Rapid changes in nuclear protein tyrosine phosphorylation after growth hormone treatment in vivo. Identification of phosphorylated mitogen-activated protein kinase and STAT91.-Reference-Cited by-同舟云学术

Rapid changes in nuclear protein tyrosine phosphorylation after growth hormone treatment in vivo. Identification of phosphorylated mitogen-activated protein kinase and STAT91.

Published:1994-03 Issue:11 Volume:269 Page:7874-7878
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Gronowski A.M.,Rotwein P.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. The Prolactin/Growth Hormone Receptor Family

2. Evidence for involvement of the growth hormone receptor-associated tyrosine kinase in actions of growth hormone.

3. Stimulation by growth hormone of MAP kinase activity in 3T3-F442A fibroblasts.

4. Growth hormone (GH) induction of tyrosine phosphorylation and activation of mitogen-activated protein kinases in cells transfected with rat GH receptor cDNA

5. Growth hormone stimulates the tyrosine phosphorylation of 42- and 45-kDa ERK-related proteins.

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