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

Fast inactivation of Shaker K+ channels is highly temperature dependent.

Experimental brain research - 1 Mar 1997

Nobile M, Olcese R, Toro L, Stefani E

Abstract excerpt

The energy profile of the interaction between the NH2-terminal inactivation domain and the internal mouth of the Shaker H4 K+ channel has been investigated. Macroscopic currents from channels normally inactivating (Shaker H4) and with the inactivation removed (Shaker H4-IR) were recorded at different temperatures using the cut-open oocyte technique. Changes in temperature had a dramatic effect on the inactivation...

Read the complete abstract on PubMed

Topics

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

Share to Xenopus laevis
Share to Drosophila
Share to Homeostasis

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

Share to Mutation

Share to Oocytes

Share to Potassium Channels

Share to Temperature

Share to Time Factors

Source

Identifiers

PMID: 9125459
DOI: 10.1007/pl00005613

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

Fast inactivation of Shaker K+ channels is highly temperature dependent.PMID 9125459Read ↗

A mammalian transient type K+ channel, rat Kv1.4, has two potential domains that could produce rapid inactivation.Semantic proximity Read ↗

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

Gating currents in Shaker K+ channels. Implications for activation and inactivation models.Semantic proximity Read ↗

ShakerIR and Kv1.5 mutant channels with enhanced slow inactivation also exhibit K⁺ o-dependent resting inactivation.Semantic proximity Read ↗

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

Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels.Semantic proximity Read ↗

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

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

Cross talk between activation and slow inactivation gates of Shaker potassium channels.Semantic proximity Read ↗

Regulation of Shaker K+ channel inactivation gating by the cAMP-dependent protein kinase.Semantic proximity Read ↗

Shaker IR T449 mutants separate C- from U-type inactivation.Semantic proximity Read ↗

Closed state-coupled C-type inactivation in BK channels.Semantic proximity Read ↗

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