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Article

Functional differences in pore properties between wild-type and cysteine-less forms of the CFTR chloride channel.

The Journal of membrane biology - 1 Oct 2011

Holstead Ryan G, Li Man-Song, Linsdell Paul

Abstract excerpt

Studies of the structure and function of the cystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channel have been advanced by the development of functional channel variants in which all 18 endogenous cysteine residues have been mutated ("cys-less" CFTR). However, cys-less CFTR has a slightly higher single-channel conductance than wild-type CFTR, raising questions as to the suitability of cys-less as...

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Source

Identifiers

PMID: 21796426
DOI: 10.1007/s00232-011-9388-0

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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Functional differences in pore properties between wild-type and cysteine-less forms of the CFTR chloride channel.PMID 21796426Read ↗

Using a cysteine-less mutant to provide insight into the structure and mechanism of CFTR.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 ↗

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

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 ↗

Mutations in CFTR associated with mild-disease-form Cl- channels with altered pore properties.Semantic proximity Read ↗

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

Multiple mutations in highly conserved residues are found in mildly affected cystic fibrosis patients.Semantic proximity Read ↗

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

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

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

Variable reactivity of an engineered cysteine at position 338 in cystic fibrosis transmembrane conductance regulator reflects different chemical states of the thiol.Semantic proximity Read ↗

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