ArticleNature2010
Structural mechanism of C-type inactivation in K(+) channels.
Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 319 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
319 citing papers in PubMed.
- Lipid gating of BK channels and activation mechanism by negatively charged lipids.Communications chemistry · 2026Article
- Gating crosstalk in potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Dynamical Nonequilibrium Molecular Dynamics Simulations Reveal Atomistic Steps of C-Type Inactivation in Cardiac hERG Channels.Journal of the American Chemical Society · 2026Article
- Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026Review
- Gating shift to an ohmic mode of TREK-1 channel induced by docosahexaenoic acid.Biophysical journal · 2026Article
- Article
- A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026Review
- Molecular Determinants of Voltage-Dependent Gating in Kv11.1 Channels.Advances in experimental medicine and biology · 2026Review
- Closed state structure of the pore revealed by uncoupled Shaker KNature communications · 2025Article
- Orphan Three-Finger Toxins from Snake Venoms: Unexplored Library of Novel Biological Ligands with Potential New Structures and Functions.International journal of molecular sciences · 2025Review
- High-Throughput MicroED for Probing Ion Channel Dynamics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Article
- Creating Coarse-Grained Systems with COBY: Toward Higher Accuracy of Complex Biological Systems.Journal of chemical information and modeling · 2025Article
- Harnessing AlphaFold to reveal hERG channel conformational state secrets.bioRxiv : the preprint server for biology · 2025Article
- Do selectivity filter carbonyls in KJournal of structural biology: X · 2024Article
- Structural biology and molecular pharmacology of voltage-gated ion channels.Nature reviews. Molecular cell biology · 2024Review
- Elucidating the role of lipid interactions in stabilizing the membrane protein KcsA.Biophysical journal · 2024Article
- Potassium dependent structural changes in the selectivity filter of HERG potassium channels.Nature communications · 2024Article
- A physical derivation of high-flux ion transport in biological channel via quantum ion coherence.Nature communications · 2024Article
- Unmasking subtype-dependent susceptibility to C-type inactivation in mammalian Kv1 channels.Biophysical journal · 2024Article
259 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Interconversion between conductive and non-conductive forms of the K(+) channel selectivity filter underlies a variety of gating events, from flicker transitions (at the microsecond timescale) to C-type inactivation (millisecond to second timescale). Here we report the crystal structure of the Streptomyces lividans K(+) channel KcsA in its open-inactivated conformation and investigate the mechanism of C-type inactivation gating at the selectivity filter from channels 'trapped' in a series of partially open conformations. Five conformer classes were identified with openings ranging from 12 A in closed KcsA (Calpha-Calpha distances at Thr 112) to 32 A when fully open. They revealed a remarkable correlation between the degree of gate opening and the conformation and ion occupancy of the selectivity filter. We show that a gradual filter backbone reorientation leads first to a loss of the S2 ion binding site and a subsequent loss of the S3 binding site, presumably abrogating ion conduction. These structures indicate a molecular basis for C-type inactivation in K(+) channels.
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.