ArticleNature communications2012
Structural rearrangements underlying ligand-gating in Kir channels.
Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 33 citations in OpenAlex.
- PIP2-driven cytoplasmic domain motions are coupled to Kir2 channel gating.The Journal of general physiology · 2025Article
- Anionic lipids modulate the membrane localization and conformational dynamics of KirBac1.1 slide helix during lipid-dependent activation.The Biochemical journal · 2025Article
- Structural Dynamics of the Slide Helix of Inactive/Closed Conformation of KirBac1.1 in Micelles and Membranes: A Fluorescence Approach.The Journal of membrane biology · 2025Article
- Oxidation Driven Reversal of PIPFunction (Oxford, England) · 2023Article
- Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements.International journal of molecular sciences · 2021Article
- Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State.Frontiers in molecular biosciences · 2021Article
- Unexpected Gating Behaviour of an Engineered Potassium Channel Kir.Frontiers in molecular biosciences · 2021Article
- Bibliometric analysis of potassium channel research.Channels (Austin, Tex.) · 2020Article
- 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
- Atomistic basis of opening and conduction in mammalian inward rectifier potassium (Kir2.2) channels.The Journal of general physiology · 2020Article
- Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019Article
- LRET Determination of Molecular Distances during pH Gating of the Mammalian Inward Rectifier Kir1.1b.Biophysical journal · 2018Article
- Conformational changes at cytoplasmic intersubunit interactions control Kir channel gating.The Journal of biological chemistry · 2017Article
- Solution-Based Single-Molecule FRET Studies of K(+) Channel Gating in a Lipid Bilayer.Biophysical journal · 2016Article
- Structural dynamics of potassium-channel gating revealed by single-molecule FRET.Nature structural & molecular biology · 2016Article
- Mutations in Nature Conferred a High Affinity Phosphatidylinositol 4,5-Bisphosphate-binding Site in Vertebrate Inwardly Rectifying Potassium Channels.The Journal of biological chemistry · 2015Article
- Molecular Dynamics Simulations of KirBac1.1 Mutants Reveal Global Gating Changes of Kir Channels.Journal of chemical information and modeling · 2015Article
- Phosphoinositide regulation of inward rectifier potassium (Kir) channels.Frontiers in physiology · 2014Review
- Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.The Journal of biological chemistry · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Inward rectifier potassium (Kir) channels are physiologically regulated by a wide range of ligands that all act on a common gate, although structural details of gating are unclear. Here we show, using small molecule fluorescent probes attached to introduced cysteines, the molecular motions associated with gating of KirBac1.1 channels. The accessibility of the probes indicates a major barrier to fluorophore entry to the inner cavity. Changes in fluorescence resonance energy transfer between fluorophores, attached to KirBac1.1 tetramers, show that phosphatidylinositol-4,5-bisphosphate-induced closure involves tilting and rotational motions of secondary structural elements of the cytoplasmic domain that couple ligand binding to a narrowing of the cytoplasmic vestibule. The observed ligand-dependent conformational changes in KirBac1.1 provide a general model for ligand-induced Kir channel gating at the molecular level.
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.