| pubmed-article:2753157 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2753157 | lifeskim:mentions | umls-concept:C0027061 | lld:lifeskim |
| pubmed-article:2753157 | lifeskim:mentions | umls-concept:C0521324 | lld:lifeskim |
| pubmed-article:2753157 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:2753157 | lifeskim:mentions | umls-concept:C1707719 | lld:lifeskim |
| pubmed-article:2753157 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:2753157 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:2753157 | pubmed:dateCreated | 1989-8-29 | lld:pubmed |
| pubmed-article:2753157 | pubmed:abstractText | To determine the significance of the global structure of the regulatory proteins in the mechanism of the Ca2+-switch in cardiac and skeletal muscle contractions, the properties of a family of Ca2+-binding proteins with 4 or 3 EF-hand motifs have been studied with desensitized skinned fiber preparations. Proteins with 4 EF hands (such as troponins C - TnCs) are dumb-bell shaped, those with 3 EF hands (parvalbumin) being ellipsoidal. The number of active sites varied between four and two. We find that the ability to anchor in the fiber is limited to proteins with 4 EF hands and, at least, two active Ca2+-binding sites, one each in the N- and C-termini. The results suggest that the dumb-bell shaped global structure is critical for the switching action in muscular contraction, and a trigger site in the N-terminus and a structural site in the C-terminus need to be active in order to regulate contractility. | lld:pubmed |
| pubmed-article:2753157 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2753157 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2753157 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2753157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2753157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2753157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2753157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2753157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2753157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2753157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2753157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2753157 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2753157 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2753157 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:2753157 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2753157 | pubmed:author | pubmed-author:LehmanWW | lld:pubmed |
| pubmed-article:2753157 | pubmed:author | pubmed-author:GulatiJJ | lld:pubmed |
| pubmed-article:2753157 | pubmed:author | pubmed-author:BabuAA | lld:pubmed |
| pubmed-article:2753157 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2753157 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:2753157 | pubmed:volume | 251 | lld:pubmed |
| pubmed-article:2753157 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2753157 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2753157 | pubmed:pagination | 177-82 | lld:pubmed |
| pubmed-article:2753157 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:meshHeading | pubmed-meshheading:2753157-... | lld:pubmed |
| pubmed-article:2753157 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2753157 | pubmed:articleTitle | Characterization of the Ca2+-switch in skeletal and cardiac muscles. | lld:pubmed |
| pubmed-article:2753157 | pubmed:affiliation | Albert Einstein College of Medicine, Bronx, NY 10461. | lld:pubmed |
| pubmed-article:2753157 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2753157 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2753157 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2753157 | lld:pubmed |
