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]
Producer: 19930128Description: 35-43 p. digitalISSN:- 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
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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