pubmed-article:10354567 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10354567 | lifeskim:mentions | umls-concept:C0872014 | lld:lifeskim |
pubmed-article:10354567 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:10354567 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:10354567 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:10354567 | pubmed:dateCreated | 1999-7-14 | lld:pubmed |
pubmed-article:10354567 | pubmed:abstractText | Compartmentalization of signalling molecules through association with anchoring proteins ensures specificity in signal transduction by placing enzymes close to their appropriate effectors and substrates. For example, 'A-kinase anchoring proteins' (AKAPs) bind to the regulatory subunit of cAMP-dependent protein kinase (PKA) to direct the kinase to discrete intracellular locations. Recently, functional studies aimed at disrupting AKAP-PKA complexes have demonstrated a role for anchored PKA in various cellular processes, including gene transcription, hormone-mediated insulin secretion and ion-channel modulation. By binding to additional signalling molecules, AKAPs might function to coordinate multiple components of signal-transduction pathways. | lld:pubmed |
pubmed-article:10354567 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10354567 | pubmed:language | eng | lld:pubmed |
pubmed-article:10354567 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10354567 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10354567 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10354567 | pubmed:month | Jun | lld:pubmed |
pubmed-article:10354567 | pubmed:issn | 0962-8924 | lld:pubmed |
pubmed-article:10354567 | pubmed:author | pubmed-author:ScottJ DJD | lld:pubmed |
pubmed-article:10354567 | pubmed:author | pubmed-author:ColledgeMM | lld:pubmed |
pubmed-article:10354567 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10354567 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:10354567 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10354567 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10354567 | pubmed:pagination | 216-21 | lld:pubmed |
pubmed-article:10354567 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
pubmed-article:10354567 | pubmed:meshHeading | pubmed-meshheading:10354567... | lld:pubmed |
pubmed-article:10354567 | pubmed:meshHeading | pubmed-meshheading:10354567... | lld:pubmed |
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pubmed-article:10354567 | pubmed:meshHeading | pubmed-meshheading:10354567... | lld:pubmed |
pubmed-article:10354567 | pubmed:meshHeading | pubmed-meshheading:10354567... | lld:pubmed |
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pubmed-article:10354567 | pubmed:meshHeading | pubmed-meshheading:10354567... | lld:pubmed |
pubmed-article:10354567 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10354567 | pubmed:articleTitle | AKAPs: from structure to function. | lld:pubmed |
pubmed-article:10354567 | pubmed:affiliation | Howard Hughes Medical Institute, L-474, Vollum Institute, Oregon Health Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97201, USA. | lld:pubmed |
pubmed-article:10354567 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10354567 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10354567 | pubmed:publicationType | Review | lld:pubmed |
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