Acetylcholine mustard labels the binding site aspartate in muscarinic acetylcholine receptors.

doi:10.1016/s0021-9258(17)41747-9

Paper

Acetylcholine mustard labels the binding site aspartate in muscarinic acetylcholine receptors.

Published Feb 11, 1994 · T. Spalding, N. Birdsall, C. Curtis

The Journal of biological chemistry

Q1 SJR score

73

Citations

2

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Abstract

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In Vitro Study

Highly Cited

Study Snapshot

Acetylcholine mustard labels the binding site aspartate in muscarinic acetylcholine receptors, indicating that Asp-105 (m1 sequence) is the site of label attachment.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Acetylcholine mustard labels the binding site aspartate in muscarinic acetylcholine receptors.

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References

Citations

Novel Irreversible Agonists Acting at the A1 Adenosine Receptor.

Novel irreversible agonists acting at the A1 adenosine receptor have been discovered, offering potential research tools for studying receptor structure and function.

The importance of muscarinic receptors in domestic animal diseases and therapy: Current and future perspectives.

Muscarinic receptors play a crucial role in domestic animal diseases and therapy, offering potential targets for treating equine recurrent airway obstruction, glaucoma, and gastrointestinal disturbances.

Classical and atypical agonists activate M1 muscarinic acetylcholine receptors through common mechanisms.

Both classical and atypical agonists activate M1 muscarinic receptors through common mechanisms, with the main difference in their interaction with D105 in the orthosteric binding site.

Covalent molecular probes for class A G protein-coupled receptors: advances and applications.

Covalent molecular probes for class A GPCRs can aid in understanding their structure and function, aiding in the development of novel therapeutics.

Molecular Mechanisms of Bitopic Ligand Engagement with the M1 Muscarinic Acetylcholine Receptor*

Bitopic ligands, such as TBPB and 77-LH-28-1, gain their selectivity by interacting with both orthosteric and allosteric receptor sites, with ECL2 playing a key role in binding and signaling.