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

K+ binding in the G-loop and water cavity facilitates Ba2+ movement in the Kir2.1 channel.

Biochimica et biophysica acta - 1 Feb 2009

Chang Hsueh-Kai, Marton Laurence J, Liang Kuo Kan, Shieh Ru-Chi

Abstract excerpt

K+ are selectively coordinated in the selectivity filter and concerted K+ and water movements in this region ensure high conduction rates in K+ channels. In channels with long pores many K+ binding sites are located intracellular to the selectivity filter (inner vestibule), but their contribution to permeation has not been well studied. We investigated this phenomenon by slowing the ion permeation process via...

Read the complete abstract on PubMed

Topics

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

Share to Barium
Share to Cations
Share to Electrophysiological Phenomena

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

Share to Potassium

Share to Potassium Channels, Inwardly Rectifying

Share to Protein Structure, Quaternary

Share to Structural Homology, Protein

Share to Xenopus laevis

Source

Identifiers

PMID: 19026608
DOI: 10.1016/j.bbamem.2008.10.016

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

K+ binding in the G-loop and water cavity facilitates Ba2+ movement in the Kir2.1 channel.PMID 19026608Read ↗

Ionic interactions of Ba2+ blockades in the MthK K+ channel.Semantic proximity Read ↗

From Selective Permeation to Physiology in Potassium Channels.Semantic proximity Read ↗

Mutation in pore-helix modulates interplay between filter gate and Ba2+ block in a Kcv channel pore.Semantic proximity Read ↗

Mechanism for attenuated outward conductance induced by mutations in the cytoplasmic pore of Kir2.1 channels.Semantic proximity Read ↗

Identification of a site involved in the block by extracellular Mg(2+) and Ba(2+) as well as permeation of K(+) in the Kir2.1 K(+) channel.Semantic proximity Read ↗

Base of pore loop is important for rectification, activation, permeation, and block of Kir3.1/Kir3.4.Semantic proximity Read ↗

Lack of negatively charged residues at the external mouth of Kir2.2 channels enable the voltage-dependent block by external Mg2+.Semantic proximity Read ↗

The role of the cytoplasmic pore in inward rectification of Kir2.1 channels.Semantic proximity Read ↗

Potassium-selective block of barium permeation through single KcsA channels.Semantic proximity Read ↗

Probing ion permeation and gating in a K+ channel with backbone mutations in the selectivity filter.Semantic proximity Read ↗

Mutations in the pore region of ROMK enhance Ba2+ block.Semantic proximity Read ↗

Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites.Semantic proximity Read ↗

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