Calpain-mediated proteolytic cleavage of the neuronal glycine transporter, GlyT2
Author:
Publisher
Wiley
Subject
Cellular and Molecular Neuroscience,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1471-4159.2003.02192.x/fullpdf
Reference38 articles.
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2. Structure and functions of inhibitory and excitatory glycine receptors;Betz;Ann. NY Acad. Sci.,1999
3. Calpain-mediated proteolysis of GluR1 subunits in organotypic hippocampal cultures following kainic acid treatment;Bi;Brain Res.,1998
4. Two glycine transporter variants with distinct localization in the CNS and peripheral tissues are encoded by a common gene;Borowsky;Neuron,1993
5. Calcium-activated neutral protease calpain system: structure, function and regulation;Croall;Physiol. Rev.,1991
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1. Correlation of calpain sensitivity, Bradford assay instability, and electrophoretic mobility in phosphomimetic mutants of GlyT2 N-terminus;Biochemistry and Biophysics Reports;2024-07
2. Neurobiology of glycine transporters: From molecules to behavior;Neuroscience & Biobehavioral Reviews;2020-11
3. Phosphorylation of Serine 157 Protects the Rat Glycine Transporter GlyT2 from Calpain Cleavage;Journal of Molecular Neuroscience;2020-03-14
4. Comparison of SynCAM1/CADM1 PDZ interactions with MUPP1 using mammalian and bacterial pull‐down systems;Brain and Behavior;2020-02-28
5. Phosphomimetic Mutation of Glycine Transporter GlyT1 C-Terminal PDZ Binding Motif Inhibits its Interactions with PSD95;Journal of Molecular Neuroscience;2019-11-18
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