Amanote Research
Register
Sign In
Mechanism of Inhibition of Protein Kinase C by 14-3-3 Isoforms. 14-3-3 Isoforms Do Not Have Phospholipase A2 Activity.
Biochemical Journal
- United Kingdom
doi 10.1042/bj2990853
Full Text
Open PDF
Abstract
Available in
full text
Categories
Biochemistry
Cell Biology
Molecular Biology
Date
May 1, 1994
Authors
K Robinson
D Jones
Y Patel
H Martin
J Madrazo
S Martin
S Howell
M Elmore
M J Finnen
A Aitken
Publisher
Portland Press Ltd.
Related search
Transgenic 14-3-3 Isoforms in Plants: The Metabolite Profiling of Repressed 14-3-3 Protein Synthesis in Transgenic Potato Plants
Biochemical Society Transactions
Biochemistry
MEKK2 Kinase Association With 14-3-3 Protein Regulates Activation of C-Jun N-Terminal Kinase
Journal of Biological Chemistry
Biochemistry
Cell Biology
Molecular Biology
Divalent Cation Effects on Interactions Between Multiple Arabidopsis 14-3-3 Isoforms and Phosphopeptide Targets
Molecular Tweezers Modulate 14-3-3 Protein-Protein Interactions
Identification of 14-3-3 Proteins in Human Platelets: Effects of Synthetic Peptides on Protein Kinase C Activation
Biochemical Journal
Biochemistry
Cell Biology
Molecular Biology
Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding
Biophysical Journal
Biophysics
Characterisation of Protein Isoforms Encoded by the Drosophila Glycogen Synthase Kinase 3 Gene Shaggy
Sphingosine-Dependent Protein Kinase-1, Directed to 14-3-3, Is Identified as the Kinase Domain of Protein Kinase Cδ
Journal of Biological Chemistry
Biochemistry
Cell Biology
Molecular Biology
G-Protein-Coupled Receptors Mediate 14-3-3 Signal Transduction
Signal Transduction and Targeted Therapy
Cancer Research
Genetics
