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 residue in the intracellular vestibule of the pore is critical for gating and permeation in Ca2+-activated K+ (BKCa) channels.

The Journal of physiology - 15 Nov 2000

Lippiat J D, Standen N B, Davies N W

Abstract excerpt

1. We have used patch clamp to record large-conductance Ca2+-activated K+ (BKCa) currents from a human embryonic kidney cell line (HEK293) expressing wild-type and mutant hSlo channels. 2. When we mutated F380 in the S6 region, thought to contribute to the intracellular vestibule of the pore, to isoleucine (F380I), very little channel activity was recorded. In contrast, mutation to tyrosine (F380Y) resulted in...

Read the complete abstract on PubMed

Topics

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

Share to Ion Channel Gating
Share to Large-Conductance Calcium-Activated Potassium Channels

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Potentials

Share to Potassium Channel Blockers

Share to Potassium Channels

Share to Potassium Channels, Calcium-Activated

Share to Scorpion Venoms

Share to Toxins, Biological

Source

Open in PubMed Open full text

Identifiers

PMID: 11080257
DOI: 10.1111/j.1469-7793.2000.00131.x
PMCID: PMC2270189

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A residue in the intracellular vestibule of the pore is critical for gating and permeation in Ca2+-activated K+ (BKCa) channels.PMID 11080257Read ↗

Intrinsic electrostatic potential in the BK channel pore: role in determining single channel conductance and block.Semantic proximity Read ↗

BK channel opening involves side-chain reorientation of multiple deep-pore residues.Semantic proximity Read ↗

Characterizing the role of Thr352 in the inhibition of the large conductance Ca2+-activated K+ channels by 1-[1-hexyl-6-(methyloxy)-1H-indazol-3-yl]-2-methyl-1-propanone.Semantic proximity Read ↗

Modulation of the conductance-voltage relationship of the BK(Ca) channel by shortening the cytosolic loop connecting two RCK domains.Semantic proximity Read ↗

Regulation of K+ flow by a ring of negative charges in the outer pore of BKCa channels. Part I: Aspartate 292 modulates K+ conduction by external surface charge effect.Semantic proximity Read ↗

A role for the S0 transmembrane segment in voltage-dependent gating of BK channels.Semantic proximity Read ↗

Localization of divalent cation-binding site in the pore of a small conductance Ca(2+)-activated K(+) channel and its role in determining current-voltage relationship.Semantic proximity Read ↗

RNA editing in eag potassium channels: biophysical consequences of editing a conserved S6 residue.Semantic proximity Read ↗

A side chain in S6 influences both open-state stability and ion permeation in a voltage-gated K+ channel.Semantic proximity Read ↗

Mutational analysis of ion conduction and drug binding sites in the inner mouth of voltage-gated K+ channels.Semantic proximity Read ↗

A residue at the cytoplasmic entrance of BK-type channels regulating single-channel opening by its hydrophobicity.Semantic proximity Read ↗

Gating of shaker-type channels requires the flexibility of S6 caused by prolines.Semantic proximity Read ↗

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