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

Calmodulin regulation of Nav1.4 current: role of binding to the carboxyl terminus.

The Journal of general physiology - 1 Mar 2008

Biswas Subrata, Deschênes Isabelle, Disilvestre Deborah, Tian Yanli, Halperin Victoria L, Tomaselli Gordon F

Abstract excerpt

Calmodulin (CaM) regulates steady-state inactivation of sodium currents (Na(V)1.4) in skeletal muscle. Defects in Na current inactivation are associated with pathological muscle conditions such as myotonia and paralysis. The mechanisms of CaM modulation of expression and function of the Na channe...

Read the complete abstract on PubMed

Topics

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

Share to Calmodulin
Share to Fluorescence Resonance Energy Transfer
Share to Gene Expression Regulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Muscle Proteins

Share to NAV1.4 Voltage-Gated Sodium Channel

Share to Protein Binding

Share to Protein Conformation

Share to Sodium Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 18270170
DOI: 10.1085/jgp.200709863
PMCID: PMC2248716

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-18270170-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Calmodulin regulation of Nav1.4 current: role of binding to the carboxyl terminus.PMID 18270170Read ↗

Structural basis for the modulation of the neuronal voltage-gated sodium channel NaV1.6 by calmodulin.Semantic proximity Read ↗

Calmodulin limits pathogenic Na+ channel persistent current.Semantic proximity Read ↗

Elementary mechanisms of calmodulin regulation of NaV1.5 producing divergent arrhythmogenic phenotypes.Semantic proximity Read ↗

Calcium-mediated dual-mode regulation of cardiac sodium channel gating.Semantic proximity Read ↗

Ca2+-dependent regulation of sodium channels NaV1.4 and NaV1.5 is controlled by the post-IQ motif.Semantic proximity Read ↗

A Mechanism of Calmodulin Modulation of the Human Cardiac Sodium Channel.Semantic proximity Read ↗

Calmodulin mediates Ca2+ sensitivity of sodium channels.Semantic proximity Read ↗

Structure of a Ca(2+)/CaM:Kv7.4 (KCNQ4) B-helix complex provides insight into M current modulation.Semantic proximity Read ↗

Characterization of the calmodulin-binding site in the N terminus of CaV1.2.Semantic proximity Read ↗

Current view on regulation of voltage-gated sodium channels by calcium and auxiliary proteins.Semantic proximity Read ↗

Calmodulin is the Ca2+ sensor for Ca2+ -dependent inactivation of L-type calcium channels.Semantic proximity Read ↗

The molecular basis of the inhibition of CaV1 calcium-dependent inactivation by the distal carboxy tail.Semantic proximity Read ↗

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