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

Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes.

The Journal of physiology - 1 Feb 1999

Sanguinetti M C, Xu Q P

Abstract excerpt

1. The structural basis for the activation gate of voltage-dependent K+ channels is not known, but indirect evidence has implicated the S4-S5 linker, the cytoplasmic region between the fourth and fifth transmembrane domains of the channel subunit. We have studied the effects of mutations in the S4-S5 linker of HERG (human ether-á-go-go-related gene), a human delayed rectifier K+ channel, in Xenopus oocytes. 2....

Read the complete abstract on PubMed

Topics

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

Share to Cytoplasm
Share to DNA-Binding Proteins
Share to Electrophysiology

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

Share to Kinetics

Share to Mutagenesis, Insertional

Share to Mutation

Share to Oocytes

Share to Potassium Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 9882738
DOI: 10.1111/j.1469-7793.1999.667ad.x
PMCID: PMC2269111

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

Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes.PMID 9882738Read ↗

The S4-S5 linker acts as a signal integrator for HERG K+ channel activation and deactivation gating.Semantic proximity Read ↗

Mutations within the S4-S5 linker alter voltage sensor constraints in hERG K+ channels.Semantic proximity Read ↗

Voltage sensor movement in the hERG K+ channel.Semantic proximity Read ↗

Role of the S3-S4 linker in Shaker potassium channel activation.Semantic proximity Read ↗

Modulation of the Shaker K(+) channel gating kinetics by the S3-S4 linker.Semantic proximity Read ↗

The evolutionarily conserved residue A653 plays a key role in HERG channel closing.Semantic proximity Read ↗

The pore domain outer helix contributes to both activation and inactivation of the HERG K+ channel.Semantic proximity Read ↗

Stabilization of the Activated hERG Channel Voltage Sensor by Depolarization Involves the S4-S5 Linker.Semantic proximity Read ↗

Direct interaction of eag domains and cyclic nucleotide-binding homology domains regulate deactivation gating in hERG channels.Semantic proximity Read ↗

Role of transmembrane segment S5 on gating of voltage-dependent K+ channels.Semantic proximity Read ↗

Structural basis of action for a human ether-a-go-go-related gene 1 potassium channel activator.Semantic proximity Read ↗

Long QT syndrome-associated mutations in the Per-Arnt-Sim (PAS) domain of HERG potassium channels accelerate channel deactivation.Semantic proximity Read ↗

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