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

Measurement of the movement of the S4 segment during the activation of a voltage-gated potassium channel.

Pflugers Archiv : European journal of physiology - 1 Jan 2000

Yusaf S P, Wray D, Sivaprasadarao A

Abstract excerpt

Voltage-gated ion channels contain a positively charged transmembrane segment termed S4. Recent evidence suggests that depolarisation of the membrane potential causes this segment to undergo conformational changes that, in turn, lead to the opening of the channel pore. In order to define these conformational changes in structural terms, we have introduced single cysteine substitutions into the S4 segment of the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Electrophysiology
Share to Ion Channel Gating

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

Share to Molecular Sequence Data

Share to Mutation

Share to Oocytes

Share to Patch-Clamp Techniques

Share to Potassium Channels

Source

Identifiers

PMID: 9019737
DOI: 10.1007/s004240050253

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

Measurement of the movement of the S4 segment during the activation of a voltage-gated potassium channel.PMID 9019737Read ↗

Transmembrane movement of the shaker K+ channel S4.Semantic proximity Read ↗

Role of hydrophobic and ionic forces in the movement of S4 of the Shaker potassium channel.Semantic proximity Read ↗

Atomic proximity between S4 segment and pore domain in Shaker potassium channels.Semantic proximity Read ↗

Gated access to the pore of a voltage-dependent K+ channel.Semantic proximity Read ↗

S4 mutations alter the single-channel gating kinetics of Shaker K+ channels.Semantic proximity Read ↗

Hydrophobic substitution mutations in the S4 sequence alter voltage-dependent gating in Shaker K+ channels.Semantic proximity Read ↗

The orientation and molecular movement of a k(+) channel voltage-sensing domain.Semantic proximity Read ↗

Molecular movement of the voltage sensor in a K channel.Semantic proximity Read ↗

Voltage-insensitive gating after charge-neutralizing mutations in the S4 segment of Shaker channels.Semantic proximity Read ↗

S1 constrains S4 in the voltage sensor domain of Kv7.1 K+ channels.Semantic proximity Read ↗

A highly conserved alanine in the S6 domain of the hERG1 K+ channel is required for normal gating.Semantic proximity Read ↗

Investigating the putative glycine hinge in Shaker potassium channel.Semantic proximity Read ↗

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