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Article

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

The Journal of biological chemistry - 26 Feb 1999

Cotten J F, Welsh M J

Abstract excerpt

Arginine 347 in the sixth transmembrane domain of cystic fibrosis transmembrane conductance regulator (CFTR) is a site of four cystic fibrosis-associated mutations. To better understand the function of Arg-347 and to learn how mutations at this site disrupt channel activity, we mutated Arg-347 to Asp, Cys, Glu, His, Leu, or Lys and examined single-channel function. Every Arg-347 mutation examined, except R347K,...

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Source

Identifiers

PMID: 10026154
DOI: 10.1074/jbc.274.9.5429

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

Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture of CFTR. Evidence for disruption of a salt bridge.PMID 10026154Read ↗

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

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 ↗

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

Two salt bridges differentially contribute to the maintenance of cystic fibrosis transmembrane conductance regulator (CFTR) channel function.Semantic proximity Read ↗

Structural identification of a selectivity filter in CFTRSemantic 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 ↗

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

Evolutionary and functional divergence between the cystic fibrosis transmembrane conductance regulator and related ATP-binding cassette transporters.Semantic proximity Read ↗

Can two wrongs make a right? F508del-CFTR ion channel rescue by second-site mutations in its transmembrane domains.Semantic proximity Read ↗

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

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