Transient activation of a distinct serine protein kinase is responsible for 27-kDa heat shock protein phosphorylation in mitogen-stimulated and heat-shocked cells.

Zhou, M

Transient activation of a distinct serine protein kinase is responsible for 27-kDa heat shock protein phosphorylation in mitogen-stimulated and heat-shocked cells. [electronic resource] - The Journal of biological chemistry Jan 1993 - 35-43 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

0021-9258


Acid Phosphatase--metabolism
Adenosine Triphosphate--metabolism
Amino Acid Sequence
Animals
CHO Cells
Chromatography
Cricetinae
Durapatite
Enzyme Activation
Fibroblast Growth Factor 2--pharmacology
Heat-Shock Proteins--metabolism
Hot Temperature
Hydroxyapatites
Intracellular Signaling Peptides and Proteins
Kinetics
Molecular Sequence Data
Molecular Weight
Peptides--pharmacology
Phosphorylation
Protein Serine-Threonine Kinases--antagonists & inhibitors
Ribosomal Protein S6 Kinases
Signal Transduction
Substrate Specificity
Thrombin--pharmacology
Time Factors