Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1992-1-9
|
pubmed:abstractText |
The model of calcium-channel gating described above, although almost certainly too simple, suggests a direct role for protein kinases and phosphatases in determining the kinetics of calcium channel gating on a subsecond time scale. In addition, it provides a unique perspective for understanding studies of calcium channel gating under widely different metabolic and pharmacological conditions. Although many of these effects may be specific to the dihydropyridine-sensitive or L-type calcium channel, they give an indication of the range of possibilities for integrating calcium-channel activity with cellular biochemistry.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0077-8923
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
635
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
26-34
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:1660238-Animals,
pubmed-meshheading:1660238-Calcium Channels,
pubmed-meshheading:1660238-Dihydropyridines,
pubmed-meshheading:1660238-Ion Channel Gating,
pubmed-meshheading:1660238-Phosphoprotein Phosphatases,
pubmed-meshheading:1660238-Phosphorylation,
pubmed-meshheading:1660238-Protein Kinases
|
pubmed:year |
1991
|
pubmed:articleTitle |
Enzymatic gating of voltage-activated calcium channels.
|
pubmed:affiliation |
Laboratory of Cellular and Molecular Pharmacology, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709.
|
pubmed:publicationType |
Journal Article,
Review
|