pubmed-article:2833884 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2833884 | lifeskim:mentions | umls-concept:C1882598 | lld:lifeskim |
pubmed-article:2833884 | lifeskim:mentions | umls-concept:C0248868 | lld:lifeskim |
pubmed-article:2833884 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:2833884 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:2833884 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
pubmed-article:2833884 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:2833884 | lifeskim:mentions | umls-concept:C1283195 | lld:lifeskim |
pubmed-article:2833884 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:2833884 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2833884 | pubmed:dateCreated | 1988-5-24 | lld:pubmed |
pubmed-article:2833884 | pubmed:abstractText | Recent molecular cloning experiments have identified a 25 amino-acid region as the calmodulin-binding domain of the alpha-subunit of rat brain Ca2+/calmodulin-dependent multifunctional protein kinase II (CaM-K II). Synthetic peptides, derived from the deduced amino-acid sequence encompassing this region, were examined for their ability to bind calmodulin in a calcium dependent manner and to inhibit the Ca2+/calmodulin-dependent autophosphorylation of CaM-K II. Comparison of these structure-function relationships highlighted a region of 5 amino-acids, which was essential for calmodulin interaction and inhibition of kinase activity. This region demonstrated some homology with other calmodulin-binding peptides, and may represent a key site of interaction of the kinase with calmodulin. These analyses provide additional insight into the molecular mechanism underlying the Ca2+ regulation of CaM-K II. | lld:pubmed |
pubmed-article:2833884 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2833884 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2833884 | pubmed:language | eng | lld:pubmed |
pubmed-article:2833884 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2833884 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2833884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2833884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2833884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2833884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2833884 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2833884 | pubmed:month | Apr | lld:pubmed |
pubmed-article:2833884 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:2833884 | pubmed:author | pubmed-author:KempB EBE | lld:pubmed |
pubmed-article:2833884 | pubmed:author | pubmed-author:MeansA RAR | lld:pubmed |
pubmed-article:2833884 | pubmed:author | pubmed-author:ShenolikarSS | lld:pubmed |
pubmed-article:2833884 | pubmed:author | pubmed-author:HanleyR MRM | lld:pubmed |
pubmed-article:2833884 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2833884 | pubmed:day | 15 | lld:pubmed |
pubmed-article:2833884 | pubmed:volume | 152 | lld:pubmed |
pubmed-article:2833884 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2833884 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2833884 | pubmed:pagination | 122-8 | lld:pubmed |
pubmed-article:2833884 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:2833884 | pubmed:meshHeading | pubmed-meshheading:2833884-... | lld:pubmed |
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pubmed-article:2833884 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:2833884 | pubmed:articleTitle | Mapping of calmodulin-binding domain of Ca2+/calmodulin-dependent protein kinase II from rat brain. | lld:pubmed |
pubmed-article:2833884 | pubmed:affiliation | University of Texas Medical School, Houston. | lld:pubmed |
pubmed-article:2833884 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2833884 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2833884 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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