pubmed-article:2123549 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2123549 | lifeskim:mentions | umls-concept:C0042567 | lld:lifeskim |
pubmed-article:2123549 | lifeskim:mentions | umls-concept:C0021948 | lld:lifeskim |
pubmed-article:2123549 | lifeskim:mentions | umls-concept:C0017963 | lld:lifeskim |
pubmed-article:2123549 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
pubmed-article:2123549 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
pubmed-article:2123549 | lifeskim:mentions | umls-concept:C1880371 | lld:lifeskim |
pubmed-article:2123549 | lifeskim:mentions | umls-concept:C1321758 | lld:lifeskim |
pubmed-article:2123549 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:2123549 | pubmed:dateCreated | 1991-1-16 | lld:pubmed |
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pubmed-article:2123549 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2123549 | pubmed:abstractText | Heterotrimeric guanine nucleotide-binding proteins (G proteins) are integral to the signal transduction pathways that mediate the cell's response to many hormones, neuromodulators, and a variety of other ligands. While many signaling processes are guanine nucleotide dependent, the precise coupling between a variety of receptors, G proteins, and effectors remains obscure. We found that the family of genes that encode the alpha subunits of heterotrimeric G proteins is much larger than had previously been supposed. These novel alpha subunits could account for some of the diverse activities attributed to G proteins. We have now obtained cDNA clones encoding two murine alpha subunits, G alpha q and G alpha 11, that are 88% identical. They lack the site that is ordinarily modified by pertussis toxin and their sequences vary from the canonical Gly-Ala-Gly-Glu-Ser (GAGES) amino acid sequence found in most other G protein alpha subunits. Multiple mRNAs as large as 7.5 kilobases hybridize to G alpha q specific probes and are expressed at various levels in many different tissues. G alpha 11 is encoded by a single 4.0-kilobase message which is expressed ubiquitously. Amino acid sequence comparisons suggest that G alpha q and G alpha 11 represent a third class of alpha subunits. A member of this class was found in Drosophila melanogaster. This alpha subunit, DG alpha q, is 76% identical to G alpha q. The presence of the Gq class in both vertebrates and invertebrates points to a role that is central to signal transduction in multicellular organisms. We suggest that these alpha subunits may be involved in pertussis toxin-insensitive pathways coupled to phospholipase C. | lld:pubmed |
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pubmed-article:2123549 | pubmed:language | eng | lld:pubmed |
pubmed-article:2123549 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2123549 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2123549 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2123549 | pubmed:month | Dec | lld:pubmed |
pubmed-article:2123549 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:2123549 | pubmed:author | pubmed-author:SimonM IMI | lld:pubmed |
pubmed-article:2123549 | pubmed:author | pubmed-author:StrathmannMM | lld:pubmed |
pubmed-article:2123549 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2123549 | pubmed:volume | 87 | lld:pubmed |
pubmed-article:2123549 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2123549 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2123549 | pubmed:pagination | 9113-7 | lld:pubmed |
pubmed-article:2123549 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:2123549 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2123549 | pubmed:articleTitle | G protein diversity: a distinct class of alpha subunits is present in vertebrates and invertebrates. | lld:pubmed |
pubmed-article:2123549 | pubmed:affiliation | Division of Biology, California Institute of Technology, Pasadena 91125. | lld:pubmed |
pubmed-article:2123549 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2123549 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:2123549 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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