Phosphorylation status of the NR2B subunit of NMDA receptor regulates its interaction with calcium/calmodulin-dependent protein kinase II (Q24311994)

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28 January 2020

title

Phosphorylation status of the NR2B subunit of NMDA receptor regulates its interaction with calcium/calmodulin-dependent protein kinase II (English)

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9

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author name string

Rajeevkumar Raveendran

1

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28 January 2020

Sudarsana Devi Suma Priya

2

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28 January 2020

Madhavan Mayadevi

3

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28 January 2020

Mathew Steephan

4

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28 January 2020

Thankayyan R Santhoshkumar

5

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John Cheriyan

6

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Rajendran Sanalkumar

7

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Kurup K Pradeep

8

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Ramakrishnapillai V Omkumar

10

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28 January 2020

language of work or name

English

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publication date

21 April 2009

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28 January 2020

number of pages

14

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Journal of Neurochemistry

inferred from page(s)

published in

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volume

110

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issue

1

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page(s)

92-105

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Sequence determinants on the NR2A and NR2B subunits of NMDA receptor responsible for specificity of phosphorylation by CaMKII.

28 January 2020

cites work

1 reference

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Inhibitory effect of okadaic acid on the p-nitrophenyl phosphate phosphatase activity of protein phosphatases

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Interaction of peptide substrate outside the active site influences catalysis by CaMKII.

21 January 2018

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NMDA receptor subunit composition controls synaptic plasticity by regulating binding to CaMKII.

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Ca2 /calmodulin-dependent activation and inactivation mechanisms of alphaCaMKII and phospho-Thr286-alphaCaMKII.

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Interaction with the NMDA receptor locks CaMKII in an active conformation

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Regulation of NMDA channel function by endogenous Ca(2 )-dependent phosphatase

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Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression

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Molecular memory by reversible translocation of calcium/calmodulin-dependent protein kinase II.

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The molecular basis of CaMKII function in synaptic and behavioural memory

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Post-synaptic density-95 promotes calcium/calmodulin-dependent protein kinase II-mediated Ser847 phosphorylation of neuronal nitric oxide synthase

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Influence of a mutation in the ATP-binding region of Ca2 /calmodulin-dependent protein kinase II on its interaction with peptide substrates

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Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Identification of a phosphorylation site for calcium/calmodulindependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor

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7 January 2021

Autophosphorylation-dependent targeting of calcium/ calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl- D-aspartate receptor

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7 January 2021

Structural examination of autoregulation of multifunctional calcium/calmodulin-dependent protein kinase II

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7 January 2021

Mechanism and Regulation of Calcium/Calmodulin-dependent Protein Kinase II Targeting to the NR2B Subunit of theN-Methyl-d-aspartate Receptor

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7 January 2021

Evidence for direct protein kinase-C mediated modulation of N-methyl-D-aspartate receptor current.

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7 January 2021

Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation

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7 January 2021

Synaptic desensitization of NMDA receptors by calcineurin

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7 January 2021

Neuronal CA2 /calmodulin-dependent protein kinase II: the role of structure and autoregulation in cellular function

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7 January 2021

Effects of serine/threonine protein phosphatases on ion channels in excitable membranes

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7 January 2021

Identification of protein phosphatase 1 in synaptic junctions: dephosphorylation of endogenous calmodulin-dependent kinase II and synapse-enriched phosphoproteins

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7 January 2021

A mechanism for Ca2 /calmodulin-dependent protein kinase II clustering at synaptic and nonsynaptic sites based on self-association.

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7 January 2021

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

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28 January 2020

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017