| pubmed-article:10836506 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10836506 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:10836506 | lifeskim:mentions | umls-concept:C0027096 | lld:lifeskim |
| pubmed-article:10836506 | lifeskim:mentions | umls-concept:C0007996 | lld:lifeskim |
| pubmed-article:10836506 | pubmed:issue | 1396 | lld:pubmed |
| pubmed-article:10836506 | pubmed:dateCreated | 2000-9-20 | lld:pubmed |
| pubmed-article:10836506 | pubmed:abstractText | There is mounting evidence that the myosin head domain contains a lever arm which amplifies small structural changes that occur at the nucleotide-binding site. The mechanical work associated with movement of the lever affects the rates at which the products of ATP hydrolysis are released. During muscle contraction, this strain-dependent chemistry leads to cooperativity of the myosin molecules within a thick filament. Two aspects of cooperative action are discussed, in the context of a simple stochastic model. (i) A modest motion of the lever arm on ADP release can serve to regulate the fraction of myosin bound to the thin filament, in order to recruit more heads at higher loads. (ii) If the lever swings through a large angle when phosphate is released, the chemical cycles of the myosin molecules can be synchronized at high loads. This leads to stepwise sliding of the filaments and suggests that the isometric condition is not a steady state. | lld:pubmed |
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| pubmed-article:10836506 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10836506 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10836506 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10836506 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10836506 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10836506 | pubmed:issn | 0962-8436 | lld:pubmed |
| pubmed-article:10836506 | pubmed:author | pubmed-author:DukeTT | lld:pubmed |
| pubmed-article:10836506 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10836506 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:10836506 | pubmed:volume | 355 | lld:pubmed |
| pubmed-article:10836506 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10836506 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10836506 | pubmed:pagination | 529-38 | lld:pubmed |
| pubmed-article:10836506 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
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| pubmed-article:10836506 | pubmed:meshHeading | pubmed-meshheading:10836506... | lld:pubmed |
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| pubmed-article:10836506 | pubmed:meshHeading | pubmed-meshheading:10836506... | lld:pubmed |
| pubmed-article:10836506 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10836506 | pubmed:articleTitle | Cooperativity of myosin molecules through strain-dependent chemistry. | lld:pubmed |
| pubmed-article:10836506 | pubmed:affiliation | Institut Curie, Section de Recherche, Paris, France. | lld:pubmed |
| pubmed-article:10836506 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10836506 | pubmed:publicationType | Review | lld:pubmed |
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