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

Inactivation determinant in the I-II loop of the Ca2+ channel alpha1-subunit and beta-subunit interaction affect sensitivity for the phenylalkylamine (-)gallopamil.

The Journal of physiology - 1 Sept 1999

Sokolov S, Weiss R G, Kurka B, Gapp F, Hering S

Abstract excerpt

1. The role of calcium (Ca2+) channel inactivation in the molecular mechanism of channel block by phenylalkylamines (PAAs) was analysed in a PAA-sensitive rabbit brain class A Ca2+ channel mutant (alpha1A-PAA). Use-dependent barium current (IBa) inhibition of alpha1A-PAA by (-)gallopamil and Ca2+ channel recovery from inactivation and block were studied with two-microlectrode voltage clamp after expression of...

Read the complete abstract on PubMed

Topics

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

Share to Algorithms
Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Calcium Channel Blockers

Share to Calcium Channels

Share to Calcium Channels, L-Type

Share to Electrophysiology

Share to Rabbits

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 10457051
DOI: 10.1111/j.1469-7793.1999.0315m.x
PMCID: PMC2269510

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

Inactivation determinant in the I-II loop of the Ca2+ channel alpha1-subunit and beta-subunit interaction affect sensitivity for the phenylalkylamine (-)gallopamil.PMID 10457051Read ↗

Voltage-dependent acceleration of Ca(v)1.2 channel current decay by (+)- and (-)-isradipine.Semantic proximity Read ↗

Opposite effects of a single IIIS5 mutation on phenylalkylamine and dihydropyridine interaction with L-type Ca2+ channels.Semantic proximity Read ↗

Distinct effects of mutations in transmembrane segment IVS6 on block of L-type calcium channels by structurally similar phenylalkylamines.Semantic proximity Read ↗

Molecular determinants of voltage-dependent slow inactivation of the Ca2+ channel.Semantic proximity Read ↗

Isradipine interacts with the open state of the L-type calcium channel at high concentrations.Semantic proximity Read ↗

Molecular determinants of frequency dependence and Ca2+ potentiation of verapamil block in the pore region of Cav1.2.Semantic proximity Read ↗

Mutations Leu427, Asn428, and Leu431 residues within transmembrane domain-I-segment 6 attenuate ginsenoside-mediated L-type Ca(2+) channel current inhibitions.Semantic proximity Read ↗

Molecular determinants of inactivation in voltage-gated Ca2+ channels.Semantic proximity Read ↗

Modulation of slow inactivation in class A Ca2+ channels by beta-subunits.Semantic proximity Read ↗

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

Flecainide sensitivity of a Na channel long QT mutation shows an open-channel blocking mechanism for use-dependent block.Semantic proximity Read ↗

Structural basis for inhibition of a voltage-gated Ca2+ channel by Ca2+ antagonist drugs.Semantic proximity Read ↗

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