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

Functional properties of a truncated recombinant GIRK5 potassium channel.

Biochimica et biophysica acta - 2 May 2001

Salvador C, Martinez M, Mora S I, Egido W, Farias J M, Gamba G, Escobar L I

Abstract excerpt

Xenopus laevis oocytes codify a G-protein-activated inward rectifier potassium channel (GIRK5 or Kir3.5). Coinjection of other GIRKs, the muscarinic m2 receptor, or Gbetagamma protein cRNAs is required to observe functional GIRKx-GIRK5 heteromultimers in oocytes. Studies with GIRK2 isoforms have shown that the size of the amino or carboxyl terminus plays a crucial role on giving functional K(+) channels. In this...

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, Divalent
Share to Chlorides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to G Protein-Coupled Inwardly-Rectifying Potassium Channels

Share to Potassium Channel Blockers

Share to Potassium Channels

Share to Potassium Channels, Inwardly Rectifying

Share to Static Electricity

Source

Identifiers

PMID: 11334631
DOI: 10.1016/s0005-2736(01)00314-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional properties of a truncated recombinant GIRK5 potassium channel.PMID 11334631Read ↗

A revised mechanism of action of hyperaldosteronism-linked mutations in cytosolic domains of GIRK4 (KCNJ5)Semantic proximity Read ↗

A revised mechanism of action of hyperaldosteronism-linked mutations in cytosolic domains of GIRK4 (KCNJ5).Semantic proximity Read ↗

Overexpression of Monomeric and Multimeric GIRK4 Subunits in Rat Atrial Myocytes Removes Fast Desensitization and Reduces Inward Rectification of Muscarinic K+ Current (IK(ACh))Semantic proximity Read ↗

The inwardly rectifying K(+) channel subunit GIRK1 rescues the GIRK2 weaver phenotype.Semantic proximity Read ↗

The sensitivity of G protein-activated K+ channels toward halothane is essentially determined by the C terminus.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 ↗

A novel ion conducting route besides the central pore in an inherited mutant of G-protein-gated inwardly rectifying K <sup>+</sup> channelSemantic proximity Read ↗

Comparison of cloned Kir2 channels with native inward rectifier K<sup>+</sup> channels from guinea‐pig cardiomyocytesSemantic proximity Read ↗

Cs+ block of the cardiac muscarinic K+ channel, GIRK1/GIRK4, is not dependent on the aspartate residue at position 173.Semantic proximity Read ↗

Cannabinoid receptors can activate and inhibit G protein-coupled inwardly rectifying potassium channels in a xenopus oocyte expression system.Semantic proximity Read ↗

Characterization and molecular basis for the block of Kv1.3 channels induced by carvedilol in HEK293 cells.Semantic proximity Read ↗

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

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