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

Effect of K+ and Rb+ on the action of verapamil on a voltage-gated K+ channel, hKv1.3: implications for a second open state?

British journal of pharmacology - 1 Jul 2009

Kuras Z, Grissmer S

Abstract excerpt

BACKGROUND AND PURPOSE: Verapamil blocks current through the voltage-gated K(+) channel K(v)1.3 in the open and inactivated state of the channel but not the closed state. The binding site for verapamil was proposed to be close to the selectivity filter and the occupancy of the selectivity filter might therefore influence verapamil affinity. EXPERIMENTAL APPROACH: We investigated the influence of intra- and...

Read the complete abstract on PubMed

Topics

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

Share to Chlorocebus aethiops
Share to COS Cells
Share to Ion Channel Gating

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Potentials

Share to Patch-Clamp Techniques

Share to Potassium

Share to Potassium Channel Blockers

Share to Verapamil

Source

Open in PubMed Open full text

Identifiers

PMID: 19371328
DOI: 10.1111/j.1476-5381.2009.00202.x
PMCID: PMC2721261

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of K+ and Rb+ on the action of verapamil on a voltage-gated K+ channel, hKv1.3: implications for a second open state?PMID 19371328Read ↗

The effect of deep pore mutations on the action of phenylalkylamines on the Kv1.3 potassium channel.Semantic proximity Read ↗

Effect of verapamil on the action of methanethiosulfonate reagents on human voltage-gated K(v)1.3 channels: implications for the C-type inactivated state.Semantic proximity Read ↗

Investigation of the phenylalkylamine binding site in hKv1.3 (H399T), a mutant with a reduced C-type inactivated state.Semantic proximity Read ↗

Mechanisms of Activation of Voltage-Gated Potassium ChannelsSemantic proximity Read ↗

Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel.Semantic proximity Read ↗

Mechanism of verapamil action on wild-type and slow-channel mutant human muscle acetylcholine receptor.Semantic proximity Read ↗

Mechanism of block and identification of the verapamil binding domain to HERG potassium channels.Semantic proximity Read ↗

The real life of voltage-gated K+ channels: more than model behaviour.Semantic proximity Read ↗

Regulation of mammalian Shaker-related K+ channels: evidence for non-conducting closed and non-conducting inactivated states.Semantic proximity Read ↗

K⁺ channel gating: C-type inactivation is enhanced by calcium or lanthanum outside.Semantic proximity Read ↗

Constitutive inactivation of the hKv1.5 mutant channel, H463G, in K+-free solutions at physiological pH.Semantic proximity Read ↗

Inactivation gating of Kv4 potassium channels: molecular interactions involving the inner vestibule of the pore.Semantic proximity Read ↗

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