Palmitylation of neuromodulin (GAP-43) is not required for phosphorylation by protein kinase C.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference70 articles.
1. Protein kinase C phosphorylates a 47 Mr protein (F1) directly related to synaptic plasticity
2. Calcium-promoted translocation of protein kinase C to synaptic membranes: relation to the phosphorylation of an endogenous substrate (protein F1) involved in synaptic plasticity
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4. Widespread occurrence of "87 kDa," a major specific substrate for protein kinase C.
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1. Genetic labelling of specific axonal pathways in the mouse central nervous system;European Journal of Neuroscience;2002-03
2. bFGF Stimulates GAP-43 Phosphorylation at Ser41 and Modifies Its Intracellular Localization in Cultured Hippocampal Neurons;Molecular and Cellular Neuroscience;2000-12
3. Direct Observation of Trapping and Release of Nitric Oxide by Glutathione and Cysteine with Electron Paramagnetic Resonance Spectroscopy;Biophysical Journal;2000-03
4. Continuous phosphorylation of GAP-43 and MARCKS by long-term TPA treatment in SK-N-SH human neuroblastoma cells;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1999-04
5. Interactions between Neurogranin and Calmodulin in Vivo;Journal of Biological Chemistry;1999-03
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