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

The S. cerevisiae outwardly-rectifying potassium channel (DUK1) identifies a new family of channels with duplicated pore domains.

Receptors & channels - 1 Jan 1996

Reid J D, Lukas W, Shafaatian R, Bertl A, Scheurmann-Kettner C, Guy H R, North R A

Abstract excerpt

Potassium channel subunits have six or two transmembrane segments in addition to a conserved pore-forming (P) domain; four subunits come together to form a channel. A gene was identified in S. cerevisiae (J0911) encoding a protein with eight probable membrane-spanning segments and two such P regi...

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 Base Sequence
Share to Cloning, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression

Share to Genes, Fungal

Share to Molecular Sequence Data

Share to Mutation

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 8723646

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-8723646-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The S. cerevisiae outwardly-rectifying potassium channel (DUK1) identifies a new family of channels with duplicated pore domains.PMID 8723646Read ↗

Interactive domains between pore loops of the yeast K+ channel TOK1 associate with extracellular K+ sensitivity.Semantic proximity Read ↗

Channeling studies in yeast: yeast as a model for channelopathies?Semantic proximity Read ↗

Mutations in the yeast two pore K+ channel YKC1 identify functional differences between the pore domains.Semantic proximity Read ↗

Functional consequences of leucine and tyrosine mutations in the dual pore motifs of the yeast K(+) channel, Tok1p.Semantic proximity Read ↗

New potassium channel gene families in flies and mammals: from mutants to molecules.Semantic proximity Read ↗

Functional characterization of a second porin isoform in Drosophila melanogaster. DmPorin2 forms voltage-independent cation-selective pores.Semantic proximity Read ↗

yam8(+), a Schizosaccharomyces pombe gene, is a potential homologue of the Saccharomyces cerevisiae MID1 gene encoding a stretch-activated Ca(2+)-permeable channel.Semantic proximity Read ↗

Alternatively spliced domains interact to regulate BK potassium channel gating.Semantic proximity Read ↗

Ionic leakage underlies a gain-of-function effect of dominant disease mutations affecting diverse P-type ATPases.Semantic proximity Read ↗

Functional expression of the pore forming subunit of the ATP-sensitive potassium channel in Saccharomyces cerevisiae.Semantic proximity Read ↗

Potassium channels in Drosophila: historical breakthroughs, significance, and perspectives.Semantic proximity Read ↗

Deletion of six open reading frames from the left arm of chromosome IV of Saccharomyces cerevisiae.Semantic proximity Read ↗

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