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

Determinants within the turret and pore-loop domains of KCNQ3 K+ channels governing functional activity.

Biophysical journal - 1 Dec 2008

Zaika Oleg, Hernandez Ciria C, Bal Manjot, Tolstykh Gleb P, Shapiro Mark S

Abstract excerpt

KCNQ1-5 (Kv7.1-7.5) subunits assemble to form a variety of functional K(+) channels in the nervous system, heart, and epithelia. KCNQ1 and KCNQ4 homomers and KCNQ2/3 heteromers yield large currents, whereas KCNQ2 and KCNQ3 homomers yield small currents. Since the unitary conductance of KCNQ3 is five- to 10-fold greater than that of KCNQ4 or KCNQ1, these differences are even more striking. To test for differential...

Read the complete abstract on PubMed

Topics

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

Share to Barium
Share to Biotinylation
Share to Cricetulus

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

Share to Electric Conductivity

Share to KCNQ3 Potassium Channel

Share to Porosity

Share to Potassium Channel Blockers

Share to Protein Stability

Source

Open in PubMed Open full text

Identifiers

PMID: 18790849
DOI: 10.1529/biophysj.108.137604
PMCID: PMC2586577

Genes

KCNQ3
KCNQ1
KCNQ4
KCNQ2

Variants

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

Determinants within the turret and pore-loop domains of KCNQ3 K+ channels governing functional activity.PMID 18790849Read ↗

Pore determinants of KCNQ3 K+ current expression.Semantic proximity Read ↗

Gating and Regulation of KCNQ1 and KCNQ1 + KCNE1 Channel ComplexesSemantic proximity Read ↗

Homomeric and heteromeric assembly of KCNQ (Kv7) K+ channels assayed by total internal reflection fluorescence/fluorescence resonance energy transfer and patch clamp analysis.Semantic proximity Read ↗

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

Pore helix-S6 interactions are critical in governing current amplitudes of KCNQ3 K+ channels.Semantic proximity Read ↗

Molecular cloning and functional expression of KCNQ5, a potassium channel subunit that may contribute to neuronal M-current diversity.Semantic proximity Read ↗

The N-Terminal Juxtamembranous Domain of KCNQ1 Is Critical for Channel Surface ExpressionSemantic proximity Read ↗

The Role of the Carboxyl Terminus Helix C-D Linker in Regulating KCNQ3 K+ Current Amplitudes by Controlling Channel Trafficking.Semantic proximity Read ↗

Identification by mass spectrometry and functional characterization of two phosphorylation sites of KCNQ2/KCNQ3 channels.Semantic proximity Read ↗

KCNE3 acts by promoting voltage sensor activation in KCNQ1.Semantic proximity Read ↗

LQT1 mutations in KCNQ1 C-terminus assembly domain suppress IKs using different mechanisms.Semantic proximity Read ↗

Calmodulin orchestrates the heteromeric assembly and the trafficking of KCNQ2/3 (Kv7.2/3) channels in neurons.Semantic proximity Read ↗

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