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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1999-6-28
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pubmed:abstractText |
The protein kinase C (PKC) family has been implicated in the control of many cellular functions. Although PKC isotypes are characterized by their allosteric activation, phosphorylation also plays a key role in controlling activity. In classical PKC isotypes, one of the three critical sites is a carboxy-terminal hydrophobic site also conserved in other AGC kinase subfamily members. Although this site is crucial to the control of this class of enzymes, the upstream kinase(s) has not been identified.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0960-9822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
522-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:10339425-Animals,
pubmed-meshheading:10339425-Binding Sites,
pubmed-meshheading:10339425-Cell Line,
pubmed-meshheading:10339425-Chromones,
pubmed-meshheading:10339425-Enzyme Inhibitors,
pubmed-meshheading:10339425-Humans,
pubmed-meshheading:10339425-Morpholines,
pubmed-meshheading:10339425-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:10339425-Phosphorylation,
pubmed-meshheading:10339425-Protein Kinase C,
pubmed-meshheading:10339425-Rats,
pubmed-meshheading:10339425-Serine,
pubmed-meshheading:10339425-Sirolimus,
pubmed-meshheading:10339425-Substrate Specificity
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pubmed:year |
1999
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pubmed:articleTitle |
Rapamycin-sensitive phosphorylation of PKC on a carboxy-terminal site by an atypical PKC complex.
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pubmed:affiliation |
Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London, WC2A 3PX, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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