| pubmed-article:9305633 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9305633 | lifeskim:mentions | umls-concept:C0084024 | lld:lifeskim |
| pubmed-article:9305633 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:9305633 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:9305633 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:9305633 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:9305633 | pubmed:dateCreated | 1997-10-17 | lld:pubmed |
| pubmed-article:9305633 | pubmed:abstractText | G-protein betagamma-subunits (G(betagamma)) are active transmembrane signalling components. Their function recently has been observed to be regulated by the cytosolic protein phosducin. We show here that a small fragment (amino acids 215-232) contained in the C-terminus of phosducin is sufficient for high-affinity interactions with G(betagamma). Corresponding peptides not only disrupt G(betagamma)-G(alpha) interactions, as defined by G(betagamma)-stimulated GTPase activity of alpha(o), but also other G(betagamma)-mediated functions. The NMR structure of a peptide encompassing this region shows a loop exposing the side chains of Glu223 and Tyr224, and peptides with a substitution of either of these amino acids show a complete loss of activity towards G(o). Mutation of this Tyr224 to Ala in full-length phosducin reduced the functional activity of phosducin to that of phosducin's isolated N-terminus, indicating the importance of this residue within the short, structurally defined C-terminal segment. This small peptide derived from phosducin, may represent a model of a G(betagamma) inhibitor, and illustrates the potential of small compounds to affect G(betagamma) functions. | lld:pubmed |
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| pubmed-article:9305633 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9305633 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9305633 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9305633 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9305633 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9305633 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9305633 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:9305633 | pubmed:author | pubmed-author:SchröderSS | lld:pubmed |
| pubmed-article:9305633 | pubmed:author | pubmed-author:LohseM JMJ | lld:pubmed |
| pubmed-article:9305633 | pubmed:author | pubmed-author:MaciasMM | lld:pubmed |
| pubmed-article:9305633 | pubmed:author | pubmed-author:OschkinatHH | lld:pubmed |
| pubmed-article:9305633 | pubmed:author | pubmed-author:BeyermannMM | lld:pubmed |
| pubmed-article:9305633 | pubmed:author | pubmed-author:SchneppWW | lld:pubmed |
| pubmed-article:9305633 | pubmed:author | pubmed-author:BlümlKK | lld:pubmed |
| pubmed-article:9305633 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9305633 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9305633 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:9305633 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9305633 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9305633 | pubmed:pagination | 4908-15 | lld:pubmed |
| pubmed-article:9305633 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9305633 | pubmed:meshHeading | pubmed-meshheading:9305633-... | lld:pubmed |
| pubmed-article:9305633 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9305633 | pubmed:articleTitle | A small region in phosducin inhibits G-protein betagamma-subunit function. | lld:pubmed |
| pubmed-article:9305633 | pubmed:affiliation | Institut für Pharmakologie und Toxikologie der Universität Würzburg, Germany. | lld:pubmed |
| pubmed-article:9305633 | pubmed:publicationType | Journal Article | lld:pubmed |
