{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T04:40:35Z","timestamp":1793508035868,"version":"4.5.0"},"reference-count":44,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2006,9,1]],"date-time":"2006-09-01T00:00:00Z","timestamp":1157068800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2006,9,1]],"date-time":"2006-09-01T00:00:00Z","timestamp":1157068800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2013,8,22]],"date-time":"2013-08-22T00:00:00Z","timestamp":1377129600000},"content-version":"vor","delay-in-days":2547,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2006,9,1]],"date-time":"2006-09-01T00:00:00Z","timestamp":1157068800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2006,9,1]],"date-time":"2006-09-01T00:00:00Z","timestamp":1157068800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2006,9,1]],"date-time":"2006-09-01T00:00:00Z","timestamp":1157068800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2006,9,1]],"date-time":"2006-09-01T00:00:00Z","timestamp":1157068800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2006,9,1]],"date-time":"2006-09-01T00:00:00Z","timestamp":1157068800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell"],"published-print":{"date-parts":[[2006,9]]},"DOI":"10.1016\/j.cell.2006.06.056","type":"journal-article","created":{"date-parts":[[2006,9,8]],"date-time":"2006-09-08T15:25:10Z","timestamp":1157729110000},"page":"869-880","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":116,"title":["Yersinia Virulence Depends on Mimicry of Host Rho-Family Nucleotide Dissociation Inhibitors"],"prefix":"10.1016","volume":"126","author":[{"given":"Gerd","family":"Prehna","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maya I.","family":"Ivanov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James B.","family":"Bliska","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C. Erec","family":"Stebbins","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cell.2006.06.056_bib1","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1007\/s10254-004-0035-3","article-title":"Modulation of Rho GTPases by type III secretion system translocated effectors of Yersinia","volume":"152","author":"Aepfelbacher","year":"2004","journal-title":"Rev. Physiol. Biochem. Pharmacol."},{"key":"10.1016\/j.cell.2006.06.056_bib2","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1515\/BC.1999.099","article-title":"The tranquilizing injection of Yersinia proteins: a pathogen's strategy to resist host defense","volume":"380","author":"Aepfelbacher","year":"1999","journal-title":"Biol. Chem."},{"key":"10.1016\/j.cell.2006.06.056_bib3","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0014-5793(00)02045-7","article-title":"The Yersinia Ser\/Thr protein kinase YpkA\/YopO directly interacts with the small GTPases RhoA and Rac-1","volume":"482","author":"Barz","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1016\/j.cell.2006.06.056_bib4","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1046\/j.1365-2958.2000.02021.x","article-title":"The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence","volume":"37","author":"Black","year":"2000","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.cell.2006.06.056_bib5","doi-asserted-by":"crossref","first-page":"3286","DOI":"10.1093\/emboj\/cdf329","article-title":"Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE","volume":"21","author":"Buchwald","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.cell.2006.06.056_bib6","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","year":"1994","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cell.2006.06.056_bib7","doi-asserted-by":"crossref","first-page":"8778","DOI":"10.1073\/pnas.97.16.8778","article-title":"Molecular and cell biology aspects of plague","volume":"97","author":"Cornelis","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2006.06.056_bib8","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1038\/nrm932","article-title":"The Yersinia Ysc-Yop \u2018type III\u2019 weaponry","volume":"3","author":"Cornelis","year":"2002","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.cell.2006.06.056_bib9","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1128\/MMBR.62.4.1315-1352.1998","article-title":"The virulence plasmid of Yersinia, an\u00a0antihost genome","volume":"62","author":"Cornelis","year":"1998","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.cell.2006.06.056_bib10","doi-asserted-by":"crossref","first-page":"35281","DOI":"10.1074\/jbc.M003009200","article-title":"The Yersinia protein kinase A is\u00a0a host factor inducible RhoA\/Rac-binding virulence factor","volume":"275","author":"Dukuzumuremyi","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2006.06.056_bib11","doi-asserted-by":"crossref","first-page":"1130","DOI":"10.1038\/sj.embor.7400293","article-title":"Always look on the bright site of Rho: structural implications for a conserved intermolecular interface","volume":"5","author":"Dvorsky","year":"2004","journal-title":"EMBO Rep."