Linked Life Data

1464620

Source:http://linkedlifedata.com/resource/pubmed/id/1464620

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1993-1-21
pubmed:abstractText
Monoclonal antibodies specific for the rod region can affect smooth muscle myosin's motor properties. Actin movement by phosphorylated myosin was inhibited by an antibody (LMM.4) which binds to the COOH-terminal end of the coiled-coil rod, a region thought to be involved in filament assembly. The actin-activated ATPase activity of the myosin-antibody LMM.4 complex was also reduced 10-fold at actin concentrations that gave maximal turnover rates with filamentous myosin. Metal-shadowing of the phosphorylated myosin-antibody complex at low ionic strength showed small bundles of parallel extended molecules, instead of filaments. Five other anti-rod antibodies had little or no effect on myosin's ability to act as a motor. This is the first demonstration that a muscle myosin's activity is affected by its state of assembly. A common theme that emerges from the studies on both muscle and non-muscle myosins is that assembly into a filamentous structure stimulates the activity of the individual myosin molecules.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26091-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Inhibition of smooth muscle myosin's activity and assembly by an anti-rod monoclonal antibody.
pubmed:affiliation
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't