Protein kinase C potentiation of N-methyl-D-aspartate receptor activity is not mediated by phosphorylation of N-methyl-D-aspartate receptor subunits.

No abstract is available for this paper.

• Publication year

  1999

• Venue

  Proceedings of the National Academy of Sciences of the United States of America

• Publication date

  1999-12-21

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1073/PNAS.96.26.15262PMID 10611373PMCID PMC24808
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  1998cited by this paper
• Competitive binding of alpha-actinin and calmodulin to the NMDA receptor.

  1997cited by this paper
• Interaction of ion channels and receptors with PDZ domain proteins.

  1997cited by this paper
• Cyclic AMP-dependent Protein Kinase and Protein Kinase C Phosphorylate N-Methyl-d-aspartate Receptors at Different Sites*

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• Characterization of Protein Kinase A and Protein Kinase C Phosphorylation of the N-Methyl-D-aspartate Receptor NR1 Subunit Using Phosphorylation Site-specific Antibodies*

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• Developmental regulation and cell-specific expression of N-methyl-D-aspartate receptor splice variants in rat hippocampus.

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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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• Interaction of the N-Methyl—aspartate Receptor Complex with a Novel Synapse-associated Protein, SAP102*

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• Selective potentiation of N-methyl-D-aspartate-induced current by protein kinase C in Xenopus oocytes injected with rat brain RNA.

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• Multiple effects of phorbol esters in the rat spinal dorsal horn

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• Coexpression of N-methyl-D-aspartate and phencyclidine receptors in Xenopus oocytes injected with rat brain mRNA.

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