pubmed-article:15178555 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15178555 | lifeskim:mentions | umls-concept:C0028128 | lld:lifeskim |
pubmed-article:15178555 | lifeskim:mentions | umls-concept:C0026844 | lld:lifeskim |
pubmed-article:15178555 | lifeskim:mentions | umls-concept:C1135918 | lld:lifeskim |
pubmed-article:15178555 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:15178555 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
pubmed-article:15178555 | lifeskim:mentions | umls-concept:C0255567 | lld:lifeskim |
pubmed-article:15178555 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:15178555 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:15178555 | lifeskim:mentions | umls-concept:C1514485 | lld:lifeskim |
pubmed-article:15178555 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:15178555 | pubmed:dateCreated | 2004-8-6 | lld:pubmed |
pubmed-article:15178555 | pubmed:abstractText | Vasodilator-stimulated phosphoprotein (VASP) was identified as a substrate for cGMP-dependent protein kinase (PKG) and cAMP-dependent protein kinase (PKA). It is preferentially phosphorylated at serine239 by PKG, whereas serine157 is a preferred phosphorylation site for PKA. In addition, serine157 is phosphorylated by PKC in response to serum. We have investigated the effects of VASP and VASP phosphorylation at serine157 and serine239 on smooth muscle cell (SMC) proliferation and nitric oxide (NO)-mediated growth inhibition. | lld:pubmed |
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pubmed-article:15178555 | pubmed:language | eng | lld:pubmed |
pubmed-article:15178555 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15178555 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15178555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:15178555 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15178555 | pubmed:month | Aug | lld:pubmed |
pubmed-article:15178555 | pubmed:issn | 1524-4636 | lld:pubmed |
pubmed-article:15178555 | pubmed:author | pubmed-author:ChitaleyKanch... | lld:pubmed |
pubmed-article:15178555 | pubmed:author | pubmed-author:ClowesAlexand... | lld:pubmed |
pubmed-article:15178555 | pubmed:author | pubmed-author:WalterUlrichU | lld:pubmed |
pubmed-article:15178555 | pubmed:author | pubmed-author:ChenLihuaL | lld:pubmed |
pubmed-article:15178555 | pubmed:author | pubmed-author:DaumGünterG | lld:pubmed |
pubmed-article:15178555 | pubmed:author | pubmed-author:EigenthalerMa... | lld:pubmed |
pubmed-article:15178555 | pubmed:author | pubmed-author:Bowen-PopeDan... | lld:pubmed |
pubmed-article:15178555 | pubmed:author | pubmed-author:CoatsScott... | lld:pubmed |
pubmed-article:15178555 | pubmed:author | pubmed-author:ThumatiNaresh... | lld:pubmed |
pubmed-article:15178555 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:15178555 | pubmed:volume | 24 | lld:pubmed |
pubmed-article:15178555 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15178555 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15178555 | pubmed:pagination | 1403-8 | lld:pubmed |
pubmed-article:15178555 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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