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

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

The journal of physiological sciences : JPS - 1 Sept 2010

Shimizu Hiroyasu, Yu Ying-Chun, Kono Koichi, Kubota Takahiro, Yasui Masato, Li Min, Hwang Tzyh-Chang, Sohma Yoshiro

Abstract excerpt

Cystic fibrosis transmembrane conductance regulator (CFTR) anion channel, a member of ABC transporter superfamily, gates following ATP-dependent conformational changes of the nucleotide binding domains (NBD). Reflecting the hundreds of milliseconds duration of the channel open state corresponding to the dimerization of two NBDs, macroscopic WT-CFTR currents usually showed a fast, single exponential relaxation...

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 ATP-Binding Cassette Transporters

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

Share to CHO Cells

Share to Cricetinae

Share to Cricetulus

Share to Cystic Fibrosis Transmembrane Conductance Regulator

Share to Ion Channel Gating

Share to Protein Multimerization

Source

Open in PubMed Open full text

Identifiers

PMID: 20628841
DOI: 10.1007/s12576-010-0102-2
PMCID: PMC4939245

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

A stable ATP binding to the nucleotide binding domain is important for reliable gating cycle in an ABC transporter CFTR.PMID 20628841Read ↗

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

CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains.Semantic proximity Read ↗

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

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

A Topological Switch in the Cystic Fibrosis Transmembrane Conductance Regulator Modulates Channel Activity and Sensitivity to Disease-Causing MutationSemantic proximity Read ↗

High affinity ATP/ADP analogues as new tools for studying CFTR gating.Semantic proximity Read ↗

Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations.Semantic proximity Read ↗

Estimating the true stability of the prehydrolytic outward-facing state in an ABC proteinSemantic proximity Read ↗

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

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

Estimating the true stability of the prehydrolytic outward-facing state in an ABC protein.Semantic proximity Read ↗

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

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