},{"key":"10.1016\/j.cell.2006.06.056_bib12","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/S0076-6879(00)25433-5","article-title":"Purification and biochemical activity of Salmonella exchange factor SopE","volume":"325","author":"Friebel","year":"2000","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.cell.2006.06.056_bib13","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1126\/science.284.5418.1322","article-title":"Type III secretion machines: bacterial devices for protein delivery into host cells","volume":"284","author":"Gal\u00e1n","year":"1999","journal-title":"Science"},{"key":"10.1016\/j.cell.2006.06.056_bib14","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1056\/NEJM199709043371004","article-title":"Multidrug resistance in Yersinia pestis mediated by a transferable plasmid","volume":"337","author":"Galimand","year":"1997","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.cell.2006.06.056_bib15","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1038\/361730a0","article-title":"A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant","volume":"361","author":"Galyov","year":"1993","journal-title":"Nature"},{"key":"10.1016\/j.cell.2006.06.056_bib16","doi-asserted-by":"crossref","first-page":"4543","DOI":"10.1128\/jb.176.15.4543-4548.1994","article-title":"Characterization of the operon encoding the YpkA Ser\/Thr protein kinase and the YopJ protein of Yersinia pseudotuberculosis","volume":"176","author":"Galyov","year":"1994","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.cell.2006.06.056_bib17","doi-asserted-by":"crossref","first-page":"10007","DOI":"10.1021\/bi010288k","article-title":"Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation","volume":"40","author":"Grizot","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.cell.2006.06.056_bib18","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1046\/j.1365-2958.1996.5251051.x","article-title":"The Yersinia YpkA Ser\/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane","volume":"20","author":"Hakansson","year":"1996","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.cell.2006.06.056_bib19","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1016\/S0092-8674(00)81442-7","article-title":"S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells","volume":"93","author":"Hardt","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.cell.2006.06.056_bib20","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1126\/science.283.5406.1279","article-title":"The looming threat of bioterrorism","volume":"283","author":"Henderson","year":"1999","journal-title":"Science"},{"key":"10.1016\/j.cell.2006.06.056_bib21","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/S0092-8674(02)00741-9","article-title":"The conformational plasticity of protein kinases","volume":"109","author":"Huse","year":"2002","journal-title":"Cell"},{"key":"10.1016\/j.cell.2006.06.056_bib22","doi-asserted-by":"crossref","first-page":"2281","DOI":"10.1001\/jama.283.17.2281","article-title":"Plague as a biological weapon: medical and public health management. Working group on civilian biodefense","volume":"283","author":"Inglesby","year":"2000","journal-title":"JAMA"},{"key":"10.1016\/j.cell.2006.06.056_bib24","doi-asserted-by":"crossref","first-page":"9431","DOI":"10.1073\/pnas.170281997","article-title":"A distinctive role for the Yersinia protein kinase: actin binding, kinase activation, and cytoskeleton disruption","volume":"97","author":"Juris","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2006.06.056_bib25","doi-asserted-by":"crossref","first-page":"4595","DOI":"10.1128\/IAI.71.8.4595-4607.2003","article-title":"Requirement of the Yersinia pseudotuberculosis effectors YopH and YopE in colonization and persistence in intestinal and lymph tissues","volume":"71","author":"Logsdon","year":"2003","journal-title":"Infect. Immun."},{"key":"10.1016\/j.cell.2006.06.056_bib26","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1016\/S1097-2765(00)80389-5","article-title":"The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN\/PRK1","volume":"4","author":"Maesaki","year":"1999","journal-title":"Mol. Cell"},{"key":"10.1016\/j.cell.2006.06.056_bib27","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1006\/jsbi.1999.4114","article-title":"Biochemical and crystallographic characterization of a Rho effector domain of the protein serine\/threonine kinase N in a complex with RhoA","volume":"126","author":"Maesaki","year":"1999","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.cell.2006.06.056_bib28","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/S1369-5274(98)80152-5","article-title":"Epidemiology of emerging\/re-emerging antimicrobial-resistant bacterial pathogens","volume":"1","author":"McCormick","year":"1998","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.cell.2006.06.056_bib29","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cell.2006.06.056_bib30","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1002\/yea.1135","article-title":"Actin distribution is disrupted upon expression of Yersinia YopO\/YpkA in yeast","volume":"21","author":"Nejedlik","year":"2004","journal-title":"Yeast"},{"key":"10.1016\/j.cell.2006.06.056_bib31","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1038\/8263","article-title":"Automated protein model building combined with iterative structure refinement","volume":"6","author":"Perrakis","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.cell.2006.06.056_bib32","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1128\/CMR.10.1.35","article-title":"Yersinia