Mode of action of quinacrine on the acetylcholine receptor ionic channel complex.

doi:10.1016/s0026-895x(25)13769-3

Paper

Mode of action of quinacrine on the acetylcholine receptor ionic channel complex.

Published Sep 1, 1979 · Ming-Cheng Tsai, A. C. Oliveira, E. X. Albuquerque

Molecular pharmacology

Q1 SJR score

39

Citations

0

Influential Citations

Full textSemantic Scholar

Abstract

Abstract hidden due to publisher request; this does not indicate any issues with the research. Click the full text link above to read the abstract and view the original source.

In Vitro Study

Study Snapshot

Quinacrine blocks neuromuscular transmission by complexly interacting with both the acetylcholine receptor and its ionic channel, affecting both agonist and antagonist effects.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Sign up to use Study Snapshot

Consensus is limited without an account. Create an account or sign in to get more searches and use the Study Snapshot.

Create an account

Paper

Mode of action of quinacrine on the acetylcholine receptor ionic channel complex.

Sign up to use Study Snapshot

References

Citations

Structural effects of quinacrine binding in the open channel of the acetylcholine receptor

Quinacrine binding in the open channel of the acetylcholine receptor causes structural changes, potentially affecting the resting gate and removing obstructions in the closed channel.

Efficacy of certain quinolines as pharmacological antagonists in botulinum neurotoxin poisoning.

Certain 4-aminoquinolines and quinacrine can prolong the time to 50% block of neuromuscular transmission in botulinum neurotoxin poisoning, potentially through raising endosomal pH or inhibiting toxin-induced channel formation.

Pharmacology of the SV channel in the vacuolar membrane of chenopodium rubrum suspension cells

The slow-activating (SV) cation-selective ion channel in Chenopodium rubrum suspension cells shows pharmacological properties similar to Maxi-K channels in animal systems, with blockers acting voltage-dependently and cytoplasmically.

The pharmacology of cholinoceptors on the somatic muscle cells of the parasitic nematode Ascaris suum.

The Ascaris nicotinic receptor exhibits some of the pharmacological properties of each type of vertebrate nicotinic receptor, with acetylcholine eliciting depolarization and increased input conductance in muscle cells.

Mapping the alpha-subunit site photolabeled by the noncompetitive inhibitor [3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor.

The [3H]QA-labeled peptide identified the alpha-subunit site of the nicotinic acetylcholine receptor, suggesting that it may play a role in regulating nicotinic acetylcholine receptor function.