| pubmed-article:9887966 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9887966 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:9887966 | lifeskim:mentions | umls-concept:C0027096 | lld:lifeskim |
| pubmed-article:9887966 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:9887966 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:9887966 | lifeskim:mentions | umls-concept:C0006746 | lld:lifeskim |
| pubmed-article:9887966 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9887966 | lifeskim:mentions | umls-concept:C1511572 | lld:lifeskim |
| pubmed-article:9887966 | lifeskim:mentions | umls-concept:C1261552 | lld:lifeskim |
| pubmed-article:9887966 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9887966 | pubmed:dateCreated | 1999-4-7 | lld:pubmed |
| pubmed-article:9887966 | pubmed:abstractText | The actin binding protein caldesmon inhibits the actin-activation of myosin ATPase activity. The steps in the cycle of ATP hydrolysis that caldesmon could inhibit include: (1) the binding of myosin to actin, (2) the transition between any two actin-myosin states and (3) the distribution between inactive and active states of actin. The analysis of these possibilities is complicated because caldesmon binds to both myosin and actin and because each caldesmon molecule binds to several actin monomers. This paper reviews procedures for analysing these interactions and summarizes current information on the stability and dynamics of the interaction of caldesmon with actin and myosin. Possible effects of caldesmon on transitions within the ATPase cycle of actomyosin are also discussed. | lld:pubmed |
| pubmed-article:9887966 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9887966 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9887966 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9887966 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9887966 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9887966 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9887966 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9887966 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9887966 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9887966 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9887966 | pubmed:issn | 0001-6772 | lld:pubmed |
| pubmed-article:9887966 | pubmed:author | pubmed-author:SenAA | lld:pubmed |
| pubmed-article:9887966 | pubmed:author | pubmed-author:LeinweberBB | lld:pubmed |
| pubmed-article:9887966 | pubmed:author | pubmed-author:NGVV | lld:pubmed |
| pubmed-article:9887966 | pubmed:author | pubmed-author:ChenY DYD | lld:pubmed |
| pubmed-article:9887966 | pubmed:author | pubmed-author:ChalovichJ... | lld:pubmed |
| pubmed-article:9887966 | pubmed:author | pubmed-author:ResetarAA | lld:pubmed |
| pubmed-article:9887966 | pubmed:author | pubmed-author:FredricksenR... | lld:pubmed |
| pubmed-article:9887966 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9887966 | pubmed:volume | 164 | lld:pubmed |
| pubmed-article:9887966 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9887966 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9887966 | pubmed:pagination | 427-35 | lld:pubmed |
| pubmed-article:9887966 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:9887966 | pubmed:meshHeading | pubmed-meshheading:9887966-... | lld:pubmed |
| pubmed-article:9887966 | pubmed:meshHeading | pubmed-meshheading:9887966-... | lld:pubmed |
| pubmed-article:9887966 | pubmed:meshHeading | pubmed-meshheading:9887966-... | lld:pubmed |
| pubmed-article:9887966 | pubmed:meshHeading | pubmed-meshheading:9887966-... | lld:pubmed |
| pubmed-article:9887966 | pubmed:meshHeading | pubmed-meshheading:9887966-... | lld:pubmed |
| pubmed-article:9887966 | pubmed:meshHeading | pubmed-meshheading:9887966-... | lld:pubmed |
| pubmed-article:9887966 | pubmed:meshHeading | pubmed-meshheading:9887966-... | lld:pubmed |
| pubmed-article:9887966 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9887966 | pubmed:articleTitle | Caldesmon: binding to actin and myosin and effects on elementary steps in the ATPase cycle. | lld:pubmed |
| pubmed-article:9887966 | pubmed:affiliation | Department of Biochemistry, East Carolina University School of Medicine, Greenville, NC 27858-4354, USA. | lld:pubmed |
| pubmed-article:9887966 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9887966 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9887966 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:9887966 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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