Activation Mechanisms of Conventional Protein Kinase C Isoforms Are Determined by the Ligand Affinity and Conformational Flexibility of Their C1 Domains-Reference-Cited by-同舟云学术

Activation Mechanisms of Conventional Protein Kinase C Isoforms Are Determined by the Ligand Affinity and Conformational Flexibility of Their C1 Domains

Published:2003-11 Issue:47 Volume:278 Page:46886-46894
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ananthanarayanan Bharath,Stahelin Robert V.,Digman Michelle A.,Cho Wonhwa

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. Protein Kinase C: Structural and Spatial Regulation by Phosphorylation, Cofactors, and Macromolecular Interactions

2. Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm

3. Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester

4. New insights into the regulation of protein kinase C and novel phorbol ester receptors

5. Membrane Targeting by C1 and C2 Domains

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