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Article

Heteromultimerization modulates P2X receptor functions through participating extracellular and C-terminal subdomains.

The Journal of biological chemistry - 6 Dec 2002

Koshimizu Taka-aki, Ueno Susumu, Tanoue Akito, Yanagihara Nobuyuki, Stojilkovic Stanko S, Tsujimoto Gozoh

Abstract excerpt

P2X purinergic receptors (P2XRs) differ among themselves with respect to their ligand preferences and channel kinetics during activation, desensitization, and recovery. However, the contributions of distinct receptor subdomains to the subtype-specific behavior have been incompletely characterized. Here we show that homomeric receptors having the extracellular domain of the P2X(3) subunit in the P2X(2a)-based...

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PMID: 12361958
DOI: 10.1074/jbc.M205274200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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