Determination of Changes in the Phosphorylation State of the Neuron-Specific Protein Kinase C Substrate B-50 (GAP43) by Quantitative Immunoprecipitation-Reference-Cited by-同舟云学术

Determination of Changes in the Phosphorylation State of the Neuron-Specific Protein Kinase C Substrate B-50 (GAP43) by Quantitative Immunoprecipitation

Published:1989-01 Issue:1 Volume:52 Page:17-23
ISSN:0022-3042
Container-title:Journal of Neurochemistry
language:en
Short-container-title:J Neurochem

Author:

Graan P. N. E.,Dekker L. V.,Oestreicher A. B.,Voorn L.,Gispen W. H.

Publisher

Wiley

Subject

Cellular and Molecular Neuroscience,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1471-4159.1989.tb10892.x/fullpdf

Reference46 articles.

1. Polymyxin B, a selective inhibitor of protein kinase C, diminishes the release of noradrenaline and the enhancement of release caused by phorbol 12,13-dibutyrate

2. Phosphorylation of B-50 Protein by Calcium-Activated, Phospholipid-Dependent Protein Kinase and B-50 Protein Kinase

3. Phorbol ester receptors and protein kinase C in primary neuronal cultures: development and stimulation of endogenous phosphorylation.

4. Phosphoprotein F1: purification and characterization of a brain kinase C substrate related to plasticity

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