pubmed-article:10219243 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10219243 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
pubmed-article:10219243 | lifeskim:mentions | umls-concept:C1565319 | lld:lifeskim |
pubmed-article:10219243 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:10219243 | lifeskim:mentions | umls-concept:C1421482 | lld:lifeskim |
pubmed-article:10219243 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:10219243 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:10219243 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:10219243 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
pubmed-article:10219243 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
pubmed-article:10219243 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
pubmed-article:10219243 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:10219243 | pubmed:dateCreated | 1999-5-17 | lld:pubmed |
pubmed-article:10219243 | pubmed:abstractText | Although small GTP-binding proteins of the Rho family have been implicated in signaling to the actin cytoskeleton, the exact nature of the linkage has remained obscure. We describe a novel mechanism that links one Rho family member, Cdc42, to actin polymerization. N-WASP, a ubiquitously expressed Cdc42-interacting protein, is required for Cdc42-stimulated actin polymerization in Xenopus egg extracts. The C terminus of N-WASP binds to the Arp2/3 complex and dramatically stimulates its ability to nucleate actin polymerization. Although full-length N-WASP is less effective, its activity can be greatly enhanced by Cdc42 and phosphatidylinositol (4,5) bisphosphate. Therefore, N-WASP and the Arp2/3 complex comprise a core mechanism that directly connects signal transduction pathways to the stimulation of actin polymerization. | lld:pubmed |
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pubmed-article:10219243 | pubmed:language | eng | lld:pubmed |
pubmed-article:10219243 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10219243 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10219243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10219243 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10219243 | pubmed:month | Apr | lld:pubmed |
pubmed-article:10219243 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:10219243 | pubmed:author | pubmed-author:TakenawaTT | lld:pubmed |
pubmed-article:10219243 | pubmed:author | pubmed-author:MikiHH | lld:pubmed |
pubmed-article:10219243 | pubmed:author | pubmed-author:LopezMM | lld:pubmed |
pubmed-article:10219243 | pubmed:author | pubmed-author:NICC | lld:pubmed |
pubmed-article:10219243 | pubmed:author | pubmed-author:KirschnerM... | lld:pubmed |
pubmed-article:10219243 | pubmed:author | pubmed-author:KirchhausenTT | lld:pubmed |
pubmed-article:10219243 | pubmed:author | pubmed-author:RohatgiRR | lld:pubmed |
pubmed-article:10219243 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10219243 | pubmed:day | 16 | lld:pubmed |
pubmed-article:10219243 | pubmed:volume | 97 | lld:pubmed |
pubmed-article:10219243 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10219243 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10219243 | pubmed:pagination | 221-31 | lld:pubmed |
pubmed-article:10219243 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:10219243 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10219243 | pubmed:articleTitle | The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. | lld:pubmed |
pubmed-article:10219243 | pubmed:affiliation | Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA. | lld:pubmed |
pubmed-article:10219243 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10219243 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:10219243 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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