Log in to save to my catalogue

Identification of P2X(4) receptor transmembrane residues contributing to channel gating and interact...

Identification of P2X(4) receptor transmembrane residues contributing to channel gating and interact...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_18427835

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

About this item

Full title

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

Publisher

Germany

Journal title

Pflügers Archiv, 2008-08, Vol.456 (5), p.939

Language

English

Formats

Publication information

Publisher

Germany

More information

Scope and Contents

Contents

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 interactio...

Alternative Titles

Full title

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmed_primary_18427835

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_18427835

Other Identifiers

ISSN

0031-6768

DOI

10.1007/s00424-008-0450-4

How to access this item