pubmed-article:10998597 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10998597 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
pubmed-article:10998597 | lifeskim:mentions | umls-concept:C0018296 | lld:lifeskim |
pubmed-article:10998597 | lifeskim:mentions | umls-concept:C1412517 | lld:lifeskim |
pubmed-article:10998597 | lifeskim:mentions | umls-concept:C1423613 | lld:lifeskim |
pubmed-article:10998597 | lifeskim:mentions | umls-concept:C1707719 | lld:lifeskim |
pubmed-article:10998597 | lifeskim:mentions | umls-concept:C0205352 | lld:lifeskim |
pubmed-article:10998597 | lifeskim:mentions | umls-concept:C1720675 | lld:lifeskim |
pubmed-article:10998597 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:10998597 | pubmed:dateCreated | 2000-11-7 | lld:pubmed |
pubmed-article:10998597 | pubmed:abstractText | Rho family GTPases control a large variety of biological processes. Cycling of Rho proteins between the GDP-bound and the GTP-bound state is controlled by several classes of regulatory proteins. In this review, we discuss the signal-transduction mechanisms that control these regulators. We will emphasize the subcellular localization of Rho GTPases and their regulatory proteins and the role of GTP hydrolysis in signal transmission. | lld:pubmed |
pubmed-article:10998597 | pubmed:language | eng | lld:pubmed |
pubmed-article:10998597 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998597 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10998597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998597 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10998597 | pubmed:month | Oct | lld:pubmed |
pubmed-article:10998597 | pubmed:issn | 0962-8924 | lld:pubmed |
pubmed-article:10998597 | pubmed:author | pubmed-author:SymonsMM | lld:pubmed |
pubmed-article:10998597 | pubmed:author | pubmed-author:SettlemanJJ | lld:pubmed |
pubmed-article:10998597 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10998597 | pubmed:volume | 10 | lld:pubmed |
pubmed-article:10998597 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10998597 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10998597 | pubmed:pagination | 415-9 | lld:pubmed |
pubmed-article:10998597 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
pubmed-article:10998597 | pubmed:meshHeading | pubmed-meshheading:10998597... | lld:pubmed |
pubmed-article:10998597 | pubmed:meshHeading | pubmed-meshheading:10998597... | lld:pubmed |
pubmed-article:10998597 | pubmed:meshHeading | pubmed-meshheading:10998597... | lld:pubmed |
pubmed-article:10998597 | pubmed:meshHeading | pubmed-meshheading:10998597... | lld:pubmed |
pubmed-article:10998597 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10998597 | pubmed:articleTitle | Rho family GTPases: more than simple switches. | lld:pubmed |
pubmed-article:10998597 | pubmed:affiliation | Picower Institute for Molecular Research, 350 Community Drive, Manhasset, NY 11030, USA. msymons@picpower.edu | lld:pubmed |
pubmed-article:10998597 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10998597 | pubmed:publicationType | Review | lld:pubmed |
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