Properties of a Protein Kinase C Activity in Synaptic Plasma Membrane and Postsynaptic Density Fractions Isolated from Canine Cerebral Cortex
Author:
Publisher
Wiley
Subject
Cellular and Molecular Neuroscience,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1471-4159.1989.tb09240.x/fullpdf
Reference101 articles.
1. Calcium-promoted translocation of protein kinase C to synaptic membranes: relation to the phosphorylation of an endogenous substrate (protein F1) involved in synaptic plasticity
2. Translocation of Protein Kinase C Activity May Mediate Hippocampal Long-Term Potentiation
3. Inhibition by calmodulin of calcium/phospholipid-dependent protein phosphorylation.
4. Widespread occurrence of "87 kDa," a major specific substrate for protein kinase C.
5. Regulation of calmodulin binding to P-57. A neurospecific calmodulin binding protein.
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1. Rapid Translocation of Cytosolic Ca2+/Calmodulin-Dependent Protein Kinase II into Postsynaptic Density After Decapitation;Journal of Neurochemistry;2002-11-23
2. Insect 86 kDa protein kinase C substrate is a filament interacting protein regulated by Ca2+/calmodulin and phosphorylation;Brain Research;1997-05
3. Protein kinases involved in the expression of long-term potentiation;International Journal of Biochemistry;1994-06
4. Characterization of protein kinase C activities in postsynaptic density fractions prepared from cerebral cortex, hippocampus, and cerebellum;Brain Research;1993-08
5. Associative learning potentiates protein kinase C activation in synaptosomes of the rabbit hippocampus.;Proceedings of the National Academy of Sciences;1993-05-01
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