pubmed-article:16473600 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16473600 | lifeskim:mentions | umls-concept:C0282114 | lld:lifeskim |
pubmed-article:16473600 | lifeskim:mentions | umls-concept:C0243044 | lld:lifeskim |
pubmed-article:16473600 | lifeskim:mentions | umls-concept:C1825534 | lld:lifeskim |
pubmed-article:16473600 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
pubmed-article:16473600 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
pubmed-article:16473600 | pubmed:dateCreated | 2006-2-13 | lld:pubmed |
pubmed-article:16473600 | pubmed:abstractText | Guanine nucleotide dissociation inhibitor (GDI) is a central regulator of Rab GTPase family members. GDI recycles Rab proteins from the membrane and sequesters the inactive GDP-bound form of Rab in the cytosol for use in multiple rounds of transport. The balance between the membrane-bound form of Rab and the cytosolic reserve pool of the Rab-GDI complex is critical for vesicular trafficking between membrane compartments. Recycling of Rab GTPases is likely to require a membrane-bound complex of GDI, Hsp90, and Rab given that alphaGDI-dependent recycling of Rab3A at the synapse and neurotransmitter transmitter release is inhibited by Hsp90-specific inhibitors. Here we describe methods required for establishing the dependence of Rab recycling pathways on Hsp90 in vitro. | lld:pubmed |
pubmed-article:16473600 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16473600 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16473600 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16473600 | pubmed:language | eng | lld:pubmed |
pubmed-article:16473600 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16473600 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16473600 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16473600 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16473600 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16473600 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16473600 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16473600 | pubmed:issn | 0076-6879 | lld:pubmed |
pubmed-article:16473600 | pubmed:author | pubmed-author:BalchWilliam... | lld:pubmed |
pubmed-article:16473600 | pubmed:author | pubmed-author:ChenChristine... | lld:pubmed |
pubmed-article:16473600 | pubmed:author | pubmed-author:SakisakaToshi... | lld:pubmed |
pubmed-article:16473600 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16473600 | pubmed:volume | 403 | lld:pubmed |
pubmed-article:16473600 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16473600 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16473600 | pubmed:pagination | 339-47 | lld:pubmed |
pubmed-article:16473600 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:16473600 | pubmed:meshHeading | pubmed-meshheading:16473600... | lld:pubmed |
pubmed-article:16473600 | pubmed:meshHeading | pubmed-meshheading:16473600... | lld:pubmed |
pubmed-article:16473600 | pubmed:meshHeading | pubmed-meshheading:16473600... | lld:pubmed |
pubmed-article:16473600 | pubmed:meshHeading | pubmed-meshheading:16473600... | lld:pubmed |
pubmed-article:16473600 | pubmed:meshHeading | pubmed-meshheading:16473600... | lld:pubmed |
pubmed-article:16473600 | pubmed:meshHeading | pubmed-meshheading:16473600... | lld:pubmed |
pubmed-article:16473600 | pubmed:meshHeading | pubmed-meshheading:16473600... | lld:pubmed |
pubmed-article:16473600 | pubmed:meshHeading | pubmed-meshheading:16473600... | lld:pubmed |
pubmed-article:16473600 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:16473600 | pubmed:articleTitle | Use of Hsp90 inhibitors to disrupt GDI-dependent Rab recycling. | lld:pubmed |
pubmed-article:16473600 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16473600 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |