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

TASK-5, a new member of the tandem-pore K(+) channel family.

Biochemical and biophysical research communications - 22 Jun 2001

Kim D, Gnatenco C

Abstract excerpt

TASKs are members of the recently identified K(+) channel family (KCNKx). Four TASKs (TASK1-4) identified so far form functional K(+) channels and encode background K(+) channels in various cell types. Recently, another member (TASK-5) was identified in the human genome. We cloned it and studied its tissue expression and functional properties. TASK-5 shares 51% amino acid identity with TASK-1 and TASK-3. Northern...

Read the complete abstract on PubMed

Topics

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

Share to Chlorocebus aethiops
Share to Chromosomes, Human, Pair 20
Share to COS Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Multigene Family

Share to Patch-Clamp Techniques

Share to Potassium Channels

Share to Potassium Channels, Tandem Pore Domain

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 11409881
DOI: 10.1006/bbrc.2001.5064

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

TASK-5, a new member of the tandem-pore K(+) channel family.PMID 11409881Read ↗

Heteromerization of alkaline-sensitive two-pore domain potassium channelsSemantic proximity Read ↗

Cloning, localisation and functional expression of a novel human, cerebellum specific, two pore domain potassium channel.Semantic proximity Read ↗

Interaction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3.Semantic proximity Read ↗

KCNQ potassium channels: physiology, pathophysiology, and pharmacology.Semantic proximity Read ↗

Defective X-gating caused by<i>de novo</i>gain-of-function mutations in<i>KCNK3</i>underlies a developmental disorder with sleep apneaSemantic proximity Read ↗

Cloning of a New Mouse Two-P Domain Channel Subunit and a Human Homologue with a Unique Pore StructureSemantic proximity Read ↗

Equivalent Gain-of-Function Variants in <i>KCNK3</i> and <i>KCNK9</i> and their Contribution to Distinct TASK K2P ChannelopathiesSemantic proximity Read ↗

Gain-of-function mutations in KCNK3 cause a developmental disorder with sleep apnea.Semantic proximity Read ↗

Structures of TASK-1 and TASK-3 K2P channels provide insight into their gating and dysfunction in diseaseSemantic proximity Read ↗

Dominant-Negative Effect of a Missense Variant in the TASK-2 (KCNK5) K+ Channel Associated with Balkan Endemic NephropathySemantic proximity Read ↗

Genetic and functional linkage of Kir5.1 and Kir2.1 channel subunitsSemantic proximity Read ↗

WNKs: protein kinases with a unique kinase domain.Semantic proximity Read ↗

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