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Article

Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63.

The Journal of biological chemistry - 18 Oct 2002

Ikeda Masahiro, Beitz Eric, Kozono David, Guggino William B, Agre Peter, Yasui Masato

Abstract excerpt

Aquaporins (AQP) were originally regarded as plasma membrane channels that are freely permeated by water or small uncharged solutes but not by ions. Unlike other aquaporins, AQP6 overexpressed in Xenopus laevis oocytes was previously found to exhibit Hg2+ or pH-activated ion conductance. AQP6 could not be analyzed electrophysiologically in mammalian cells, however, because the protein is restricted to...

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Source

Identifiers

PMID: 12177001
DOI: 10.1074/jbc.M207008200

Genes

AQP6

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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