Linked Life Data

3839002

Source:http://linkedlifedata.com/resource/pubmed/id/3839002

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-7-12
pubmed:abstractText
A phosphorylation occurs at two sites in chicken gizzard myosin light chain kinase that appears to be catalyzed by an autophosphorylation reaction. This reaction is inhibited by approximately 75% in the presence of Ca2+-calmodulin, but is unaffected by the cAMP-dependent protein kinase inhibitor. Whereas the catalytic subunit of cAMP-dependent protein kinase phosphorylates myosin light chain kinase at only serine residues, the non cAMP-dependent phosphorylation occurs at both serine and threonine residues. One, if not both, of these latter sites are distinct from the sites recognized by the catalytic subunit of cAMP-dependent protein kinase. Consequently, there must be at least three and possibly four sites in myosin light chain kinase capable of incorporating phosphate, either in response to catalytic subunit or by autophosphorylation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0746-3898
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
143-55
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Characterization and analysis of an apparent autophosphorylation of chicken gizzard myosin light chain kinase.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.