{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,4]],"date-time":"2026-03-04T08:31:50Z","timestamp":1772613110028,"version":"3.50.1"},"reference-count":34,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2002,3,1]],"date-time":"2002-03-01T00:00:00Z","timestamp":1014940800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,16]],"date-time":"2013-07-16T00:00:00Z","timestamp":1373932800000},"content-version":"vor","delay-in-days":4155,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Cell"],"published-print":{"date-parts":[[2002,3]]},"DOI":"10.1016\/s1097-2765(02)00485-9","type":"journal-article","created":{"date-parts":[[2004,4,21]],"date-time":"2004-04-21T06:04:48Z","timestamp":1082527488000},"page":"673-683","source":"Crossref","is-referenced-by-count":255,"title":["ClpS, a Substrate Modulator of the ClpAP Machine"],"prefix":"10.1016","volume":"9","author":[{"given":"David A","family":"Dougan","sequence":"first","affiliation":[]},{"given":"Brian G","family":"Reid","sequence":"additional","affiliation":[]},{"given":"Arthur L","family":"Horwich","sequence":"additional","affiliation":[]},{"given":"Bernd","family":"Bukau","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S1097-2765(02)00485-9_BIB1","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1038\/35001629","article-title":"The structures of HsIU and the ATP-dependent protease HsIU-HsIV","volume":"403","author":"Bochtler","year":"2000","journal-title":"Nature"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB2","doi-asserted-by":"crossref","first-page":"6640","DOI":"10.1073\/pnas.120163297","article-title":"One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products","volume":"97","author":"Datsenko","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB3","doi-asserted-by":"crossref","first-page":"10584","DOI":"10.1073\/pnas.191375298","article-title":"Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis","volume":"98","author":"Flynn","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB4","doi-asserted-by":"crossref","first-page":"13732","DOI":"10.1073\/pnas.96.24.13732","article-title":"Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network","volume":"96","author":"Goloubinoff","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB5","doi-asserted-by":"crossref","first-page":"5251","DOI":"10.1093\/emboj\/19.19.5251","article-title":"Subunit-specific degradation of the UmuD\/D\u2032 heterodimer by the ClpXP protease","volume":"19","author":"Gonzalez","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB6","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/S1369-5274(99)80025-3","article-title":"Regulation by proteolysis","volume":"2","author":"Gottesman","year":"1999","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB7","doi-asserted-by":"crossref","first-page":"7886","DOI":"10.1016\/S0021-9258(19)39014-3","article-title":"The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate","volume":"265","author":"Gottesman","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB8","doi-asserted-by":"crossref","first-page":"22618","DOI":"10.1016\/S0021-9258(18)41573-6","article-title":"ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities","volume":"268","author":"Gottesman","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB9","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.1101\/gad.12.9.1338","article-title":"The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system","volume":"12","author":"Gottesman","year":"1998","journal-title":"Genes Dev."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB10","doi-asserted-by":"crossref","first-page":"35361","DOI":"10.1074\/jbc.M006288200","article-title":"Substrate recognition by the ClpA chaperone component of ClpAP protease","volume":"275","author":"Hoskins","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB11","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1126\/science.271.5251.990","article-title":"Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA","volume":"271","author":"Keiler","year":"1996","journal-title":"Science"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB12","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1038\/40411","article-title":"p47 is a cofactor for p97-mediated membrane fusion","volume":"388","author":"Kondo","year":"1997","journal-title":"Nature"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB13","doi-asserted-by":"crossref","first-page":"2354","DOI":"10.1126\/science.289.5488.2354","article-title":"A specificity-enhancing factor for the ClpXP degradation machine","volume":"289","author":"Levchenko","year":"2000","journal-title":"Science"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB14","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1110\/ps.41401","article-title":"Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp\/HSP100 ATPase","volume":"10","author":"Lo","year":"2001","journal-title":"Protein Sci."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB15","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.1093\/emboj\/19.10.2181","article-title":"A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways","volume":"19","author":"Meyer","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB16","doi-asserted-by":"crossref","first-page":"6934","DOI":"10.1093\/emboj\/18.24.6934","article-title":"Identification of thermolabile Escherichia coli proteins","volume":"18","author":"Mogk","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB17","doi-asserted-by":"crossref","first-page":"7184","DOI":"10.1073\/pnas.96.13.7184","article-title":"Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones","volume":"96","author":"Motohashi","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB18","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1002\/j.1460-2075.1996.tb00475.x","article-title":"The response regulator RssB controls stability of the sigma(S) subunit of RNA polymerase in Escherichia coli","volume":"15","author":"Muffler","year":"1996","journal-title":"EMBO J."