pubmed-article:10506187 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10506187 | lifeskim:mentions | umls-concept:C0043406 | lld:lifeskim |
pubmed-article:10506187 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
pubmed-article:10506187 | lifeskim:mentions | umls-concept:C0010868 | lld:lifeskim |
pubmed-article:10506187 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
pubmed-article:10506187 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
pubmed-article:10506187 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:10506187 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
pubmed-article:10506187 | pubmed:issue | 41 | lld:pubmed |
pubmed-article:10506187 | pubmed:dateCreated | 1999-11-9 | lld:pubmed |
pubmed-article:10506187 | pubmed:abstractText | Pathogenic Yersinia enterocolitica produces two virulence plasmid-encoded cytotoxins, YopE and YopT, that are translocated into target cells where they disrupt the actin cytoskeleton. Here we show that infection of cells with wild type Y. enterocolitica and a yopE mutant, but not with a yopT mutant, induces an increase in the electrophoretic mobility of the small GTPase RhoA. As tested by isoelectric focusing, YopT-dependent modification resulted in an acidic shift of RhoA. Furthermore, RhoA modification induced by YopT was accompanied by redistribution of membrane-bound RhoA toward the cytosol. Finally, a yopE mutant of Y. enterocolitica expressing the cytotoxic activity of YopT specifically disrupted RhoA-controlled actin stress fibers. These findings provide evidence for inactivation of RhoA by the translocated Y. enterocolitica cytotoxin YopT and suggest a novel inhibitory modification of RhoA by a bacterial virulence factor. | lld:pubmed |
pubmed-article:10506187 | pubmed:language | eng | lld:pubmed |
pubmed-article:10506187 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10506187 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10506187 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10506187 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10506187 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10506187 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10506187 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10506187 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10506187 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10506187 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10506187 | pubmed:month | Oct | lld:pubmed |
pubmed-article:10506187 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10506187 | pubmed:author | pubmed-author:RouotBB | lld:pubmed |
pubmed-article:10506187 | pubmed:author | pubmed-author:HeesemannJJ | lld:pubmed |
pubmed-article:10506187 | pubmed:author | pubmed-author:AepfelbacherM... | lld:pubmed |
pubmed-article:10506187 | pubmed:author | pubmed-author:AndohKK | lld:pubmed |
pubmed-article:10506187 | pubmed:author | pubmed-author:ZumbihlRR | lld:pubmed |
pubmed-article:10506187 | pubmed:author | pubmed-author:JacobsC WCW | lld:pubmed |
pubmed-article:10506187 | pubmed:author | pubmed-author:RuckdeschelKK | lld:pubmed |
pubmed-article:10506187 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10506187 | pubmed:day | 8 | lld:pubmed |
pubmed-article:10506187 | pubmed:volume | 274 | lld:pubmed |
pubmed-article:10506187 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10506187 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10506187 | pubmed:pagination | 29289-93 | lld:pubmed |
pubmed-article:10506187 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:10506187 | pubmed:meshHeading | pubmed-meshheading:10506187... | lld:pubmed |
pubmed-article:10506187 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10506187 | pubmed:articleTitle | The cytotoxin YopT of Yersinia enterocolitica induces modification and cellular redistribution of the small GTP-binding protein RhoA. | lld:pubmed |
pubmed-article:10506187 | pubmed:affiliation | Max von Pettenkofer Institut für Hygiene und Mikrobiologie, Pettenkoferstrasse 9a, 80336 Munich, Germany. | lld:pubmed |
pubmed-article:10506187 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10506187 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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