pubmed-article:1631113 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1631113 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
pubmed-article:1631113 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:1631113 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
pubmed-article:1631113 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:1631113 | lifeskim:mentions | umls-concept:C1823153 | lld:lifeskim |
pubmed-article:1631113 | lifeskim:mentions | umls-concept:C2349976 | lld:lifeskim |
pubmed-article:1631113 | lifeskim:mentions | umls-concept:C1552644 | lld:lifeskim |
pubmed-article:1631113 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:1631113 | pubmed:issue | 13 | lld:pubmed |
pubmed-article:1631113 | pubmed:dateCreated | 1992-8-14 | lld:pubmed |
pubmed-article:1631113 | pubmed:abstractText | Signal-transducing guanine nucleotide-binding proteins (G proteins) are made up of three subunits, alpha, beta, and gamma. Each of these subunits comprises a family of proteins. The rules for association between members of one family with members of another to form a multimer are not known; it is not clear whether associations are specific or nonspecific. Other than transducin (Gt), the G protein in rod photoreceptors, most purified G proteins contain more than one subtype of beta or gamma subunits. The Gt alpha subunit is associated only with beta 1 and gamma 1. It is not known whether this specificity is due to the differential expression of these subunit types in a cell type or due to intrinsically different affinities between different beta and gamma subunit types. We have used a transfected cell assay system to examine the association of the beta 1, beta 2, and beta 3 proteins with the gamma 1 and gamma 2 proteins. Results show that gamma 1 does not associate with beta 2 and that beta 3 does not associate with gamma 1 or gamma 2. Differences in affinities between types of G protein subunits will impose restrictions on the formation of certain heterotrimers and determine which G protein will be active in a cell. A chimeric molecule of beta 1 and beta 2 was used to broadly map the regions on these subunits that determine specificity of association. | lld:pubmed |
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pubmed-article:1631113 | pubmed:language | eng | lld:pubmed |
pubmed-article:1631113 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1631113 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1631113 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1631113 | pubmed:month | Jul | lld:pubmed |
pubmed-article:1631113 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:1631113 | pubmed:author | pubmed-author:ProninA NAN | lld:pubmed |
pubmed-article:1631113 | pubmed:author | pubmed-author:GautamNN | lld:pubmed |
pubmed-article:1631113 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1631113 | pubmed:day | 1 | lld:pubmed |
pubmed-article:1631113 | pubmed:volume | 89 | lld:pubmed |
pubmed-article:1631113 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1631113 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1631113 | pubmed:pagination | 6220-4 | lld:pubmed |
pubmed-article:1631113 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:1631113 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1631113 | pubmed:articleTitle | Interaction between G-protein beta and gamma subunit types is selective. | lld:pubmed |
pubmed-article:1631113 | pubmed:affiliation | Department of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110. | lld:pubmed |
pubmed-article:1631113 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1631113 | pubmed:publicationType | In Vitro | lld:pubmed |
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