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

An Additional Ca2+ Binding Site Allosterically Controls TMEM16A Activation.

Cell reports - 29 Dec 2020

Le Son C, Yang Huanghe

Abstract excerpt

Calcium (Ca2+) is the primary stimulus for transmembrane protein 16 (TMEM16) Ca2+-activated chloride channels and phospholipid scramblases, which regulate important physiological processes ranging from smooth muscle contraction to blood coagulation and tumor progression. Binding of intracellular Ca2+ to two highly conserved orthosteric binding sites in transmembrane helices (TMs) 6-8 efficiently opens the...

Read the complete abstract on PubMed

Topics

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

Share to Cadmium
Share to Calcium
Share to Chloride Channels

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

Share to Electrophysiology

Share to Ion Channel Gating

Share to Ion Transport

Share to Phospholipid Transfer Proteins

Share to Protein Domains

Source

Open in PubMed Open full text

Identifiers

PMID: 33378669
DOI: 10.1016/j.celrep.2020.108570
PMCID: PMC7786149

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

An Additional Ca2+ Binding Site Allosterically Controls TMEM16A Activation.PMID 33378669Read ↗

A comprehensive search for calcium binding sites critical for TMEM16A calcium-activated chloride channel activity.Semantic proximity Read ↗

Molecular simulation assisted identification of Ca(2+) binding residues in TMEM16A.Semantic proximity Read ↗

Independent activation of ion conduction pores in the double-barreled calcium-activated chloride channel TMEM16A.Semantic proximity Read ↗

Activation of TMEM16F by inner gate charged mutations and possible lipid/ion permeation mechanisms.Semantic proximity Read ↗

Two Ca(2+)-Binding Sites Cooperatively Couple Together in TMEM16A Channel.Semantic proximity Read ↗

Independent activation of distinct pores in dimeric TMEM16A channels.Semantic proximity Read ↗

Divalent Cation Modulation of Ion Permeation in TMEM16 Proteins.Semantic proximity Read ↗

Gating mechanism of the extracellular entry to the lipid pathway in a TMEM16 scramblase.Semantic proximity Read ↗

Gating modes of calcium-activated chloride channels TMEM16A and TMEM16B.Semantic proximity Read ↗

Gating the pore of the calcium-activated chloride channel TMEM16A.Semantic proximity Read ↗

Permeation Mechanisms in the TMEM16B Calcium-Activated Chloride Channels.Semantic proximity Read ↗

Ca2+ Sensitivity of Anoctamin 6/TMEM16F Is Regulated by the Putative Ca2+-Binding Reservoir at the N-Terminal Domain.Semantic proximity Read ↗

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