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

Divalent cations slow activation of EAG family K+ channels through direct binding to S4.

Biophysical journal - 8 Jul 2009

Zhang Xiaofei, Bursulaya Badry, Lee Christian C, Chen Bihan, Pivaroff Kendra, Jegla Timothy

Abstract excerpt

Voltage-gated K+ channels share a common voltage sensor domain (VSD) consisting of four transmembrane helices, including a highly mobile S4 helix that contains the major gating charges. Activation of ether-a-go-go (EAG) family K+ channels is sensitive to external divalent cations. We show here that divalent cations slow the activation rate of two EAG family channels (Kv12.1 and Kv10.2) by forming a bridge between...

Read the complete abstract on PubMed

Topics

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

Share to Xenopus
Share to Cadmium
Share to Cations, Divalent

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

Share to Ether-A-Go-Go Potassium Channels

Share to Magnesium

Share to Membrane Potentials

Share to Nickel

Source

Open in PubMed Open full text

Identifiers

PMID: 19580749
DOI: 10.1016/j.bpj.2009.04.032
PMCID: PMC2711382

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

Divalent cations slow activation of EAG family K+ channels through direct binding to S4.PMID 19580749Read ↗

Role of hydrophobic and ionic forces in the movement of S4 of the Shaker potassium channel.Semantic proximity Read ↗

Reciprocal voltage sensor-to-pore coupling leads to potassium channel C-type inactivation.Semantic proximity Read ↗

The conserved phenylalanine in the K+ channel voltage-sensor domain creates a barrier with unidirectional effects.Semantic proximity Read ↗

Block by internal Mg2+ causes voltage-dependent inactivation of Kv1.5.Semantic proximity Read ↗

Functional interactions of voltage sensor charges with an S2 hydrophobic plug in hERG channels.Semantic proximity Read ↗

Molecular mapping of a site for Cd2+-induced modification of human ether-à-go-go-related gene (hERG) channel activation.Semantic proximity Read ↗

Movements near the gate of a hyperpolarization-activated cation channel.Semantic proximity Read ↗

Tracking a complete voltage-sensor cycle with metal-ion bridges.Semantic proximity Read ↗

External protons destabilize the activated voltage sensor in hERG channels.Semantic proximity Read ↗

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

A novel mechanism for fine-tuning open-state stability in a voltage-gated potassium channel.Semantic proximity Read ↗

The voltage-sensing domain of a hERG1 mutant is a cation-selective channel.Semantic proximity Read ↗

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