Identification of a major autophosphorylation site on postsynaptic density-associated Ca2+/calmodulin-dependent protein kinase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference32 articles.
1. Biochemical and immunochemical evidence that the "major postsynaptic density protein" is a subunit of a calmodulin-dependent protein kinase.
2. Evidence that the major postsynaptic density protein is a component of a Ca2+/calmodulin-dependent protein kinase.
3. An essential role for postsynaptic calmodulin and protein kinase activity in long-term potentiation
4. Inhibition of Postsynaptic PKC or CaMKII Blocks Induction But Not Expression of LTP
5. Long-term potentiation is associated with an increased activity of Ca2+/calmodulin-dependent protein kinase II.
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1. Proteomic Analysis of Postsynaptic Protein Complexes Underlying Neuronal Plasticity;ACS Chemical Neuroscience;2017-02-23
2. Quantitative Proteomics Analysis of CaMKII Phosphorylation and the CaMKII Interactome in the Mouse Forebrain;ACS Chemical Neuroscience;2015-02-24
3. Regulation of CaMKII by phospho-Thr253 or phospho-Thr286 sensitive targeting alters cellular function;Cellular Signalling;2010-05
4. Regulation of phosphorylation at the postsynaptic density during different activity states of Ca2+/calmodulin-dependent protein kinase II;Biochemical and Biophysical Research Communications;2010-01
5. Regulation of CaMKII In vivo: The Importance of Targeting and the Intracellular Microenvironment;Neurochemical Research;2009-05-05
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