| pubmed-article:15665867 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15665867 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:15665867 | lifeskim:mentions | umls-concept:C0969679 | lld:lifeskim |
| pubmed-article:15665867 | lifeskim:mentions | umls-concept:C1510470 | lld:lifeskim |
| pubmed-article:15665867 | lifeskim:mentions | umls-concept:C0086168 | lld:lifeskim |
| pubmed-article:15665867 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15665867 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:15665867 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:15665867 | pubmed:dateCreated | 2005-2-9 | lld:pubmed |
| pubmed-article:15665867 | pubmed:abstractText | Myosin V is a calmodulin-binding motor protein. The dissociation of single calmodulin molecules from individual myosin V molecules at 1 microM Ca(2+) correlates with a reduction in sliding velocity in an in vitro motility assay. The dissociation of two calmodulin molecules at 5 microM Ca(2+) correlates with a detachment of actin filaments from myosin V. To mimic the regulation of myosin V motility by Ca(2+) in a cell, caged Ca(2+) coupled with a UV flash system was used to produce Ca(2+) transients. During the Ca(2+) transient, myosin V goes through the functional cycle of reduced sliding velocity, actin detachment and reattachment followed by the recovery of the sliding velocity. These results indicate that myosin V motility is regulated by Ca(2+) through a reduction in actin-binding affinity resulting from the dissociation of single calmodulin molecules. | lld:pubmed |
| pubmed-article:15665867 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15665867 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15665867 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15665867 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15665867 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15665867 | pubmed:issn | 1545-9993 | lld:pubmed |
| pubmed-article:15665867 | pubmed:author | pubmed-author:HiguchiHideoH | lld:pubmed |
| pubmed-article:15665867 | pubmed:author | pubmed-author:NguyenHoaAnhH | lld:pubmed |
| pubmed-article:15665867 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15665867 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:15665867 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15665867 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15665867 | pubmed:pagination | 127-32 | lld:pubmed |
| pubmed-article:15665867 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15665867 | pubmed:meshHeading | pubmed-meshheading:15665867... | lld:pubmed |
| pubmed-article:15665867 | pubmed:meshHeading | pubmed-meshheading:15665867... | lld:pubmed |
| pubmed-article:15665867 | pubmed:meshHeading | pubmed-meshheading:15665867... | lld:pubmed |
| pubmed-article:15665867 | pubmed:meshHeading | pubmed-meshheading:15665867... | lld:pubmed |
| pubmed-article:15665867 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15665867 | pubmed:articleTitle | Motility of myosin V regulated by the dissociation of single calmodulin. | lld:pubmed |
| pubmed-article:15665867 | pubmed:affiliation | Center for Interdisciplinary Research, Tohoku University, Sendai 980-8578, Japan. | lld:pubmed |
| pubmed-article:15665867 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15665867 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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