ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF

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 o...

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Bibliographic Details
Published in:	Cell Vol. 65; no. 4; p. 663
Main Authors:	Boulton, Teri G, Nye, Steven H, Robbins, David J, Ip, Nancy Y, Radziejewska, Elizabeth, Morgenbesser, Sharon D, DePinho, Ronald A, Panayotatos, Nikos, Cobb, Melanie H, Yancopoulos, George D
Format:	Journal Article
Language:	English
Published:	United States 17-05-1991
Subjects:	Amino Acid Sequence Animals Astrocytes - enzymology Base Sequence Cell Line Cells, Cultured Cloning, Molecular Enzyme Activation Hippocampus - enzymology Humans Insulin - pharmacology Mitogen-Activated Protein Kinase 1 Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinase 6 Mitogen-Activated Protein Kinases Molecular Sequence Data Nerve Growth Factors - pharmacology Organ Specificity Phosphorylation Protein Kinases - genetics Protein Kinases - isolation & purification Protein Kinases - metabolism Pseudogenes Rats Recombinant Proteins - metabolism Sequence Homology, Nucleic Acid Teratoma Tyrosine
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