Associated Papers
Orthosteric interactions with PIP 2 activate TMEM16A channels.
Xu J et al.
Biorxiv : the Preprint Server for Biology, 2025
Gating and anion selectivity are reciprocally regulated in TMEM16A (ANO1).
De Jesús-Pérez JJ et al.
The Journal of General Physiology, 2022
Anoctamin 1 controls bone resorption by coupling Cl- channel activation with RANKL-RANK signaling transduction.
Sun W et al.
Nature Communications, 2022
Polymodal Control of TMEM16x Channels and Scramblases.
Agostinelli E et al.
International Journal of Molecular Sciences, 2022
Gating and Regulatory Mechanisms of TMEM16 Ion Channels and Scramblases.
Le SC et al.
Frontiers in Physiology, 2021
Voltage-Dependent Protonation of the Calcium Pocket Enable Activation of the Calcium-Activated Chloride Channel Anoctamin-1 (TMEM16A).
Segura-Covarrubias G et al.
Scientific Reports, 2020
Two Ca(2+)-Binding Sites Cooperatively Couple Together in TMEM16A Channel.
Han Y et al.
The Journal of Membrane Biology, 2016
Protons inhibit anoctamin 1 by competing with calcium.
Chun H et al.
Cell Calcium, 2015
X-ray structure of a calcium-activated TMEM16 lipid scramblase.
Brunner JD et al.
Nature, 2014
TMEM16A-TMEM16B chimaeras to investigate the structure-function relationship of calcium-activated chloride channels.
Scudieri P et al.
The Biochemical Journal, 2013
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