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Article

Identification of positive charges situated at the outer mouth of the CFTR chloride channel pore.

Pflugers Archiv : European journal of physiology - 1 Nov 2008

Zhou Jing-Jun, Fatehi Mohammad, Linsdell Paul

Abstract excerpt

We have used site-directed mutagenesis and functional analysis to identify positively charged amino acid residues in the cystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channel that interact with extracellular anions. Mutation of two positively charged arginine residues in the first extracellular loop (ECL) of CFTR, R104, and R117, as well as lysine residue K335 in the sixth transmembrane region,...

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Source

Identifiers

PMID: 18449561
DOI: 10.1007/s00424-008-0521-6

Genes

CFTR

Provenance

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.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of positive charges situated at the outer mouth of the CFTR chloride channel pore.PMID 18449561Read ↗

Positive charges at the intracellular mouth of the pore regulate anion conduction in the CFTR chloride channel.Semantic proximity Read ↗

Two positively charged amino acid side-chains in the inner vestibule of the CFTR channel pore play analogous roles in controlling anion binding and anion conductance.Semantic proximity Read ↗

Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride channel pore.Semantic proximity Read ↗

Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture of CFTR. Evidence for disruption of a salt bridge.Semantic proximity Read ↗

Trivalent anions as probes of the CFTR channel pore.Semantic proximity Read ↗

Direct comparison of the functional roles played by different transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore.Semantic proximity Read ↗

Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.Semantic proximity Read ↗

Interactions between permeant and blocking anions inside the CFTR chloride channel pore.Semantic proximity Read ↗

Role of Hydrophobic Amino-Acid Side-Chains in the Narrow Selectivity Filter of the CFTR Chloride Channel Pore in Conductance and Selectivity.Semantic proximity Read ↗

Functional organization of cytoplasmic portals controlling access to the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel pore.Semantic proximity Read ↗

Novel pore-lining residues in CFTR that govern permeation and open-channel block.Semantic proximity Read ↗

Structural identification of a selectivity filter in CFTRSemantic proximity Read ↗

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