| pubmed-article:7787096 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7787096 | lifeskim:mentions | umls-concept:C0025979 | lld:lifeskim |
| pubmed-article:7787096 | lifeskim:mentions | umls-concept:C1510470 | lld:lifeskim |
| pubmed-article:7787096 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:7787096 | lifeskim:mentions | umls-concept:C1510438 | lld:lifeskim |
| pubmed-article:7787096 | lifeskim:mentions | umls-concept:C0348080 | lld:lifeskim |
| pubmed-article:7787096 | pubmed:issue | 4 Suppl | lld:pubmed |
| pubmed-article:7787096 | pubmed:dateCreated | 1995-7-27 | lld:pubmed |
| pubmed-article:7787096 | pubmed:abstractText | With sliding actin-filament motility assays, filament velocity should be independent of changes in the level of actomyosin activation under unloaded conditions. Using a simple modification of the motility assay to measure relative changes in isometric force (activation), we determined that isometric force increased 200-fold with thiophosphorylation of the myosin regulatory light chain, and that with thiophosphorylated myosin, isometric force was further increased by the addition of saturating smooth-muscle tropomyosin (100%) or tropomyosin plus calponin (500%), and decreased with the addition of saturating caldesmon (-100%). Under "reducing conditions," filament velocity (2.0 microns/s) was constant for mixtures of dephosphorylated and thiophosphorylated myosin containing > 5% thiophosphorylated myosin, and was unaffected by the addition of saturating concentrations of tropomyosin or caldesmon. In contrast, "standard assay conditions" were found to be nonreducing. With fully thiophosphorylated smooth-muscle myosin, saturating smooth-muscle tropomyosin increased velocity to 150% of control, and caldesmon halted all filament motion; with fully dephosphorylated myosin (< 0.002 mol/mol) filaments only moved when tropomyosin or tropomyosin plus calponin was added. Taken together, these observations suggest that under "standard conditions" a mechanical load is present that is eliminated by "reducing conditions." Filament velocity was insensitive to changes in cross-bridge density, under all conditions, suggesting that noncycling cross-bridges, generated by photochemical oxidation of myosin, is a likely source of mechanical loading. | lld:pubmed |
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| pubmed-article:7787096 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7787096 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7787096 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7787096 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7787096 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7787096 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7787096 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:7787096 | pubmed:author | pubmed-author:HaeberleJ RJR | lld:pubmed |
| pubmed-article:7787096 | pubmed:author | pubmed-author:HemricM EME | lld:pubmed |
| pubmed-article:7787096 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7787096 | pubmed:volume | 68 | lld:pubmed |
| pubmed-article:7787096 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7787096 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7787096 | pubmed:pagination | 306S-310S; discussion 310S-311S | lld:pubmed |
| pubmed-article:7787096 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:7787096 | pubmed:meshHeading | pubmed-meshheading:7787096-... | lld:pubmed |
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| pubmed-article:7787096 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7787096 | pubmed:articleTitle | Are actin filaments moving under unloaded conditions in the in vitro motility assay? | lld:pubmed |
| pubmed-article:7787096 | pubmed:affiliation | Department of Molecular Physiology and Biophysics, University of Vermont, Burlington 05405, USA. | lld:pubmed |
| pubmed-article:7787096 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7787096 | pubmed:publicationType | In Vitro | lld:pubmed |
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