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

Differential polyamine sensitivity in inwardly rectifying Kir2 potassium channels.

The Journal of physiology - 1 Mar 2006

Panama Brian K, Lopatin Anatoli N

Abstract excerpt

Recent studies have shown that Kir2 channels display differential sensitivity to intracellular polyamines, and have raised a number of questions about several properties of inward rectification important to the understanding of their physiological roles. In this study, we have carried out a detailed characterization of steady-state and kinetic properties of block of Kir2.1-3 channels by spermine. High-resolution...

Read the complete abstract on PubMed

Topics

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

Share to Dose-Response Relationship, Drug
Share to Membrane Potentials
Share to Polyamines

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, Secondary

Share to Sequence Homology

Share to Spermine

Source

Open in PubMed Open full text

Identifiers

PMID: 16373386
DOI: 10.1113/jphysiol.2005.097741
PMCID: PMC1796793

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

Differential polyamine sensitivity in inwardly rectifying Kir2 potassium channels.PMID 16373386Read ↗

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

Inward rectification in KATP channels: a pH switch in the pore.Semantic proximity Read ↗

Control of rectification and permeation by two distinct sites after the second transmembrane region in Kir2.1 K+ channel.Semantic proximity Read ↗

Na(+)-induced inward rectification in the two-pore domain K(+) channel, TASK-2.Semantic proximity Read ↗

Inward rectification by polyamines in mouse Kir2.1 channels: synergy between blocking components.Semantic proximity Read ↗

Inward rectification and implications for cardiac excitability.Semantic proximity Read ↗

Voltage-dependent gating and block by internal spermine of the murine inwardly rectifying K+ channel, Kir2.1.Semantic proximity Read ↗

Interaction mechanisms between polyamines and IRK1 inward rectifier K+ channels.Semantic proximity Read ↗

Voltage-dependent inhibition of outward Kir2.1 currents by extracellular spermine.Semantic proximity Read ↗

Novel gating mechanism of polyamine block in the strong inward rectifier K channel Kir2.1.Semantic proximity Read ↗

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

Intracellular pH regulates the strength of the intrinsic inward rectification of Kir4.1/Kir5.1 channels.Semantic proximity Read ↗

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