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Article

Identification of P2X(4) receptor transmembrane residues contributing to channel gating and interaction with ivermectin.

Pflugers Archiv : European journal of physiology - 1 Aug 2008

Jelínkova Irena, Vávra Vojtech, Jindrichova Marie, Obsil Tomas, Zemkova Hana W, Zemkova Hana, Stojilkovic Stanko S

Abstract excerpt

Ivermectin (IVM), a large macrocyclic lactone, specifically enhances P2X(4) receptor-channel function by interacting with residues of transmembrane (TM) helices in the open conformation state. In this paper, we used cysteine-scanning mutagenesis of rat P2X(4)-TMs to identify and map residues of potential importance for channel gating and interaction with IVM. The receptor function was unchanged by mutations in 29...

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Source

Identifiers

PMID: 18427835
DOI: 10.1007/s00424-008-0450-4

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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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