Mechanism of activation gating in the full-length KcsA K+ channel
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference21 articles.
1. Crystal structure of full-length KcsA in its closed conformation
2. Structure of the Human BK Channel Ca 2+ -Activation Apparatus at 3.0 Å Resolution
3. Structural basis for modulation and agonist specificity of HCN pacemaker channels
4. Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
5. Molecular Architecture of Full-Length KcsA
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1. Steady-state and time-resolved fluorescent methodologies to characterize the conformational landscape of the selectivity filter of K+ channels;Methods;2024-05
2. Studying KcsA Channel Clustering Using Single Channel Voltage-Clamp Fluorescence Imaging*;Frontiers in Physiology;2022-06-03
3. Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements;International Journal of Molecular Sciences;2021-11-04
4. Hysteresis of a Tension-Sensitive K+ Channel Revealed by Time-Lapse Tension Measurements;JACS Au;2021-03-22
5. NMR studies of lipid regulation of the K+ channel KcsA;Biochimica et Biophysica Acta (BBA) - Biomembranes;2021-03
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