| pubmed-article:7663132 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7663132 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:7663132 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:7663132 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:7663132 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7663132 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:7663132 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:7663132 | pubmed:dateCreated | 1995-10-6 | lld:pubmed |
| pubmed-article:7663132 | pubmed:abstractText | Calmodulin (CaM) acts as an intracellular calcium sensor that translates the Ca2+ signal into a variety of cellular processes. Ca(2+)-CaM recognition of a short polypeptide segment in target proteins induces conformational changes in both CaM and the target, enabling the target protein to become functionally active. The solution and crystal structures of Ca(2+)-CaM bound to peptides derived from three CaM-dependent enzymes reveal structural features that are common in target recognition by Ca(2+)-CaM. Phosphorylation of the target proteins at sites in or near the CaM-binding region modulates binding of CaM, thereby providing an additional mechanism of functional regulation. The structural aspects of target recognition by Ca(2+)-CaM are discussed using mainly the three-dimensional structural information obtained with nuclear magnetic resonance spectroscopy and X-ray diffraction methods. | lld:pubmed |
| pubmed-article:7663132 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7663132 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7663132 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7663132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7663132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7663132 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7663132 | pubmed:issn | 1056-8700 | lld:pubmed |
| pubmed-article:7663132 | pubmed:author | pubmed-author:IkuraMM | lld:pubmed |
| pubmed-article:7663132 | pubmed:author | pubmed-author:CriviciAA | lld:pubmed |
| pubmed-article:7663132 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7663132 | pubmed:volume | 24 | lld:pubmed |
| pubmed-article:7663132 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7663132 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7663132 | pubmed:pagination | 85-116 | lld:pubmed |
| pubmed-article:7663132 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:7663132 | pubmed:meshHeading | pubmed-meshheading:7663132-... | lld:pubmed |
| pubmed-article:7663132 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7663132 | pubmed:articleTitle | Molecular and structural basis of target recognition by calmodulin. | lld:pubmed |
| pubmed-article:7663132 | pubmed:affiliation | Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada. | lld:pubmed |
| pubmed-article:7663132 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7663132 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:7663132 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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