Regulation of the Phosphorylation and Dephosphorylation of a 96,000 Dalton Phosphoprotein (P96) in Intact Synaptosomes
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Publisher
Springer US
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http://link.springer.com/content/pdf/10.1007/978-1-4684-7618-7_12.pdf
Reference23 articles.
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3. Chan, S. Y., Hess, E. J., Rahamimoff, H. and Goldin, S. M., Purification and immunological characterization of a calcium pump from bovine brain synaptosomal vesicles, J. Neurosci. 4:1468 (1984).
4. DeLorenzo, R. J., The calmodulin hypothesis of neurotransmission, Cell Calcium 2:399 (1981).
5. DeLorenzo, R. J., Freedman, S. D., Yohe, W. B. and Maurer, S. C., Stimulation of Ca2+-dependent neurotransmitter release and presynaptic nerve terminal protein phosphorylation by a calmodulin-like protein isolated from synaptic vesicles, Proc. Natl. Acad. Sci. 76:1838 (1979).
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Differential stimulation of protein kinase C activity by phorbol ester or calcium/phosphatidylserine in vitro and in intact synaptosomes.;Journal of Biological Chemistry;1992-10
2. Localized Ca2+ entry preferentially effects protein dephosphorylation, phosphorylation, and glutamate release.;Journal of Biological Chemistry;1992-01
3. The role of protein kinase C and its neuronal substrates dephosphin, B-50, and MARCKS in neurotransmitter release;Molecular Neurobiology;1991-06
4. Dephosphin, a 96 000 Da substrate of protein kinase C in synaptosomal cytosol, is phosphorylated in intact synaptosomes;FEBS Letters;1991-05-06
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