Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains.

The Journal of general physiology - 1 Sept 2000

Csanády L, Chan K W, Seto-Young D, Kopsco D C, Nairn A C, Gadsby D C

Abstract excerpt

Opening and closing of a CFTR Cl(-) channel is controlled by PKA-mediated phosphorylation of its cytoplasmic regulatory (R) domain and by ATP binding, and likely hydrolysis, at its two nucleotide binding domains. Functional interactions between the R domain and the two nucleotide binding domains were probed by characterizing the gating of severed CFTR channels expressed in Xenopus oocytes. Expression levels were...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Cyclic AMP-Dependent Protein Kinases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cystic Fibrosis

Share to Cystic Fibrosis Transmembrane Conductance Regulator

Share to In Vitro Techniques

Share to Ion Channel Gating

Share to Oocytes

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 10962022
DOI: 10.1085/jgp.116.3.477
PMCID: PMC2233695

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains.PMID 10962022Read ↗

Electrophysiological, biochemical, and bioinformatic methods for studying CFTR channel gating and its regulation.Semantic proximity Read ↗

A cluster of inhibitory residues in the regulatory domain prevents activation of the cystic fibrosis transmembrane conductance regulator.Semantic proximity Read ↗

A Conserved Region of the R Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is Important in Processing and FunctionSemantic proximity Read ↗

Dibasic phosphorylation sites in the R domain of CFTR have stimulatory and inhibitory effects on channel activation.Semantic proximity Read ↗

Physiological and pharmacological characterization of the N1303K mutant CFTR.Semantic proximity Read ↗

The gating of the CFTR channel.Semantic proximity Read ↗

Quantitative analysis of ATP-dependent gating of CFTR.Semantic proximity Read ↗

The most common cystic fibrosis‐associated mutation destabilizes the dimeric state of the nucleotide‐binding domains of CFTRSemantic proximity Read ↗

The non-hydrolytic pathway of cystic fibrosis transmembrane conductance regulator ion channel gating.Semantic proximity Read ↗

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

Thermally unstable gating of the most common cystic fibrosis mutant channel (ΔF508): "rescue" by suppressor mutations in nucleotide binding domain 1 and by constitutive mutations in the cytosolic loops.Semantic proximity Read ↗

The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.