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

Structural basis for severe pain caused by mutations in the S4-S5 linkers of voltage-gated sodium channel NaV1.7.

Proceedings of the National Academy of Sciences of the United States of America - 4 Apr 2023

Wisedchaisri Goragot, Gamal El-Din Tamer M, Zheng Ning, Catterall William A

Abstract excerpt

Gain-of-function mutations in voltage-gated sodium channel NaV1.7 cause severe inherited pain syndromes, including inherited erythromelalgia (IEM). The structural basis of these disease mutations, however, remains elusive. Here, we focused on three mutations that all substitute threonine residues...

Topics

Humans
NAV1.7 Voltage-Gated Sodium Channel
Pain
Mutation
Erythromelalgia
Voltage-Gated Sodium Channels
Threonine

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 36996107
DOI: 10.1073/pnas.2219624120
PMCID: PMC10083536

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-36996107-2026-08-30.1. 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

Structural basis for severe pain caused by mutations in the S4-S5 linkers of voltage-gated sodium channel NaV1.7.PMID 36996107Read ↗

Structural basis for severe pain caused by mutations in the voltage sensors of sodium channel NaV1.7.Semantic proximity Read ↗

Erythromelalgia mutation Q875E Stabilizes the activated state of sodium channel Nav1.7.Semantic proximity Read ↗

Mutations at opposite ends of the DIII/S4-S5 linker of sodium channel Na V 1.7 produce distinct pain disorders.Semantic proximity Read ↗

Size matters: Erythromelalgia mutation S241T in Nav1.7 alters channel gating.Semantic proximity Read ↗

Unwinding and spiral sliding of S4 and domain rotation of VSD during the electromechanical coupling in Nav1.7.Semantic proximity Read ↗

Paroxysmal extreme pain disorder mutations within the D3/S4-S5 linker of Nav1.7 cause moderate destabilization of fast inactivation.Semantic proximity Read ↗

NaV1.7 gain-of-function mutations as a continuum: A1632E displays physiological changes associated with erythromelalgia and paroxysmal extreme pain disorder mutations and produces symptoms of both disorders.Semantic proximity Read ↗

Inherited erythermalgia: limb pain from an S4 charge-neutral Na channelopathy.Semantic proximity Read ↗

L596-W733 bond between the start of the S4-S5 linker and the TRP box stabilizes the closed state of TRPV4 channel.Semantic proximity Read ↗

The S4---S5 linker - gearbox of TRP channel gating.Semantic proximity Read ↗

Regulation and drug modulation of a voltage-gated sodium channel: Pivotal role of the S4-S5 linker in activation and slow inactivation.Semantic proximity Read ↗

Dissection of the structure-function relationship of Nav channels.Semantic proximity Read ↗

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