Linked Life Data

2983692

Source:http://linkedlifedata.com/resource/pubmed/id/2983692

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-4-4
pubmed:abstractText
Calmodulin and other calcium-modulated proteins bind in vitro to purified junctional polypeptides from rat liver gap junctions, bovine lens fiber junctions, a chymotryptic fragment from bovine lens junctions, and crayfish hepatopancreas gap junctions. The potential biological relevance of the interaction of calmodulin with junctional proteins is suggested by immunocytochemical localization of endogenous calmodulin in cortical regions of the cell where gap junctions exist. These observations provide a molecular basis for understanding the potential regulatory role of calmodulin on cell-cell communication channels in vivo. In addition, the calmodulin binding represents the first molecular homology that has been found for junctional channel proteins from mammalian and arthropod tissues.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
825-32
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Interaction of calmodulin and other calcium-modulated proteins with mammalian and arthropod junctional membrane proteins.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't