| pubmed-article:2143486 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2143486 | lifeskim:mentions | umls-concept:C0036226 | lld:lifeskim |
| pubmed-article:2143486 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:2143486 | lifeskim:mentions | umls-concept:C1413043 | lld:lifeskim |
| pubmed-article:2143486 | lifeskim:mentions | umls-concept:C0449911 | lld:lifeskim |
| pubmed-article:2143486 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2143486 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2143486 | pubmed:dateCreated | 1990-9-18 | lld:pubmed |
| pubmed-article:2143486 | pubmed:abstractText | The ATP-dependent Ca2+ transport in sarcoplasmic reticulum involves transitions between several structural states of the Ca2(+)-ATPase, that occur without major changes in the secondary structure. The rates of these transitions are modulated by the lipid environment and by interactions between ATPase molecules. Although the Ca2(+)-ATPase restricts the rotational mobility of a population of lipids, there is no evidence for specific interaction of the Ca2(+)-ATPase with phospholipids. Fluorescence polarization and energy transfer (FET) studies, using site specific fluorescent indicators, combined with crystallographic, immunological and chemical modification data, yielded a structural model of Ca2(+)-ATPase in which the binding sites of Ca2+ and ATP are tentatively identified. The temperature dependence of FET between fluorophores attached to different regions of the ATPase indicates the existence of 'rigid' and 'flexible' regions within the molecule characterized, by different degrees of thermally induced structural fluctuations. | lld:pubmed |
| pubmed-article:2143486 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2143486 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2143486 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2143486 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2143486 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2143486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2143486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2143486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2143486 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2143486 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:2143486 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2143486 | pubmed:author | pubmed-author:MartonosiA... | lld:pubmed |
| pubmed-article:2143486 | pubmed:author | pubmed-author:JonaII | lld:pubmed |
| pubmed-article:2143486 | pubmed:author | pubmed-author:VargaSS | lld:pubmed |
| pubmed-article:2143486 | pubmed:author | pubmed-author:BuchetRR | lld:pubmed |
| pubmed-article:2143486 | pubmed:author | pubmed-author:MolnarEE | lld:pubmed |
| pubmed-article:2143486 | pubmed:author | pubmed-author:SeidlerN WNW | lld:pubmed |
| pubmed-article:2143486 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2143486 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2143486 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:2143486 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2143486 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2143486 | pubmed:pagination | 365-70 | lld:pubmed |
| pubmed-article:2143486 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:meshHeading | pubmed-meshheading:2143486-... | lld:pubmed |
| pubmed-article:2143486 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2143486 | pubmed:articleTitle | Emerging views on the structure and dynamics of the Ca2(+)-ATPase in sarcoplasmic reticulum. | lld:pubmed |
| pubmed-article:2143486 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, State University of New York, Syracuse 13210. | lld:pubmed |
| pubmed-article:2143486 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2143486 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2143486 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2143486 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:2143486 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
