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

Intracellular zinc protects Kv7 K+ channels from Ca2+/calmodulin-mediated inhibition.

The Journal of biological chemistry - 1 Feb 2023

Yang Xinhe, Chen Shuai, Zhang Shuo, Shi Sai, Zong Rui, Gao Yiting, Guan Bingcai, Gamper Nikita, Gao Haixia

Abstract excerpt

Zinc (Zn) is an essential trace element; it serves as a cofactor for a great number of enzymes, transcription factors, receptors, and other proteins. Zinc is also an important signaling molecule, which can be released from intracellular stores into the cytosol or extracellular space, for example, during synaptic transmission. Amongst cellular effects of zinc is activation of Kv7 (KCNQ, M-type) voltage-gated...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Calcium Signaling

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

Share to Calmodulin

Share to Intracellular Space

Share to KCNQ Potassium Channels

Share to KCNQ2 Potassium Channel

Share to KCNQ3 Potassium Channel

Source

Open in PubMed Open full text

Identifiers

PMID: 36549648
DOI: 10.1016/j.jbc.2022.102819
PMCID: PMC9852549

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

Intracellular zinc protects Kv7 K+ channels from Ca2+/calmodulin-mediated inhibition.PMID 36549648Read ↗

Activity Dependent Inhibition of AMPA Receptors by Zn2.Semantic proximity Read ↗

Subunit-dependent high-affinity zinc inhibition of acid-sensing ion channels.Semantic proximity Read ↗

Upregulation of KCC2 activity by zinc-mediated neurotransmission via the mZnR/GPR39 receptor.Semantic proximity Read ↗

Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor.Semantic proximity Read ↗

Structure of a Ca(2+)/CaM:Kv7.4 (KCNQ4) B-helix complex provides insight into M current modulation.Semantic proximity Read ↗

Control of voltage-independent zinc inhibition of NMDA receptors by the NR1 subunit.Semantic proximity Read ↗

Zinc alleviates pain through high-affinity binding to the NMDA receptor NR2A subunit.Semantic proximity Read ↗

Unliganded human mutant alpha 7 nicotinic receptors are modulated by Ca2+ and trace levels of Zn2+.Semantic proximity Read ↗

Mechanisms of Calmodulin Regulation of Different Isoforms of Kv7.4 K+ Channels.Semantic proximity Read ↗

Lack of negatively charged residues at the external mouth of Kir2.2 channels enable the voltage-dependent block by external Mg2+.Semantic proximity Read ↗

Probing the molecular basis for signal transduction through the Zinc-Activated Channel (ZAC).Semantic proximity Read ↗

Modulators of voltage-dependent calcium channels for the treatment of nervous system diseases.Semantic proximity Read ↗

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