| pubmed-article:15192109 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15192109 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:15192109 | lifeskim:mentions | umls-concept:C0908604 | lld:lifeskim |
| pubmed-article:15192109 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15192109 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:15192109 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:15192109 | lifeskim:mentions | umls-concept:C1705810 | lld:lifeskim |
| pubmed-article:15192109 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:15192109 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:15192109 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:15192109 | pubmed:dateCreated | 2004-8-9 | lld:pubmed |
| pubmed-article:15192109 | pubmed:abstractText | We show herein that removal of the first 86 amino acids (aa) of the N terminus (designated N) of type VI adenylyl cyclase (ACVI) caused the resultant ACVI mutant (ACVI-DeltaA87) to be more greatly inhibited by a Galpha(i)-coupled receptor or activated Galpha(i) protein. Moreover, in vitro binding of the full-length N and C1a domain (designated C1a), which interacts with Galpha(i), was detected. A truncated N terminus (aa 1-86) also interacted with C1a, suggesting that the C1a-interacting region is located within aa 1-86. Mutation analyses further revealed that N might interact with C1a in the region (aa 434-505) where Galpha(i) is bound. Mutations of two residues (Leu-472 and Val-476) located in this N-binding region of C1a suppressed the interaction between recombinant N and C1a and markedly reduced Galpha(i)-mediated inhibition of ACVI-DeltaA87. Further biochemical analyses of the effect of internal mutations of Leu-472/Val-476 on Galpha(i)-mediated inhibition of wild-type ACVI and ACVI-DeltaA87 suggested that N modulates the Galpha(i)-mediated inhibition of ACVI via binding to C1a when the level of Galpha(i) is low (i.e. around the IC(50) value) and that a more complicated interfering mode results when the level of Galpha(i) is high (i.e. approximately 10- to 20-fold of the IC(50) value). Collectively, data presented herein suggest a novel function of the N terminus of ACVI in Galpha(i)-mediated regulation. | lld:pubmed |
| pubmed-article:15192109 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15192109 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15192109 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15192109 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15192109 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15192109 | pubmed:author | pubmed-author:LaiHsing-LinH... | lld:pubmed |
| pubmed-article:15192109 | pubmed:author | pubmed-author:KaoYu-YaYY | lld:pubmed |
| pubmed-article:15192109 | pubmed:author | pubmed-author:HwangMing-Jin... | lld:pubmed |
| pubmed-article:15192109 | pubmed:author | pubmed-author:ChernYijuangY | lld:pubmed |
| pubmed-article:15192109 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15192109 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:15192109 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:15192109 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15192109 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15192109 | pubmed:pagination | 34440-8 | lld:pubmed |
| pubmed-article:15192109 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15192109 | pubmed:meshHeading | pubmed-meshheading:15192109... | lld:pubmed |
| pubmed-article:15192109 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15192109 | pubmed:articleTitle | An important functional role of the N terminus domain of type VI adenylyl cyclase in Galphai-mediated inhibition. | lld:pubmed |
| pubmed-article:15192109 | pubmed:affiliation | Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan, ROC. | lld:pubmed |
| pubmed-article:15192109 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15192109 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:25289 | entrezgene:pubmed | pubmed-article:15192109 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:15192109 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15192109 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15192109 | lld:pubmed |