pestis\u2013etiologic agent of plague","volume":"10","author":"Perry","year":"1997","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.cell.2006.06.056_bib33","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1107\/S0907444903008126","article-title":"A\u00a0graphical user interface to the CCP4 program suite","volume":"59","author":"Potterton","year":"2003","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cell.2006.06.056_bib35","doi-asserted-by":"crossref","first-page":"30501","DOI":"10.1074\/jbc.274.43.30501","article-title":"Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for RhoGTPases","volume":"274","author":"Rudolph","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2006.06.056_bib36","doi-asserted-by":"crossref","first-page":"9851","DOI":"10.1021\/bi00088a041","article-title":"Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: an X-ray analysis at 1.8-A resolution","volume":"32","author":"Rypniewski","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.cell.2006.06.056_bib37","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1038\/72392","article-title":"The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI","volume":"7","author":"Scheffzek","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.cell.2006.06.056_bib38","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1016\/S0092-8674(02)00766-3","article-title":"A\u00a0Yersinia effector and a Pseudomonas avirulence protein define a\u00a0family\u00a0of cysteine proteases functioning in bacterial pathogenesis","volume":"109","author":"Shao","year":"2002","journal-title":"Cell"},{"key":"10.1016\/j.cell.2006.06.056_bib39","doi-asserted-by":"crossref","first-page":"4414","DOI":"10.1128\/iai.60.10.4414-4417.1992","article-title":"Invasin expression in Yersinia pseudotuberculosis","volume":"60","author":"Simonet","year":"1992","journal-title":"Infect. Immun."},{"key":"10.1016\/j.cell.2006.06.056_bib40","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1038\/35089000","article-title":"Structural mimicry in bacterial virulence","volume":"412","author":"Stebbins","year":"2001","journal-title":"Nature"},{"key":"10.1016\/j.cell.2006.06.056_bib41","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1107\/S0909049503023938","article-title":"SOLVE and RESOLVE: automated structure solution, density modification and model building","volume":"11","author":"Terwilliger","year":"2004","journal-title":"J. Synchrotron Radiat."},{"key":"10.1016\/j.cell.2006.06.056_bib42","doi-asserted-by":"crossref","first-page":"5227","DOI":"10.1128\/IAI.72.9.5227-5234.2004","article-title":"Contribution of the major secreted Yops of Yersinia enterocolitica O:8 to pathogenicity in the mouse infection model","volume":"72","author":"Tr\u00fclzsch","year":"2004","journal-title":"Infect. Immun."},{"key":"10.1016\/j.cell.2006.06.056_bib43","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1146\/annurev.micro.59.030804.121320","article-title":"Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis","volume":"59","author":"Viboud","year":"2005","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.cell.2006.06.056_bib44","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1038\/nsb0997-699","article-title":"Crystal structure of RhoA-GDP and its functional implications","volume":"4","author":"Wei","year":"1997","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.cell.2006.06.056_bib45","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1107\/S0907444900014736","article-title":"Use of TLS parameters to model anisotropic displacements in macromolecular refinement","volume":"57","author":"Winn","year":"2001","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cell.2006.06.056_bib46","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/S0076-6879(03)74014-2","article-title":"Macromolecular TLS refinement in REFMAC at moderate resolutions","volume":"374","author":"Winn","year":"2003","journal-title":"Methods Enzymol."}],"container-title":["Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867406010178?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867406010178?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,25]],"date-time":"2025-09-25T10:56:23Z","timestamp":1758797783000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0092867406010178"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,9]]},"references-count":44,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2006,9]]}},"alternative-id":["S0092867406010178"],"URL":"https:\/\/doi.org\/10.1016\/j.cell.2006.06.056","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.1040864.496452","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.1040864.490918","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.1040864.497087","asserted-by":"object"}]},"ISSN":["0092-8674"],"issn-type":[{"value":"0092-8674","type":"print"}],"subject":[],"published":{"date-parts":[[2006,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Yersinia Virulence Depends on Mimicry of Host Rho-Family Nucleotide Dissociation Inhibitors","name":"articletitle","label":"Article Title"},{"value":"Cell","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cell.2006.06.056","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2006 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}