Molecular determinants of coordinated proton and zinc inhibition of N-methyl-D-aspartate NR1/NR2A receptors (Q28776368)

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F Zheng

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P Lyuboslavsky

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S F Traynelis

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

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language of work or name

English

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publication date

26 September 2000

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published in

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volume

97

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issue

20

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page(s)

11062-7

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cites work

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Identification and mechanism of action of two histidine residues underlying high-affinity Zn2+ inhibition of the NMDA receptor.

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Four residues of the extracellular N-terminal domain of the NR2A subunit control high-affinity Zn2+ binding to NMDA receptors.

21 January 2018

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NMDA receptor channels: subunit-specific potentiation by reducing agents

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Phenylethanolamines inhibit NMDA receptors by enhancing proton inhibition

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Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins

21 January 2018

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N-terminal domains in the NR2 subunit control desensitization of NMDA receptors

21 January 2018

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Glycine-independent NMDA receptor desensitization: localization of structural determinants.

21 January 2018

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Selective release of endogenous zinc from the hippocampal mossy fibers in situ

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/10984504

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.180307497

1 reference

ADS bibcode

2000PNAS...9711062L

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1 reference

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PubMed publication ID

10984504

1 reference