Linked Life Data

4033798

Source:http://linkedlifedata.com/resource/pubmed/id/4033798

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6033
pubmed:dateCreated
1985-10-22
pubmed:abstractText
It is now widely accepted that the ATP-induced active sliding of adjacent thin and thick filaments mediated by myosin heads (cross-bridges) is responsible for muscle contraction. Despite intensive studies, the behaviour of the myosin heads during muscle contraction is still unclear. Recent progress in the rapid freezing electron microscope technique has greatly improved the temporal resolution of the images that can be obtained. Here, we report a new type of actomyosin structure captured by rapid freezing. We have analysed images from thin sections of freeze-substituted rabbit skeletal muscle rapidly frozen during isometric contraction. For comparison, we also studied relaxed and rigor muscles. Our results show that, during isometric contraction, most myosin heads are regularly arrayed along the helix of the actin filaments and that this actomyosin structure appears to be distinct from that observed in rigor muscle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:volume
317
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
182-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Actomyosin structure in contracting muscle detected by rapid freezing.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't