Synapsin I phosphorylated by Ca2+, calmodulin-dependent protein kinase II is able to self-degrade
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(91)80897-C/fullpdf
Reference14 articles.
1. Adenosine 3':5'-monophosphate-regulated phosphoprotein system of neuronal membranes. I. Solubilization, purification, and some properties of an endogenous phosphoprotein.
2. The cytoskeletal architecture of the presynaptic terminal and molecular structure of synapsin 1.
3. Differential phosphorylation of multiple sites in purified protein I by cyclic AMP-dependent and calcium-dependent protein kinases.
4. Multiple phosphorylation sites in protein I and their differential regulation by cyclic AMP and calcium.
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. Determination of synapsin I and synaptophysin in body fluids by two-site enzyme-linked immunosorbent assays;Journal of Immunological Methods;1998-06
2. Vesicle-associated proteins and calcium in nerve terminals of chick ciliary ganglia during development of facilitation.;The Journal of Physiology;1996-12-15
3. The synaptic vesicle and its targets;Neuroscience;1995-01
4. Simultaneous purification of the neuroproteins synapsin I and synaptophysin;Journal of Chromatography A;1992-04
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