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

Quinidine normalizes the open duration of slow-channel mutants of the acetylcholine receptor.

Neuroreport - 1 Jun 1998

Fukudome T, Ohno K, Brengman J M, Engel A G

Abstract excerpt

Quinidine is a long-lived open-channel blocker of the wild-type endplate acetylcholine receptor (AChR). To test the hypothesis that quinidine can normalize the prolonged channel opening events of slow-channel mutants of human AChR, we expressed wild-type AChR and five well characterized slow-chan...

Topics

Cholinergic Antagonists
Humans
Linear Models
Logistic Models
Membrane Potentials
Mutation
Patch-Clamp Techniques
Quinidine
Receptors, Cholinergic

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 9665624
DOI: 10.1097/00001756-199806010-00044

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9665624-2026-08-30.1. 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

Quinidine normalizes the open duration of slow-channel mutants of the acetylcholine receptor.PMID 9665624Read ↗

Quinine sulfate as a therapeutic option in a patient with slow channel congenital myasthenic syndrome.Semantic proximity Read ↗

A novel fast-channel myasthenia caused by mutation in β subunit of AChR reveals subunit-specific contribution of the intracellular M1-M2 linker to channel gating.Semantic proximity Read ↗

New mutations in acetylcholine receptor subunit genes reveal heterogeneity in the slow-channel congenital myasthenic syndrome.Semantic proximity Read ↗

Novel beta subunit mutation causes a slow-channel syndrome by enhancing activation and decreasing the rate of agonist dissociation.Semantic proximity Read ↗

Modulation of the Ca(2+) permeability of human endplate acetylcholine receptor-channel.Semantic proximity Read ↗

Repurposing polyamines to prevent life-threatening arrhythmias in Short QT Syndrome type 3.Semantic proximity Read ↗

Slow‐channel mutation in acetylcholine receptor αM4 domain and its efficient knockdownSemantic proximity Read ↗

Mouse Model of Fast-Channel Genetic Myasthenic Syndrome Carrying Chrne p.P141L Mutation.Semantic proximity Read ↗

Slow-channel myasthenic syndrome caused by enhanced activation, desensitization, and agonist binding affinity attributable to mutation in the M2 domain of the acetylcholine receptor alpha subunit.Semantic proximity Read ↗

Treatment of slow-channel congenital myasthenic syndrome in a Thai family with fluoxetine.Semantic proximity Read ↗

End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease.Semantic proximity Read ↗

Ranolazine for Congenital Long-QT Syndrome Type III: Experimental and Long-Term Clinical Data.Semantic proximity Read ↗

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