Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Intracellular Mg2+ interacts with structural determinants of the narrow constriction contributed by the NR1-subunit in the NMDA receptor channel.

The Journal of physiology - 1 Jan 1998

Wollmuth L P, Kuner T, Sakmann B

Abstract excerpt

1. N-methyl-D-aspartate (NMDA) receptor channels are blocked by intracellular Mg2+ in a voltage-dependent manner. Amino acid residues positioned at or near the narrow constriction that interact with intracellular Mg2+ were identified in recombinant NR1-NR2A channels expressed in Xenopus oocytes o...

Topics

Animals
Asparagine
Calcium
Cell Line
Electrophysiology
Humans
Ion Channel Gating
Magnesium
Membrane Potentials
Mutation
Oocytes
Receptors, N-Methyl-D-Aspartate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Solutions

Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 9481671
DOI: 10.1111/j.1469-7793.1998.00033.x
PMCID: PMC2230705

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9481671-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Intracellular Mg2+ interacts with structural determinants of the narrow constriction contributed by the NR1-subunit in the NMDA receptor channel.PMID 9481671Read ↗

Adjacent asparagines in the NR2-subunit of the NMDA receptor channel control the voltage-dependent block by extracellular Mg2+.Semantic proximity Read ↗

Internal Mg2+ block of recombinant NMDA channels mutated within the selectivity filter and expressed in Xenopus oocytes.Semantic proximity Read ↗

Open-channel block of Na+ channels by intracellular Mg2+.Semantic proximity Read ↗

Lack of negatively charged residues at the external mouth of Kir2.2 channels enable the voltage-dependent block by external Mg2+.Semantic proximity Read ↗

Ring of negative charge in BK channels facilitates block by intracellular Mg2+ and polyamines through electrostatics.Semantic proximity Read ↗

Site within N-Methyl-D-aspartate receptor pore modulates channel gating.Semantic proximity Read ↗

Control of voltage-independent zinc inhibition of NMDA receptors by the NR1 subunit.Semantic proximity Read ↗

Differential responses of disease-related GRIN variants located in pore-forming M2 domain of N-methyl-D-aspartate receptor to FDA-approved inhibitors.Semantic proximity Read ↗

Intracellular Mg2+ is a voltage-dependent pore blocker of HCN channels.Semantic proximity Read ↗

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

NMDAR channel segments forming the extracellular vestibule inferred from the accessibility of substituted cysteines.Semantic proximity Read ↗

Characterization of the effects of charged residues in the intracellular loop on ion permeation in alpha1 glycine receptor channels.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.