Source:http://linkedlifedata.com/resource/pubmed/id/11865181
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
2002-2-26
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| pubmed:abstractText |
The kinases of mitogen-activated protein (MAP) kinase cascades transmit signals through sequential phosphorylation and activation of the enzymes. However, recent evidence indicates that protein-protein interactions between the kinases themselves or with substrates or other components are also a critical means of regulation. Whitmarsh and Davis summarize these findings with emphasis on new evidence from yeast that, when phosphorylated, a MAP kinase kinase actually switches from a negative regulator that binds to and inhibits its target MAP kinase to a positive regulator of that same enzyme.
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| pubmed:language |
eng
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| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:author | |
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
PE1
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:11865181-Animals,
pubmed-meshheading:11865181-Humans,
pubmed-meshheading:11865181-MAP Kinase Signaling System,
pubmed-meshheading:11865181-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11865181-Phosphorylation,
pubmed-meshheading:11865181-Phosphotransferases,
pubmed-meshheading:11865181-Signal Transduction
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| pubmed:articleTitle |
Signal transduction by MAP kinases: regulation by phosphorylation-dependent switches.
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| pubmed:affiliation |
Howard Hughes Medical Institute, Program in Molecular Medicine, Department of Biochemistry, University of Massachusetts Medical School, Worcester, MA 01605 USA. roger.davis@umassmed.edu
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| pubmed:publicationType |
Journal Article,
Review
|