Linked Life Data

16563742

Source:http://linkedlifedata.com/resource/pubmed/id/16563742

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-4-17
pubmed:abstractText
Myosin filaments interact with actin to generate muscle contraction and many forms of cell motility. X-ray and electron microscopy (EM) studies have revealed the general organization of myosin molecules in relaxed filaments, but technical difficulties have prevented a detailed description. Recent studies using improved ultrastructural and image analysis techniques are overcoming these problems. Three-dimensional reconstructions using single-particle methods have provided many new insights into the organization of the myosin heads and tails. Docking of atomic structures into cryo-EM density maps suggests how regulated myosin filaments are 'switched off', bringing about muscle relaxation. Additionally, sequence analysis suggests probable interactions between myosin tails in the backbone, whereas crystallographic and EM studies are starting to reveal tail interactions directly in three dimensions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0959-440X
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
204-12
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Structure and function of myosin filaments.
pubmed:affiliation
Department of Cell Biology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA. roger.craig@umassmed.edu
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Extramural