Mutation of carboxyl-terminal threonine residues in human m3 muscarinic acetylcholine receptor modulates the extent of sequestration and desensitization.

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

Back to search

Article

Mutation of carboxyl-terminal threonine residues in human m3 muscarinic acetylcholine receptor modulates the extent of sequestration and desensitization.

Molecular pharmacology - 1 Sept 1995

Yang J, Williams J A, Yule D I, Logsdon C D

Abstract excerpt

We previously reported that a mutant human m3 muscarinic acetylcholine receptor in which threonine residues at positions 550, 553, and 554 in the carboxyl terminus had been substituted with alanines showed a significant blockage of receptor down-regulation when expressed in Chinese hamster ovary-...

Topics

Carbachol
Cells, Cultured
Down-Regulation
Embryo, Mammalian
Humans
Hydrolysis
Kidney
Mutation
Phosphatidylinositols
Receptors, Muscarinic
Signal Transduction
Threonine
Transfection

Source

Open in PubMed

Identifiers

PMID: 7565628

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7565628-2026-08-30.1. 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.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics