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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1994-6-30
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pubmed:abstractText |
One of the ways in which higher eukaryotes receive messages from the environment is via cell surface receptor tyrosine kinases. These are transmembrane proteins with an extracellular binding domain that specifies the growth factor with which it will interact, and an intracellular domain that encodes the tyrosine kinase. The mechanism by which receptor tyrosine kinases direct intracellular signal relay appears to involve receptor autophosphorylation that permits the stable binding of SH2 domain containing signal transduction enzymes. Some of the more recent advances are summarized in this review.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/IRS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin Receptor Substrate Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/STAT1 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/STAT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Src peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0959-437X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5-14
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8193540-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:8193540-Animals,
pubmed-meshheading:8193540-Cell Differentiation,
pubmed-meshheading:8193540-Cell Division,
pubmed-meshheading:8193540-DNA-Binding Proteins,
pubmed-meshheading:8193540-GRB2 Adaptor Protein,
pubmed-meshheading:8193540-Humans,
pubmed-meshheading:8193540-Insulin Receptor Substrate Proteins,
pubmed-meshheading:8193540-Oligopeptides,
pubmed-meshheading:8193540-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:8193540-Phosphoproteins,
pubmed-meshheading:8193540-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:8193540-Proteins,
pubmed-meshheading:8193540-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:8193540-STAT1 Transcription Factor,
pubmed-meshheading:8193540-Signal Transduction,
pubmed-meshheading:8193540-Trans-Activators,
pubmed-meshheading:8193540-Type C Phospholipases
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pubmed:year |
1994
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pubmed:articleTitle |
Receptor tyrosine kinases and their targets.
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pubmed:affiliation |
Department of Pediatrics, National Jewish Center for Immunology and Respiratory Medicine, Denver, Colorado 80206.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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