{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T19:56:36Z","timestamp":1760298996067},"reference-count":26,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2014,9,1]],"date-time":"2014-09-01T00:00:00Z","timestamp":1409529600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"name":"Ministry of Science and Technology of China","award":["2012CB917202","2013CB910200"],"award-info":[{"award-number":["2012CB917202","2013CB910200"]}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31100538","31100847","31470740"],"award-info":[{"award-number":["31100538","31100847","31470740"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2014,9]]},"DOI":"10.1016\/j.bbrc.2014.09.002","type":"journal-article","created":{"date-parts":[[2014,9,7]],"date-time":"2014-09-07T08:08:40Z","timestamp":1410077320000},"page":"817-821","update-policy":"http:\/\/dx.doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":6,"title":["Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP"],"prefix":"10.1016","volume":"452","author":[{"given":"Wei","family":"Wang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peng","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yao","family":"He","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lu","family":"Yu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ying","family":"Xiong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Changlin","family":"Tian","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fangming","family":"Wu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2014.09.002_b0005","first-page":"243","article-title":"Die rhodanbildung in tierkorper","volume":"259","author":"Lang","year":"1933","journal-title":"Biochem. Z."},{"key":"10.1016\/j.bbrc.2014.09.002_b0010","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1016\/S0272-0590(83)80008-6","article-title":"The sulfurtransferases","volume":"3","author":"Westley","year":"1983","journal-title":"Fundam. Appl. Toxicol."},{"key":"10.1016\/j.bbrc.2014.09.002_b0015","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1080\/15216540701206859","article-title":"Common themes and variations in the rhodanese superfamily","volume":"59","author":"Cipollone","year":"2007","journal-title":"IUBMB Life"},{"key":"10.1016\/j.bbrc.2014.09.002_b0020","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1093\/embo-reports\/kvf150","article-title":"The rhodanese\/Cdc25 phosphatase superfamily. Sequence-structure-function relations","volume":"3","author":"Bordo","year":"2002","journal-title":"EMBO Rep."},{"key":"10.1016\/j.bbrc.2014.09.002_b0025","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1038\/273124a0","article-title":"The covalent and tertiary structure of bovine liver rhodanese","volume":"273","author":"Ploegman","year":"1978","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2014.09.002_b0030","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/S1357-2725(99)00035-7","article-title":"Rhodanese as a thioredoxin oxidase","volume":"32","author":"Nandi","year":"2000","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.bbrc.2014.09.002_b0035","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1006\/jmbi.2000.3651","article-title":"The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families","volume":"298","author":"Bordo","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbrc.2014.09.002_b0040","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1016\/S0092-8674(00)81190-3","article-title":"Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A","volume":"93","author":"Fauman","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.bbrc.2014.09.002_b0045","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1006\/jmbi.1999.3168","article-title":"Crystal structure of the catalytic subunit of Cdc25B required for G2\/M phase transition of the cell cycle","volume":"293","author":"Reynolds","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbrc.2014.09.002_b0050","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1126\/science.277.5331.1453","article-title":"The complete genome sequence of Escherichia coli K-12","volume":"277","author":"Blattner","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.bbrc.2014.09.002_b0055","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1016\/S0969-2126(01)00666-9","article-title":"Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily","volume":"9","author":"Spallarossa","year":"2001","journal-title":"Structure"},{"key":"10.1016\/j.bbrc.2014.09.002_b0060","doi-asserted-by":"crossref","first-page":"e54378","DOI":"10.1371\/journal.pone.0054378","article-title":"Detergent\/nanodisc screening for high-resolution NMR studies of an integral membrane protein containing a cytoplasmic domain","volume":"8","author":"Tzitzilonis","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bbrc.2014.09.002_b0065","doi-asserted-by":"crossref","first-page":"4377","DOI":"10.1021\/bi800039n","article-title":"Solution structures and backbone dynamics of Escherichia coli rhodanese PspE in its sulfur-free and persulfide-intermediate forms: implications for the catalytic mechanism of rhodanese","volume":"47","author":"Li","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2014.09.002_b0070","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M114.571935","article-title":"Solution NMR structure and functional analysis of the integral membrane protein YgaP from E. coli","author":"Eichmann","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2014.09.002_b0075","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.bbrc.2014.09.002_b0080","article-title":"UCSF sparky \u2013 an NMR display, annotation and assignment tool","author":"Kneller","year":"1993","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.bbrc.2014.09.002_b0085","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1007\/s10858-009-9333-z","article-title":"TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts","volume":"44","author":"Shen","year":"2009","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.bbrc.2014.09.002_b0090","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S1090-7807(02)00014-9","article-title":"The Xplor-NIH NMR molecular structure determination package","volume":"160","author":"Schwieters","year":"2003","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.bbrc.2014.09.002_b0095","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1007\/BF00228148","article-title":"AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR","volume":"8","author":"Laskowski","year":"1996","journal-title":"J. Biomol. NMR"},{"issue":"51\u201355","key":"10.1016\/j.bbrc.2014.09.002_b0100","first-page":"29","article-title":"MOLMOL: a program for display and analysis of macromolecular structures","volume":"14","author":"Koradi","year":"1996","journal-title":"J. Mol. Graph."},{"key":"10.1016\/j.bbrc.2014.09.002_b0105","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1093\/nar\/29.1.221","article-title":"PDBsum: summaries and analyses of PDB structures","volume":"29","author":"Laskowski","year":"2001","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbrc.2014.09.002_b0110","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/s12104-010-9277-y","article-title":"1H, 13C and 15N resonance assignments of the rhodanese domain of YgaP from Escherichia coli","volume":"5","author":"Li","year":"2011","journal-title":"Biomol. NMR Assign"},{"key":"10.1016\/j.bbrc.2014.09.002_b0115","doi-asserted-by":"crossref","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.bbrc.2014.09.002_b0120","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering key features in protein structures with the new ENDscript server","volume":"42","author":"Robert","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbrc.2014.09.002_b0125","doi-asserted-by":"crossref","first-page":"2780","DOI":"10.1093\/bioinformatics\/btn507","article-title":"Searching protein structure databases with DaliLite v. 3","volume":"24","author":"Holm","year":"2008","journal-title":"Bioinformatics"},{"key":"10.1016\/j.bbrc.2014.09.002_b0130","doi-asserted-by":"crossref","first-page":"3623","DOI":"10.1021\/cr030413t","article-title":"NMR characterization of the dynamics of biomacromolecules","volume":"104","author":"Palmer","year":"2004","journal-title":"Chem. Rev."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X14015915?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X14015915?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,8,14]],"date-time":"2019-08-14T15:09:28Z","timestamp":1565795368000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X14015915"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,9]]},"references-count":26,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2014,9]]}},"alternative-id":["S0006291X14015915"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2014.09.002","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2014,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrc.2014.09.002","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}