| pubmed-article:1351298 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1351298 | lifeskim:mentions | umls-concept:C0001478 | lld:lifeskim |
| pubmed-article:1351298 | pubmed:issue | 1276 | lld:pubmed |
| pubmed-article:1351298 | pubmed:dateCreated | 1992-7-10 | lld:pubmed |
| pubmed-article:1351298 | pubmed:abstractText | Studies of the interaction between actin and myosin subfragment 1 (S1) in solution have shown that the association reaction takes place in at least two steps. Initially the association is relatively weak to form a complex called the A state which can then isomerize to the R state. The rate and equilibrium constants for the isomerization have been measured and are shown to depend upon the nucleotide bound to the S1 ATPase site; with ATP bound the A state is preferred but as ATP is hydrolysed and the products are sequentially released then the complex gradually shifts to the A state. An extensive series of experiments have characterized the A-to-R isomerization both in solution and in contracting muscle fibres and have shown it to be closely associated with the key events in the ATP-driven contraction cycle: the conformational change from the A to the R state can be monitored by fluorescent probes on either actin or the nucleotide; the isomerization can be perturbed by increases in hydrostatic pressure; the actin-induced acceleration of the rate of product release from myosin is coupled to the A-to-R isomerization; tropomyosin may control actin and myosin interaction by controlling the isomerization step and finally pressure perturbations of contracting muscle fibres shows there to be a close coupling between the isomerization of acto.S1 and the force generating event of muscle contraction. | lld:pubmed |
| pubmed-article:1351298 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1351298 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1351298 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1351298 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1351298 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1351298 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1351298 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1351298 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:1351298 | pubmed:issn | 0962-8436 | lld:pubmed |
| pubmed-article:1351298 | pubmed:author | pubmed-author:GeevesM AMA | lld:pubmed |
| pubmed-article:1351298 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1351298 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:1351298 | pubmed:volume | 336 | lld:pubmed |
| pubmed-article:1351298 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1351298 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1351298 | pubmed:pagination | 63-70; discussion 70-1 | lld:pubmed |
| pubmed-article:1351298 | pubmed:dateRevised | 2010-8-25 | lld:pubmed |
| pubmed-article:1351298 | pubmed:meshHeading | pubmed-meshheading:1351298-... | lld:pubmed |
| pubmed-article:1351298 | pubmed:meshHeading | pubmed-meshheading:1351298-... | lld:pubmed |
| pubmed-article:1351298 | pubmed:meshHeading | pubmed-meshheading:1351298-... | lld:pubmed |
| pubmed-article:1351298 | pubmed:meshHeading | pubmed-meshheading:1351298-... | lld:pubmed |
| pubmed-article:1351298 | pubmed:meshHeading | pubmed-meshheading:1351298-... | lld:pubmed |
| pubmed-article:1351298 | pubmed:meshHeading | pubmed-meshheading:1351298-... | lld:pubmed |
| pubmed-article:1351298 | pubmed:meshHeading | pubmed-meshheading:1351298-... | lld:pubmed |
| pubmed-article:1351298 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1351298 | pubmed:articleTitle | The actomyosin ATPase: a two-state system. | lld:pubmed |
| pubmed-article:1351298 | pubmed:affiliation | Department of Biochemistry, School of Medical Sciences, University of Bristol, U.K. | lld:pubmed |
| pubmed-article:1351298 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1351298 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:1351298 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:1351298 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1351298 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1351298 | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1351298 | lld:pubmed |
