ArticleBiophysical journal2016
Solution-Based Single-Molecule FRET Studies of K(+) Channel Gating in a Lipid Bilayer.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed.
- Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026Review
- Labelizer: systematic selection of protein residues for covalent fluorophore labeling.Nature communications · 2025Article
- Article
- Conformational Dynamic Studies of Prokaryotic Potassium Channels Explored by Homo-FRET Methodologies.Methods in molecular biology (Clifton, N.J.) · 2024Article
- pH-induced conformational changes in the selectivity filter of a potassium channel lead to alterations in its selectivity and permeation properties.Frontiers in pharmacology · 2024Article
- Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements.International journal of molecular sciences · 2021Article
- Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins.Membranes · 2021Review
- Single-molecule fluorescence vistas of how lipids regulate membrane proteins.Biochemical Society transactions · 2021Review
- The Lipid Activation Mechanism of a Transmembrane Potassium Channel.Journal of the American Chemical Society · 2020Article
- Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Confinement-Free Wide-Field Ratiometric Tracking of Single Fluorescent Molecules.Biophysical journal · 2019Article
- Regulation of Membrane Calcium Transport Proteins by the Surrounding Lipid Environment.Biomolecules · 2019Review
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- We FRET so You Don't Have To: New Models of the Lipoprotein Lipase Dimer.Biochemistry · 2018Article
- LRET Determination of Molecular Distances during pH Gating of the Mammalian Inward Rectifier Kir1.1b.Biophysical journal · 2018Article
- Artificial Lipid Membranes: Past, Present, and Future.Membranes · 2017Review
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Ion channels are dynamic multimeric proteins that often undergo multiple unsynchronized structural movements as they switch between their open and closed states. Such structural changes are difficult to measure within the context of a native lipid bilayer and have often been monitored via macroscopic changes in Förster resonance energy transfer (FRET) between probes attached to different parts of the protein. However, the resolution of this approach is limited by ensemble averaging of structurally heterogeneous subpopulations. These problems can be overcome by measurement of FRET in single molecules, but this presents many challenges, in particular the ability to control labeling of subunits within a multimeric protein with acceptor and donor fluorophores, as well as the requirement to image large numbers of individual molecules in a membrane environment. To address these challenges, we randomly labeled tetrameric KirBac1.1 potassium channels, reconstituted them into lipid nanodiscs, and performed single-molecule FRET confocal microscopy with alternating-laser excitation as the channels diffused in solution. These solution-based single-molecule FRET measurements of a multimeric ion channel in a lipid bilayer have allowed us to probe the structural changes that occur upon channel activation and inhibition. Our results provide direct evidence of the twist-to-shrink movement of the helix bundle crossing during channel gating and demonstrate how this method might be applied to real-time structural studies of ion channel gating.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.