Effect of Digestion with Phospholipase A2on Endogenous Protein Phosphorylation in Particulate Fractions from Rat Brain Synaptosomes
Author:
Publisher
Wiley
Subject
Cellular and Molecular Neuroscience,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1471-4159.1987.tb05637.x/fullpdf
Reference22 articles.
1. Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain.
2. Use of phospholipid-converting enzymes for the study of membrane-bound enzymes
3. Protein Phosphorylation and Neuronal Function
4. Synapsin I (protein I), a nerve terminal-specific phosphoprotein. I. Its general distribution in synapses of the central and peripheral nervous system demonstrated by immunofluorescence in frozen and plastic sections.
5. Synapsin I (Protein I), a nerve terminal-specific phosphoprotein. II. Its specific association with synaptic vesicles demonstrated by immunocytochemistry in agarose-embedded synaptosomes.
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1. Inhibition of Phosphorylation of Synapsin I and Other Synaptosomal Proteins by β-Bungarotoxin, a Phospholipase A2 Neurotoxin;Journal of Neurochemistry;2006-10-05
2. Association of cyclic-AMP-dependent protein kinase with neurofilaments;Biochemical Journal;1992-03-01
3. Temporal changes in edema, Na+, K+, and Ca++ in focal cortical stroke: GM1 ganglioside reduces ischemic injury;Journal of Neuroscience Research;1991-11
4. Inhibition of phosphorylation of rat synaptosomal proteins by snake venom phospholipase A2 neurotoxins (β-bungarotoxin, notexin) and enzymes (Naja naja atra, Naja nigricollis);Toxicon;1990-01
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