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB19","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1101\/gr.9.1.27","article-title":"Aaa+","volume":"9","author":"Neuwald","year":"1999","journal-title":"Genome Res."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB20","doi-asserted-by":"crossref","first-page":"2488","DOI":"10.1073\/pnas.93.6.2488","article-title":"The response regulator SprE controls the stability of RpoS","volume":"93","author":"Pratt","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB21","doi-asserted-by":"crossref","first-page":"3768","DOI":"10.1073\/pnas.071043698","article-title":"ClpA mediates directional translocation of substrate proteins into the ClpP protease","volume":"98","author":"Reid","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB22","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1016\/S1097-2765(00)00144-1","article-title":"A major conformational change in p97 AAA ATPase upon ATP binding","volume":"6","author":"Rouiller","year":"2000","journal-title":"Mol. Cell"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB23","doi-asserted-by":"crossref","first-page":"4137","DOI":"10.1002\/j.1460-2075.1993.tb06097.x","article-title":"DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage","volume":"12","author":"Schr\u00f6der","year":"1993","journal-title":"EMBO J."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB24","doi-asserted-by":"crossref","first-page":"6678","DOI":"10.1073\/pnas.96.12.6678","article-title":"Lon and Clp family proteases and chaperones share homologous substrate-recognition domains","volume":"96","author":"Smith","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB25","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/S0092-8674(00)00166-5","article-title":"Crystal and solution structures of an HslUV protease-chaperone complex","volume":"103","author":"Sousa","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB26","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.1126\/science.1962196","article-title":"The N-end rule in bacteria","volume":"254","author":"Tobias","year":"1991","journal-title":"Science"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB27","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1101\/gad.11.1.119","article-title":"Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis","volume":"11","author":"Turgay","year":"1997","journal-title":"Genes Dev."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB28","doi-asserted-by":"crossref","first-page":"6730","DOI":"10.1093\/emboj\/17.22.6730","article-title":"Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor","volume":"17","author":"Turgay","year":"1998","journal-title":"EMBO J."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB29","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1016\/S0092-8674(00)80431-6","article-title":"The structure of ClpP at 2.3 \u00c5 resolution suggests a model for ATP-dependent proteolysis","volume":"91","author":"Wang","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB30","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1038\/43481","article-title":"Global unfolding of a substrate protein by the Hsp100 chaperone ClpA","volume":"401","author":"Weber-Ban","year":"1999","journal-title":"Nature"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB31","doi-asserted-by":"crossref","first-page":"12218","DOI":"10.1073\/pnas.91.25.12218","article-title":"A molecular chaperone, ClpA, functions like DnaK and DnaJ","volume":"91","author":"Wickner","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB32","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.1126\/science.286.5446.1888","article-title":"Posttranslational quality control","volume":"286","author":"Wickner","year":"1999","journal-title":"Science"},{"key":"10.1016\/S1097-2765(02)00485-9_BIB33","doi-asserted-by":"crossref","first-page":"22609","DOI":"10.1016\/S0021-9258(18)41572-4","article-title":"Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli","volume":"268","author":"Wojtkowiak","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1097-2765(02)00485-9_BIB34","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1101\/gad.864401","article-title":"The RssB response regulator directly targets \u03c3S for degradation by ClpXP","volume":"15","author":"Zhou","year":"2001","journal-title":"Genes Dev."}],"container-title":["Molecular Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1097276502004859?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1097276502004859?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,4,28]],"date-time":"2023-04-28T11:56:26Z","timestamp":1682682986000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1097276502004859"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,3]]},"references-count":34,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2002,3]]}},"alternative-id":["S1097276502004859"],"URL":"https:\/\/doi.org\/10.1016\/s1097-2765(02)00485-9","relation":{},"ISSN":["1097-2765"],"issn-type":[{"value":"1097-2765","type":"print"}],"subject":[],"published":{"date-parts":[[2002,3]]}}}