Dephosphorylation of Neurofilaments by Exogenous Phosphatases Has No Effect on Reassembly of Subunits
Author:
Publisher
Wiley
Subject
Cellular and Molecular Neuroscience,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1471-4159.1986.tb04526.x/fullpdf
Reference28 articles.
1. Slow posttranslational modification of a neurofilament protein;Bennett;J. Cell Biol.,1985
2. Vimentin filaments are assembled from a soluble precursor in avian erythroid cells;Blikstad;J. Cell Biol.,1983
3. Decomposition of phosphoserine and phosphothreonine during acid hydrolysis;Bylund;Anal. Biochem.,1976
4. The structure, biochemical properties and immunogenicity of neurofilament peripheral regions are determined by phosphorylation state;Carden;J. Biol. Chem.,1985
5. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane;Fairbanks;Biochemistry,1971
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1. Phosphorylation state of the native high-molecular-weight neurofilament subunit protein from cervical spinal cord in sporadic amyotrophic lateral sclerosis;Journal of Neurochemistry;2001-12-20
2. Neurofilament-L Is a Protein Phosphatase-1-binding Protein Associated with Neuronal Plasma Membrane and Post-synaptic Density;Journal of Biological Chemistry;2000-01
3. Contiguous phosphorylated and non-phosphorylated domains along axonal neurofilaments;Journal of Cell Science;1998-02-15
4. Triton-soluble phosphovariants of the heavy neurofilament subunit in developing and mature mouse central nervous system;Journal of Neuroscience Research;1997-06-15
5. Neurofilament phosphorylation;Biochemistry and Cell Biology;1995-09-01
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