ArticleNature communications2025
Structural insights into light-gating of potassium-selective channelrhodopsin.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed.
- Optogenetics meets automated patch clamp.iScience · 2026Article
- Experimentally informed, quantitative photocycle model of the light-gated potassium channel WiChR.Biophysical journal · 2026Article
- Channel gating in bacteriorhodopsin-like channelrhodopsins with contrasting KBiophysical journal · 2026Article
- Theoretical analysis of low-power optogenetic suppression of action potentials in human ventricular cardiomyocytes expressed with potassium-selective channelrhodopsins.Scientific reports · 2026Article
- Stabilized Ion Selectivity Corrects Activation Drift in Kalium Channelrhodopsins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Microsecond Time-Resolved Cryo-EM Based on Jet Vitrification.bioRxiv : the preprint server for biology · 2025Article
- Pore-Opening and Ion-Conduction Mechanism in Channelrhodopsins C1C2, ChR2, and iChloC by Computational Electrophysiology and Constant-pH Simulations.Journal of chemical information and modeling · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors.
Funding
Abstract
Structural information on channelrhodopsins' mechanism of light-gated ion conductance is scarce, limiting its engineering as optogenetic tools. Here, we use single-particle cryo-electron microscopy of peptidisc-incorporated protein samples to determine the structures of the slow-cycling mutant C110A of kalium channelrhodopsin 1 from Hyphochytrium catenoides (HcKCR1) in the dark and upon laser flash excitation. Upon photoisomerization of the retinal chromophore, the retinylidene Schiff base NH-bond reorients from the extracellular to the cytoplasmic side. This switch triggers a series of side chain reorientations and merges intramolecular cavities into a transmembrane K
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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.