rdf:type |
|
lifeskim:mentions |
umls-concept:C0015576,
umls-concept:C0021641,
umls-concept:C0027752,
umls-concept:C0041485,
umls-concept:C0109317,
umls-concept:C0752312,
umls-concept:C0871261,
umls-concept:C1150579,
umls-concept:C1333340,
umls-concept:C1366882,
umls-concept:C1370600,
umls-concept:C1414387,
umls-concept:C1704632,
umls-concept:C1705767,
umls-concept:C1705791,
umls-concept:C1706817,
umls-concept:C1879547,
umls-concept:C2911692
|
pubmed:issue |
4
|
pubmed:dateCreated |
1991-6-27
|
pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M60958,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M60959,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M60960,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M60961,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M60962,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M61177,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64300,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64301,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64302,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64383,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64384
|
pubmed:abstractText |
We recently described the purification and cloning of extracellular signal-regulated kinase 1 (ERK1), which appears to play a pivotal role in converting tyrosine phosphorylation into the serine/threonine phosphorylations that regulate downstream events. We now describe cloning and characterization of two ERK1-related kinases, ERK2 and ERK3, and provide evidence suggesting that there are additional ERK family members. At least two of the ERKs are activated in response to growth factors; their activations correlate with tyrosine phophorylation, but also depend on additional modifications. Transcripts corresponding to the three cloned ERKs are distinctly regulated both in vivo and in a differentiating cell line. Thus, this family of kinases may serve as intermediates that depend on tyrosine phosphorylation to activate serine/threonine phosphorylation cascades. Individual family members may mediate responses in different developmental stages, in different cell types, or following exposure to different extracellular signals.
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pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0092-8674
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
17
|
pubmed:volume |
65
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
663-75
|
pubmed:dateRevised |
2011-11-17
|
pubmed:meshHeading |
pubmed-meshheading:2032290-Amino Acid Sequence,
pubmed-meshheading:2032290-Animals,
pubmed-meshheading:2032290-Astrocytes,
pubmed-meshheading:2032290-Base Sequence,
pubmed-meshheading:2032290-Cell Line,
pubmed-meshheading:2032290-Cells, Cultured,
pubmed-meshheading:2032290-Cloning, Molecular,
pubmed-meshheading:2032290-Enzyme Activation,
pubmed-meshheading:2032290-Hippocampus,
pubmed-meshheading:2032290-Humans,
pubmed-meshheading:2032290-Insulin,
pubmed-meshheading:2032290-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:2032290-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:2032290-Mitogen-Activated Protein Kinase 6,
pubmed-meshheading:2032290-Mitogen-Activated Protein Kinases,
pubmed-meshheading:2032290-Molecular Sequence Data,
pubmed-meshheading:2032290-Nerve Growth Factors,
pubmed-meshheading:2032290-Organ Specificity,
pubmed-meshheading:2032290-Phosphorylation,
pubmed-meshheading:2032290-Protein Kinases,
pubmed-meshheading:2032290-Pseudogenes,
pubmed-meshheading:2032290-Rats,
pubmed-meshheading:2032290-Recombinant Proteins,
pubmed-meshheading:2032290-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2032290-Teratoma,
pubmed-meshheading:2032290-Tyrosine
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pubmed:year |
1991
|
pubmed:articleTitle |
ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF.
|
pubmed:affiliation |
Department of Pharmacology, University of Texas Southwestern Graduate School of Biomedical Sciences, Dallas 75235-9041.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|