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

Localization of the activation gate of a voltage-gated Ca2+ channel.

The Journal of general physiology - 1 Sept 2005

Xie Cheng, Zhen Xiao-Guang, Yang Jian

Abstract excerpt

Ion channels open and close in response to changes in transmembrane voltage or ligand concentration. Recent studies show that K+ channels possess two gates, one at the intracellular end of the pore and the other at the selectivity filter. In this study we determined the location of the activation gate in a voltage-gated Ca2+ channel (VGCC) by examining the open/closed state dependence of the rate of modification...

Read the complete abstract on PubMed

Topics

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

Share to Calcium Channels, N-Type
Share to Intracellular Membranes
Share to Ion Channel Gating

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Potentials

Share to Mesylates

Share to Patch-Clamp Techniques

Share to Sulfhydryl Reagents

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 16129771
DOI: 10.1085/jgp.200509293
PMCID: PMC2266579

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Localization of the activation gate of a voltage-gated Ca2+ channel.PMID 16129771Read ↗

Localization of PIP2 activation gate in inward rectifier K+ channels.Semantic proximity Read ↗

Gated access to the pore of a voltage-dependent K+ channel.Semantic proximity Read ↗

The pore domain outer helix contributes to both activation and inactivation of the HERG K+ channel.Semantic proximity Read ↗

Coupling of Ca <sup>2+</sup> and voltage activation in BK channels through the αB helix/voltage sensor interfaceSemantic proximity Read ↗

Structural determinants of voltage-gating properties in calcium channels.Semantic proximity Read ↗

Upward movement of IS4 and IIIS4 is a rate-limiting stage in Cav1.2 activation.Semantic proximity Read ↗

Conformational switch between slow and fast gating modes: allosteric regulation of voltage sensor mobility in the EAG K+ channel.Semantic proximity Read ↗

Congruent pattern of accessibility identifies minimal pore gate in a non-symmetric voltage-gated sodium channel.Semantic proximity Read ↗

A single amino acid mutation attenuates rundown of voltage-gated calcium channels.Semantic proximity Read ↗

Gating dependence of inner pore access in inward rectifier K(+) channels.Semantic proximity Read ↗

Neutralisation of a single voltage sensor affects gating determinants in all four pore-forming S6 segments of Ca(V)1.2: a cooperative gating model.Semantic proximity Read ↗

A Kv channel with an altered activation gate sequence displays both "fast" and "slow" activation kinetics.Semantic proximity Read ↗

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