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

A new mode of regulation of N-type inactivation in a Caenorhabditis elegans voltage-gated potassium channel.

The Journal of biological chemistry - 22 Jun 2007

Cai Shi-Qing, Sesti Federico

Abstract excerpt

N-type inactivation in voltage-gated K+ (Kv) channels is a widespread means to modulate neuronal excitability and signaling. Here we have shown a novel mechanism of N-type inactivation in a Caenorhabditis elegans Kv channel. The N-terminal sequence of KVS-1 contains a domain of 22 amino acids that resembles the inactivation ball in A-type channels, which is preceded by a domain of eighteen amino acids. Wild type...

Read the complete abstract on PubMed

Topics

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

Share to Caenorhabditis elegans
Share to Caenorhabditis elegans Proteins

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

Share to CHO Cells

Share to Cricetinae

Share to Cricetulus

Share to Potassium Channels, Voltage-Gated

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 17488718
DOI: 10.1074/jbc.M702079200

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

A new mode of regulation of N-type inactivation in a Caenorhabditis elegans voltage-gated potassium channel.PMID 17488718Read ↗

Inactivation gating of Kv7.1 channels does not involve concerted cooperative subunit interactions.Semantic proximity Read ↗

NIP domain prevents N-type inactivation in voltage-gated potassium channels.Semantic proximity Read ↗

Modulation of K+ current by frequency and external [K+]: a tale of two inactivation mechanisms.Semantic proximity Read ↗

Domain IV voltage-sensor movement is both sufficient and rate limiting for fast inactivation in sodium channels.Semantic proximity Read ↗

Unmasking subtype-dependent susceptibility to C-type inactivation in mammalian Kv1 channels.Semantic proximity Read ↗

A different mechanism of C-type inactivation in the Kv-like KcsA mutant E71VSemantic proximity Read ↗

Mechanisms of sodium channel inactivation.Semantic proximity Read ↗

A sodium channel mutant removes fast inactivation with the inactivation particle bound.Semantic proximity Read ↗

Role of outer-pore residue Y380 in U-type inactivation of KV2.1 channels.Semantic proximity Read ↗

Effect of inserting charged peptide at NH(2)-terminal on N-type inactivation of Kv1.4 channel.Semantic proximity Read ↗

Closed state-coupled C-type inactivation in BK channels.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.