Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2003-8-29
pubmed:abstractText
Myosin-Va, a processive actin-based motor thought to be involved in organelle transport, now stands ready to join myosin-II (from muscle) as one of the most highly characterized members of the myosin superfamily. Recent reports from the laboratories of Goldman and colleagues and Selvin and colleagues have provided unprecedented, high-resolution views of the structural changes that take place while this motor moves along its track. Taken together, the new results indicate that myosin-Va tilts its light chain binding domains to 'walk' along actin in a hand-over-hand fashion.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0962-8924
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
447-51
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Myosin-V motility: these levers were made for walking.
pubmed:affiliation
Department of Molecular, Cellular and Developmental Biology, Yale University, 342 Kline Biology Tower, 266 Whitney Avenue, New Haven, CT 06511, USA. matthew.tyska@yale.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review