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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2010-10-13
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pubmed:abstractText |
Proteinase-activated-receptor-2 (PAR2) is a seven transmembrane receptor that can activate two separate signaling arms: one through G?q and Ca2+ mobilization, and a second through recruitment of ?-arrestin scaffolds. In some cases downstream targets of the G?q/Ca2+ signaling arm are directly inhibited by ?-arrestins, while in other cases the two pathways are synergistic; thus ?-arrestins act as molecular switches capable of modifying the signal generated by the receptor.
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pubmed:grant |
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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:issn |
1471-2091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
36
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pubmed:meshHeading |
pubmed-meshheading:20858278-Animals,
pubmed-meshheading:20858278-Arrestins,
pubmed-meshheading:20858278-Calcium-Calmodulin-Dependent Protein Kinase Kinase,
pubmed-meshheading:20858278-Mice,
pubmed-meshheading:20858278-NIH 3T3 Cells,
pubmed-meshheading:20858278-Phosphorylation,
pubmed-meshheading:20858278-Protein Kinases,
pubmed-meshheading:20858278-Receptor, PAR-2,
pubmed-meshheading:20858278-Recombinant Proteins,
pubmed-meshheading:20858278-Signal Transduction
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pubmed:year |
2010
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pubmed:articleTitle |
Beta-arrestin inhibits CAMKKbeta-dependent AMPK activation downstream of protease-activated-receptor-2.
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pubmed:affiliation |
Division of Biomedical Sciences University of California Riverside, California, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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