Source:http://linkedlifedata.com/resource/pubmed/id/11137038
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2001-2-5
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pubmed:abstractText |
Protein phosphatase 5 (PP5) possesses unique biochemical properties, which include its tetratricopeptide repeat (TPR) targeting/regulatory domain and its ability to be activated by lipids. PP5 has been studied as a paradigm for TPR protein structure and function. Roles for PP5 in signal transduction are emerging: from cell cycle regulation and signaling by nuclear receptors, to possible regulation of membrane receptors and ion channels.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1043-2760
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
28-32
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11137038-Animals,
pubmed-meshheading:11137038-Cell Cycle,
pubmed-meshheading:11137038-Humans,
pubmed-meshheading:11137038-Nuclear Proteins,
pubmed-meshheading:11137038-Phosphoprotein Phosphatases,
pubmed-meshheading:11137038-Potassium Channels,
pubmed-meshheading:11137038-Signal Transduction
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pubmed:articleTitle |
Protein phosphatase 5 in signal transduction.
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pubmed:affiliation |
Dept of Pharmacology, University of South Alabama, Mobile, AL 36688, USA. michaelc@jaguar1.usouthal.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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