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 voltage-dependent ClC-2 chloride channel has a dual gating mechanism.

The Journal of physiology - 16 Mar 2004

Zúñiga Leandro, Niemeyer María Isabel, Varela Diego, Catalán Marcelo, Cid L Pablo, Sepúlveda Francisco V

Abstract excerpt

Functional and structural studies demonstrate that Cl(-) channels of the ClC family have a dimeric double-barrelled structure, with each monomer contributing an identical pore. Single protopore gating is a fast process dependent on Cl(-) interaction within the selectivity filter and in ClC-0 has a low temperature coefficient over a 10 degrees C range (Q(10)). A slow gating process closes both protopores...

Read the complete abstract on PubMed

Topics

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

Share to Mutation
Share to Rats
Share to Cadmium

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

Share to Cell Line

Share to Chloride Channels

Share to Electrophysiology

Share to Ion Channel Gating

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 14724195
DOI: 10.1113/jphysiol.2003.060046
PMCID: PMC1664870

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 voltage-dependent ClC-2 chloride channel has a dual gating mechanism.PMID 14724195Read ↗

Removal of gating in voltage-dependent ClC-2 chloride channel by point mutations affecting the pore and C-terminus CBS-2 domain.Semantic proximity Read ↗

Modulation of the slow/common gating of CLC channels by intracellular cadmium.Semantic proximity Read ↗

Chloride dependence of hyperpolarization-activated chloride channel gates.Semantic proximity Read ↗

Voltage-dependent and -independent titration of specific residues accounts for complex gating of a ClC chloride channel by extracellular protons.Semantic proximity Read ↗

Temperature dependence of fast and slow gating relaxations of ClC-0 chloride channels.Semantic proximity Read ↗

Proton sensing of CLC-0 mutant E166D.Semantic proximity Read ↗

CryoEM structures of the human CLC-2 voltage gated chloride channel reveal a ball and chain gating mechanismSemantic proximity Read ↗

Electro-steric opening of the CLC-2 chloride channel gate.Semantic proximity Read ↗

Structure and function of ClC chloride channels.Semantic proximity Read ↗

CLC Chloride Channels and Transporters: Structure, Function, Physiology, and Disease.Semantic proximity Read ↗

Two physically distinct pores in the dimeric ClC-0 chloride channel.Semantic proximity Read ↗

Dynamical model of the CLC-2 ion channel reveals conformational changes associated with selectivity-filter gating.Semantic proximity Read ↗

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