pubmed-article:11680787 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11680787 | lifeskim:mentions | umls-concept:C0043405 | lld:lifeskim |
pubmed-article:11680787 | lifeskim:mentions | umls-concept:C0205101 | lld:lifeskim |
pubmed-article:11680787 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:11680787 | lifeskim:mentions | umls-concept:C1166758 | lld:lifeskim |
pubmed-article:11680787 | lifeskim:mentions | umls-concept:C0174045 | lld:lifeskim |
pubmed-article:11680787 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
pubmed-article:11680787 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:11680787 | pubmed:dateCreated | 2001-10-26 | lld:pubmed |
pubmed-article:11680787 | pubmed:abstractText | Pathogenic species of the genus Yersinia employ a type III secretion apparatus to inject up to six effector proteins (Yersinia outer proteins; Yops) into host cells. Thereby yersiniae disarm the immune cell system of the host to proliferate extracellularly. At least four of the Yop effectors (YopE, YpkA/YopO, YopT and YopH) are involved in the rearrangement of the actin cytoskeleton: YopE, YopT and YpkA/YopO modulate the activity of actin-regulating Rho GTP-binding proteins, whereas YopH dephosphorylates phospho-tyrosine residues in focal adhesion proteins. In this review we will focus on recent evidence implicating Rho GTPases and the actin cytoskeleton as major targets of Yersinia Yops. | lld:pubmed |
pubmed-article:11680787 | pubmed:language | eng | lld:pubmed |
pubmed-article:11680787 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11680787 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11680787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11680787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11680787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11680787 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11680787 | pubmed:month | Sep | lld:pubmed |
pubmed-article:11680787 | pubmed:issn | 1438-4221 | lld:pubmed |
pubmed-article:11680787 | pubmed:author | pubmed-author:HeesemannJJ | lld:pubmed |
pubmed-article:11680787 | pubmed:author | pubmed-author:AepfelbacherM... | lld:pubmed |
pubmed-article:11680787 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11680787 | pubmed:volume | 291 | lld:pubmed |
pubmed-article:11680787 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11680787 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11680787 | pubmed:pagination | 269-76 | lld:pubmed |
pubmed-article:11680787 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:11680787 | pubmed:meshHeading | pubmed-meshheading:11680787... | lld:pubmed |
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pubmed-article:11680787 | pubmed:meshHeading | pubmed-meshheading:11680787... | lld:pubmed |
pubmed-article:11680787 | pubmed:meshHeading | pubmed-meshheading:11680787... | lld:pubmed |
pubmed-article:11680787 | pubmed:meshHeading | pubmed-meshheading:11680787... | lld:pubmed |
pubmed-article:11680787 | pubmed:meshHeading | pubmed-meshheading:11680787... | lld:pubmed |
pubmed-article:11680787 | pubmed:meshHeading | pubmed-meshheading:11680787... | lld:pubmed |
pubmed-article:11680787 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11680787 | pubmed:articleTitle | Modulation of Rho GTPases and the actin cytoskeleton by Yersinia outer proteins (Yops). | lld:pubmed |
pubmed-article:11680787 | pubmed:affiliation | Max-von-Pettenkofer Institut für Hygiene und Medizinische Mikrobiologie, München, Germany. aepfelbacher@m3401.mpk.med.uni-muenchen.de | lld:pubmed |
pubmed-article:11680787 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11680787 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:11680787 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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