pubmed-article:8226731 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8226731 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:8226731 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:8226731 | lifeskim:mentions | umls-concept:C1419206 | lld:lifeskim |
pubmed-article:8226731 | lifeskim:mentions | umls-concept:C0214541 | lld:lifeskim |
pubmed-article:8226731 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
pubmed-article:8226731 | pubmed:issue | 30 | lld:pubmed |
pubmed-article:8226731 | pubmed:dateCreated | 1993-12-1 | lld:pubmed |
pubmed-article:8226731 | pubmed:abstractText | Rabphilin-3A is a putative target protein for Rab3A, a member of the small G protein superfamily that is implicated in regulated secretion, particularly in neurotransmitter release. Rabphilin-3A contains at least two functionally different domains: the N-terminal Rab3A-binding domain and the C-terminal C2 domain, which interacts with both Ca2+ and phospholipid. Because Rabphilin-3A interacts preferentially with GTP-Rab3A rather than with GDP-Rab3A, we have examined here whether Rabphilin-3A affects the GTPase activity of Rab3A. Rabphilin-3A and its N-terminal fragment, but not its C-terminal fragment, very weakly stimulated the basal GTPase activity of Rab3A. However, Rabphilin-3A and its N-terminal fragment strongly inhibited the Rab3A GAP-stimulated GTPase activity of Rab3A. Ca2+ and phospholipid showed no effect on these activities of Rabphilin-3A. The physiological significance of the GAP activity of Rabphilin-3A is obscure, but it is likely that Rabphilin-3A inhibits Rab3A GAP activity and keeps Rab3A in the GTP-bound active form during its action as a target molecule for Rab3A. | lld:pubmed |
pubmed-article:8226731 | pubmed:language | eng | lld:pubmed |
pubmed-article:8226731 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8226731 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8226731 | pubmed:month | Oct | lld:pubmed |
pubmed-article:8226731 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:8226731 | pubmed:author | pubmed-author:KatoMM | lld:pubmed |
pubmed-article:8226731 | pubmed:author | pubmed-author:SasakiTT | lld:pubmed |
pubmed-article:8226731 | pubmed:author | pubmed-author:TakaiYY | lld:pubmed |
pubmed-article:8226731 | pubmed:author | pubmed-author:KishidaSS | lld:pubmed |
pubmed-article:8226731 | pubmed:author | pubmed-author:KaibuchiKK | lld:pubmed |
pubmed-article:8226731 | pubmed:author | pubmed-author:ShiratakiHH | lld:pubmed |
pubmed-article:8226731 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8226731 | pubmed:day | 25 | lld:pubmed |
pubmed-article:8226731 | pubmed:volume | 268 | lld:pubmed |
pubmed-article:8226731 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8226731 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8226731 | pubmed:pagination | 22259-61 | lld:pubmed |
pubmed-article:8226731 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:8226731 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8226731 | pubmed:articleTitle | Rab3A GTPase-activating protein-inhibiting activity of Rabphilin-3A, a putative Rab3A target protein. | lld:pubmed |
pubmed-article:8226731 | pubmed:affiliation | Department of Biochemistry, Kobe University School of Medicine, Japan. | lld:pubmed |
pubmed-article:8226731 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8226731 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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