| pubmed-article:9632688 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9632688 | lifeskim:mentions | umls-concept:C0002395 | lld:lifeskim |
| pubmed-article:9632688 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:9632688 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:9632688 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:9632688 | lifeskim:mentions | umls-concept:C0299212 | lld:lifeskim |
| pubmed-article:9632688 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:9632688 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:9632688 | pubmed:dateCreated | 1998-8-3 | lld:pubmed |
| pubmed-article:9632688 | pubmed:abstractText | To investigate a possible association between G-proteins and presenilin-1 (PS-1), a series of glutathione S-transferase-fusion proteins containing portions of PS-1 were prepared and used in vitro in binding experiments with tissue and recombinant G-proteins. The results demonstrate that the 39 C-terminal amino acids of PS-1 selectively bind the brain G-protein, Go. Addition of guanosine 5'-3-O-(thio)triphosphate promoted Go dissociation from PS-1, indicating that this domain mimics the function of G-protein-coupling domains found in receptors. The 39-amino acid synthetic polypeptide activated Go in a magnesium ion-dependent manner. Physical interaction of full-length PS-1 and Go was also demonstrated. Following transfection of Goalpha and N-terminally FLAG-tagged PS-1 in COS-7 cells, Go was immunoprecipitated by FLAG antibodies. In addition, endogenous PS-1 and Goalpha were colocalized immunocytochemically in human glioma cell lines. The results indicate that PS-1 regulates Go activities in living cells. | lld:pubmed |
| pubmed-article:9632688 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632688 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9632688 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632688 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9632688 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9632688 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9632688 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632688 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9632688 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9632688 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:YasuharaSS | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:OkamotoTT | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:GambettiPP | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:NishiyamaKK | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:KatadaTT | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:HomburgerVV | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:YadavS PSP | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:GAYJ PJP | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:JogN VNV | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:ShiY CYC | lld:pubmed |
| pubmed-article:9632688 | pubmed:author | pubmed-author:SmineAA | lld:pubmed |
| pubmed-article:9632688 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9632688 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:9632688 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9632688 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9632688 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9632688 | pubmed:pagination | 16281-8 | lld:pubmed |
| pubmed-article:9632688 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9632688 | pubmed:meshHeading | pubmed-meshheading:9632688-... | lld:pubmed |
| pubmed-article:9632688 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9632688 | pubmed:articleTitle | Regulation of brain G-protein go by Alzheimer's disease gene presenilin-1. | lld:pubmed |
| pubmed-article:9632688 | pubmed:affiliation | The Lerner Research Institute, Department of Neurosciences, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA. | lld:pubmed |
| pubmed-article:9632688 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9632688 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9632688 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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