13967","DOI":"10.1016\/S0021-9258(18)71626-8","article-title":"Selective inhibition of protein disulfide isomerase by estrogens","volume":"264","author":"Tsibris","year":"1989","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB15","doi-asserted-by":"crossref","first-page":"7684","DOI":"10.1021\/bi960335m","article-title":"Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C\/15N NMR spectroscopy","volume":"35","author":"Kemmink","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB16","doi-asserted-by":"crossref","first-page":"11725","DOI":"10.1021\/bi00037a009","article-title":"Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase","volume":"34","author":"Darby","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB17","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1002\/pro.5560050516","article-title":"Protein fold recognition using sequence-derived predictions","volume":"5","author":"Fischer","year":"1996","journal-title":"Protein Sci"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB18","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1146\/annurev.bi.64.070195.001443","article-title":"The multiplicity of domains in proteins","volume":"64","author":"Doolittle","year":"1995","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB19","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1007\/BF02498636","article-title":"Intron position as an evolutionary marker of thioredoxins and thioredoxin domains","volume":"42","author":"Sahrawy","year":"1996","journal-title":"J Mol Evol"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB20","doi-asserted-by":"crossref","first-page":"3050","DOI":"10.1016\/S0021-9258(18)89471-6","article-title":"Structure and assembly of the endoplasmic reticulum","volume":"260","author":"Lewis","year":"1985","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB21","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1016\/S0021-9258(19)40163-4","article-title":"ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active-site sequence of protein disulfide isomerase","volume":"265","author":"Mazzarella","year":"1990","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB22","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\/S0960-9822(06)00119-9_BIB23","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1016\/S0969-2126(01)00245-3","article-title":"Crystal structure of thioredoxin-2 from Anabaena","volume":"3","author":"Saarinen","year":"1995","journal-title":"Structure"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB24","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/S0969-2126(01)00159-9","article-title":"Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF\u03baB","volume":"3","author":"Qin","year":"1995","journal-title":"Structure"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB25","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1002\/j.1460-2075.1987.tb04803.x","article-title":"Molecular cloning of the \u03b2-subunit of human prolyl 4-hydroxylase. This subunit and protein disulfide isomerase are products of the same gene","volume":"6","author":"Pihlajaniemi","year":"1987","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB26","doi-asserted-by":"crossref","first-page":"9800","DOI":"10.1016\/S0021-9258(19)38742-3","article-title":"Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex","volume":"265","author":"Wetterau","year":"1990","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB27","doi-asserted-by":"crossref","first-page":"4601","DOI":"10.1128\/MCB.12.10.4601","article-title":"The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase","volume":"12","author":"Tachibana","year":"1992","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB28","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1111\/j.1432-1033.1983.tb07429.x","article-title":"The refined structure of the selenoenzyme glutathione peroxidase at 0.2 nm resolution","volume":"133","author":"Epp","year":"1983","journal-title":"Eur J Biochem"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB29","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1002\/j.1460-2075.1991.tb07729.x","article-title":"The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 \u00c5 resolution","volume":"10","author":"Reinemer","year":"1991","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB30","doi-asserted-by":"crossref","first-page":"2587","DOI":"10.1002\/pro.5560041216","article-title":"Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase","volume":"4","author":"Kemmink","year":"1995","journal-title":"Protein Sci"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB31","first-page":"201","article-title":"An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins","volume":"99","author":"Grzesiek","year":"1992","journal-title":"J Magn Reson"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB32","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1007\/BF00178261","article-title":"Amino acid type determination in the sequential assignment procedure of uniformly 13C\/15N-enriched proteins","volume":"3","author":"Grzesiek","year":"1993","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB33","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1006\/jmrb.1993.1053","article-title":"A gradient-enhanced HCCH-TOCSY experiment for recording side-chain 1H and 13C correlations in H2O samples of proteins","volume":"101","author":"Kay","year":"1993","journal-title":"J Magn Reson B"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB34","first-page":"620","article-title":"Practical aspects of proton\u2013carbon\u2013carbon\u2013proton three-dimensional correlation spectroscopy of 13C-labelled proteins","volume":"87","author":"Bax","year":"1990","journal-title":"J Magn Reson"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB35","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1007\/BF00398416","article-title":"Measurement of HN\u2013H\u03b1 J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods","volume":"4","author":"Kuboniwa","year":"1994","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB36","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1007\/BF01874566","article-title":"Stereospecific assignments of \u03b2-methylene protons in larger proteins using 3D 15N-separated Hartmann\u2013Hahn and 13C-separated rotating frame Overhauser spectroscopy","volume":"1","author":"Clore","year":"1991","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB37","first-page":"636","article-title":"An alternative 3D NMR technique for correlating backbone 15N with side chain H\u03b2 resonances in larger proteins","volume":"95","author":"Archer","year":"1991","journal-title":"J Magn Reson"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB38","series-title":"X-PLOR Version 3.1. A System For X-ray Crystallography and NMR","author":"Br\u00fcnger","year":"1992"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB39","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/0014-5793(88)81148-7","article-title":"Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry\u2013dynamical simulated annealing calculations","volume":"229","author":"Nilges","year":"1988","journal-title":"FEBS Lett"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB40","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/0014-5793(87)81181-X","article-title":"A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data","volume":"219","author":"Nilges","year":"1987","journal-title":"FEBS Lett"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB41","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1107\/S0021889891004399","article-title":"MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures","volume":"24","author":"Kraulis","year":"1991","journal-title":"J Appl Crystallog"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB42","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1006\/jmbi.1993.1489","article-title":"Protein structure comparison by alignment of distance matrices","volume":"233","author":"Holm","year":"1993","journal-title":"J Mol Biol"},{"key":"10.1016\/S0960-9822(06)00119-9_BIB43","first-page":"3600","article-title":"The FSSP database of structurally aligned protein fold families","volume":"22","author":"Holm","year":"1994","journal-title":"Nucl Acids Res"}],"container-title":["Current Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0960982206001199?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0960982206001199?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,15]],"date-time":"2021-06-15T11:15:21Z","timestamp":1623755721000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0960982206001199"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,4]]},"references-count":43,"journal-issue":{"issue":"4","published-print":{"date-parts":[[1997,4]]}},"alternative-id":["S0960982206001199"],"URL":"https:\/\/doi.org\/10.1016\/s0960-9822(06)00119-9","relation":{},"ISSN":["0960-9822"],"issn-type":[{"value":"0960-9822","type":"print"}],"subject":[],"published":{"date-parts":[[1997,4]]}}}