Protein Phosphorylation Changes Ligand-Binding Efficiency of Cytochrome P450c17 (CYP17) and Accelerates Its Proteolytic Degradation: Putative Relevance for Hormonal Regulation of CYP17 Activity-Reference-Cited by-同舟云学术

Protein Phosphorylation Changes Ligand-Binding Efficiency of Cytochrome P450c17 (CYP17) and Accelerates Its Proteolytic Degradation: Putative Relevance for Hormonal Regulation of CYP17 Activity

Published:1997-02 Issue:2 Volume:231 Page:403-408
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Löhr Jörg B.,Kühn-Velten W.Nikolaus

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference30 articles.

1. Substrate-regulated, cAMP-dependent phosphorylation, denaturation, and degradation of glucocorticoid-inducible rat liver cytochrome P450 3A1

2. Relationship between phosphorylation and cytochrome P450 destruction

3. Isoenzyme-specific phosphorylation of cytochromes P-450 and other drug metabolizing enzymes

4. Adrenocortical cytochrome P-450 responsible for cholesterol side chain cleavage (P-450scc) is phosphorylated by the calcium-activated, phospholipid-sensitive protein kinase (protein kinase C)

5. Ethanol Induces CYP2E1 by Protein Stabilization

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