ArticleChannels (Austin, Tex.)2019
The influence of membrane bilayer thickness on KcsA channel activity.
Article in Channels (Austin, Tex.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Lipid trapping slows ball-and-chain inactivation in a calcium-activated potassium channel.Nature communications · 2026Article
- Modulation of Kv Channel Gating by Light-Controlled Membrane Thickness.Biomolecules · 2025Article
- Current Trends and Changes in Use of Membrane Molecular Dynamics Simulations within Academia and the Pharmaceutical Industry.Membranes · 2023Review
- Studying KcsA Channel Clustering Using Single Channel Voltage-Clamp Fluorescence Imaging.Frontiers in physiology · 2022Article
- Mechanisms underlying drug-mediated regulation of membrane protein function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mechanisms and Applications of Neuromodulation Using Surface Acoustic Waves-A Mini-Review.Frontiers in neuroscience · 2021Review
- Lipid-protein interactions modulate the conformational equilibrium of a potassium channel.Nature communications · 2020Article
- Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Atomic resolution structures have provided significant insight into the gating and permeation mechanisms of various ion channels, including potassium channels. However, ion channels may also be regulated by numerous factors, including the physiochemical properties of the membrane in which they are embedded. For example, the matching of the bilayer's hydrophobic region to the hydrophobic external surface of the ion channel is thought to minimize the energetic penalty needed to solvate hydrophobic residues or exposed lipid tails. To understand the molecular basis of such regulation by hydrophobic matching requires examining channels in the presence of the lipid membrane. Here we examine the role of hydrophobic matching in regulating the activity of the model potassium channel, KcsA.
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