ArticleThe Journal of biological chemistry2012
Structural model of channelrhodopsin.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Ion-conducting and gating molecular mechanisms of channelrhodopsin revealed by true-atomic-resolution structures of open and closed states.Nature structural & molecular biology · 2025Article
- Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.Journal of the American Chemical Society · 2025Article
- Metadynamics simulations reveal mechanisms of Na+ and Ca2+ transport in two open states of the channelrhodopsin chimera, C1C2.PloS one · 2024Article
- Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin.eLife · 2021Article
- Gate-keeper of ion transport-a highly conserved helix-3 tryptophan in a channelrhodopsin chimera, C1C2/ChRWR.Biophysics and physicobiology · 2020Article
- Molecular Dynamics Simulation of Transmembrane Transport of Chloride Ions in Mutants of Channelrhodopsin.Biomolecules · 2019Article
- Formation Mechanism of Ion Channel in Channelrhodopsin-2: Molecular Dynamics Simulation and Steering Molecular Dynamics Simulations.International journal of molecular sciences · 2019Article
- a-ARM: Automatic Rhodopsin Modeling with Chromophore Cavity Generation, Ionization State Selection, and External Counterion Placement.Journal of chemical theory and computation · 2019Article
- Retinal isomerization and water-pore formation in channelrhodopsin-2.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mutational analysis of the conserved carboxylates of anion channelrhodopsin-2 (ACR2) expressed inBiophysics and physicobiology · 2018Article
- Mechanism by which water and protein electrostatic interactions control proton transfer at the active site of channelrhodopsin.PloS one · 2018Article
- Molecular determinants of proton selectivity and gating in the red-light activated channelrhodopsin Chrimson.Scientific reports · 2017Article
- Proton transfer reactions in the red light-activatable channelrhodopsin variant ReaChR and their relevance for its function.The Journal of biological chemistry · 2017Article
- Adjacent channelrhodopsin-2 residues within transmembranes 2 and 7 regulate cation selectivity and distribution of the two open states.The Journal of biological chemistry · 2017Article
- Active site structure and absorption spectrum of channelrhodopsin-2 wild-type and C128T mutant.Chemical science · 2016Article
- An improved chloride-conducting channelrhodopsin for light-induced inhibition of neuronal activity in vivo.Scientific reports · 2015Article
- Kinetic and vibrational isotope effects of proton transfer reactions in channelrhodopsin-2.Biophysical journal · 2015Article
- Kinetic evaluation of photosensitivity in bi-stable variants of chimeric channelrhodopsins.PloS one · 2015Article
- Role of a helix B lysine residue in the photoactive site in channelrhodopsins.Biophysical journal · 2014Article
- Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Chemical reviews · 2014Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Channelrhodopsins (ChRs) are light-gated cation channels that mediate ion transport across membranes in microalgae (vectorial catalysis). ChRs are now widely used for the analysis of neural networks in tissues and living animals with light (optogenetics). For elucidation of functional mechanisms at the atomic level, as well as for further engineering and application, a detailed structure is urgently needed. In the absence of an experimental structure, here we develop a structural ChR model based on several molecular computational approaches, capitalizing on characteristic patterns in amino acid sequences of ChR1, ChR2, Volvox ChRs, Mesostigma ChR, and the recently identified ChR of the halophilic alga Dunaliella salina. In the present model, we identify remarkable structural motifs that may explain fundamental electrophysiological properties of ChR2, ChR1, and their mutants, and in a crucial validation of the model, we successfully reproduce the excitation energy predicted by absorption spectra.
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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.