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

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

The Journal of biological chemistry - 27 Jan 1995

Carson M R, Travis S M, Welsh M J

Abstract excerpt

The cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel contains two cytoplasmic nucleotide-binding domains (NBDs). After phosphorylation of the R domain, ATP interacts with the NBDs to regulate channel activity. To learn how the NBDs regulate channel function, we used the patch-clamp technique to study CFTR and variants which contained site-directed mutations in the conserved Walker A motif...

Read the complete abstract on PubMed

Topics

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

Share to 3T3 Cells
Share to Adenosine Triphosphate

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

Share to Amino Acid Sequence

Share to Binding Sites

Share to Conserved Sequence

Share to Genetic Variation

Share to HeLa Cells

Share to Membrane Proteins

Source

Identifiers

PMID: 7530246
DOI: 10.1074/jbc.270.4.1711

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

The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity.PMID 7530246Read ↗

On the mechanism of MgATP-dependent gating of CFTR Cl- channels.Semantic proximity Read ↗

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

Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains.Semantic proximity Read ↗

Cysteine residues in the nucleotide binding domains regulate the conductance state of CFTR channels.Semantic proximity Read ↗

The cystic fibrosis transmembrane conductance regulator is an extracellular chloride sensor.Semantic proximity Read ↗

The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics.Semantic proximity Read ↗

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

G551D and G1349D, Two CF-associated Mutations in the Signature Sequences of CFTR, Exhibit Distinct Gating DefectsSemantic proximity Read ↗

Dibasic protein kinase A sites regulate bursting rate and nucleotide sensitivity of the cystic fibrosis transmembrane conductance regulator chloride channel.Semantic proximity Read ↗

Differential sensitivity of the cystic fibrosis (CF)-associated mutants G551D and G1349D to potentiators of the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel.Semantic proximity Read ↗

A stable ATP binding to the nucleotide binding domain is important for reliable gating cycle in an ABC transporter CFTR.Semantic proximity Read ↗

Mechanism of dysfunction of two nucleotide binding domain mutations in cystic fibrosis transmembrane conductance regulator that are associated with pancreatic sufficiency.Semantic proximity Read ↗

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