| Literature DB >> 15647159 |
H Lee Sweeney1, Anne Houdusse.
Abstract
It is 50 years since the sliding of actin and myosin filaments was proposed as the basis of force generation and shortening in striated muscle. Although this is now generally accepted, the detailed molecular mechanism of how myosin uses adenosine triphosphate to generate force during its cyclic interaction with actin is only now being unravelled. New insights have come from the unconventional myosins, especially myosin V. Myosin V is kinetically tuned to allow movement on actin filaments as a single molecule, which has led to new kinetic, mechanical and structural data that have filled in missing pieces of the actomyosin-chemo-mechanical transduction puzzle.Entities:
Mesh:
Substances:
Year: 2004 PMID: 15647159 PMCID: PMC1693472 DOI: 10.1098/rstb.2004.1576
Source DB: PubMed Journal: Philos Trans R Soc Lond B Biol Sci ISSN: 0962-8436 Impact factor: 6.237