ArticleNature communications2018
Crystal structure of the red light-activated channelrhodopsin Chrimson.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 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.
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Who cites it
82 citing papers in PubMed, 166 citations in OpenAlex.
- Multicolored, Sonosensitizer-Optimized Organic Mechanoluminescent Nanoparticles for Functional Sono-Optogenetics.Journal of the American Chemical Society · 2026Article
- Active pixel power control for crosstalk-free all-optical neural interrogation.Nature communications · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Multicolor photoreactions of the red light-activated channelrhodopsin Chrimson.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- A second photoactivatable state of the anion-conducting channelrhodopsin GtACR1 empowers persistent activity.Communications biology · 2025Article
- Ion-conducting and gating molecular mechanisms of channelrhodopsin revealed by true-atomic-resolution structures of open and closed states.Nature structural & molecular biology · 2025Article
- Blue-shifted ancyromonad channelrhodopsins for multiplex optogenetics.bioRxiv : the preprint server for biology · 2025Article
- CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments.Science advances · 2025Article
- Neurons and molecules involved in noxious light sensation in Caenorhabditis elegans.G3 (Bethesda, Md.) · 2025Article
- Article
- Retinal to Retinal Energy Transfer in a Bistable Microbial Rhodopsin Dimer.Journal of the American Chemical Society · 2025Article
- Optogenetic engineering for ion channel modulation.Current opinion in chemical biology · 2025Review
- Electrophysiologically calibrated optogenetic stimulation of dentate granule cells mitigates dendritic spine loss in denervated organotypic entorhino-hippocampal slice cultures.Scientific reports · 2025Article
- Advancing Neuroscience and Therapy: Insights into Genetic and Non-Genetic Neuromodulation Approaches.Cells · 2025Review
- Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.Journal of the American Chemical Society · 2025Article
- Protein design accelerates the development and application of optogenetic tools.Computational and structural biotechnology journal · 2025Review
- HulaChrimson: A Chrimson-like cation channelrhodopsin discovered using freshwater metatranscriptomics from Lake Hula.Biophysics and physicobiology · 2025Article
- Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025Review
- Sodium-Selective Channelrhodopsins.Cells · 2024Review
22 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
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Channelrhodopsins are light-activated ion channels that mediate cation permeation across cell membranes upon light absorption. Red-light-activated channelrhodopsins are of particular interest, because red light penetrates deeper into biological tissues and also enables dual-color experiments in combination with blue-light-activated optogenetic tools. Here we report the crystal structure of the most red-shifted channelrhodopsin from the algae Chlamydomonas noctigama, Chrimson, at 2.6 Å resolution. Chrimson resembles prokaryotic proton pumps in the retinal binding pocket, while sharing similarity with other channelrhodopsins in the ion-conducting pore. Concomitant mutation analysis identified the structural features that are responsible for Chrimson's red light sensitivity; namely, the protonation of the counterion for the retinal Schiff base, and the polar residue distribution and rigidity of the retinal binding pocket. Based on these mechanistic insights, we engineered ChrimsonSA, a mutant with a maximum activation wavelength red-shifted beyond 605 nm and accelerated closing kinetics.
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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.