
OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!
If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.
Requested Article:
Bacteriorhodopsin-like channelrhodopsins: Alternative mechanism for control of cation conductance
Oleg A. Sineshchekov, Elena G. Govorunova, Hai Li, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 45
Open Access | Times Cited: 56
Oleg A. Sineshchekov, Elena G. Govorunova, Hai Li, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 45
Open Access | Times Cited: 56
Showing 1-25 of 56 citing articles:
Optogenetics for light control of biological systems
Valentina Emiliani, Emilia Entcheva, Rainer Hedrich, et al.
Nature Reviews Methods Primers (2022) Vol. 2, Iss. 1
Open Access | Times Cited: 255
Valentina Emiliani, Emilia Entcheva, Rainer Hedrich, et al.
Nature Reviews Methods Primers (2022) Vol. 2, Iss. 1
Open Access | Times Cited: 255
Structural basis for channel conduction in the pump-like channelrhodopsin ChRmine
Koichiro Kishi, Yoon Seok Kim, Masahiro Fukuda, et al.
Cell (2022) Vol. 185, Iss. 4, pp. 672-689.e23
Open Access | Times Cited: 108
Koichiro Kishi, Yoon Seok Kim, Masahiro Fukuda, et al.
Cell (2022) Vol. 185, Iss. 4, pp. 672-689.e23
Open Access | Times Cited: 108
Kalium channelrhodopsins are natural light-gated potassium channels that mediate optogenetic inhibition
Elena G. Govorunova, Yueyang Gou, Oleg A. Sineshchekov, et al.
Nature Neuroscience (2022) Vol. 25, Iss. 7, pp. 967-974
Open Access | Times Cited: 100
Elena G. Govorunova, Yueyang Gou, Oleg A. Sineshchekov, et al.
Nature Neuroscience (2022) Vol. 25, Iss. 7, pp. 967-974
Open Access | Times Cited: 100
Towards the Idea of Molecular Brains
Youri Timsit, Stéphane Grégoire
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 21, pp. 11868-11868
Open Access | Times Cited: 64
Youri Timsit, Stéphane Grégoire
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 21, pp. 11868-11868
Open Access | Times Cited: 64
WiChR, a highly potassium-selective channelrhodopsin for low-light one- and two-photon inhibition of excitable cells
Johannes Vierock, Enrico Peter, Christiane Grimm, et al.
Science Advances (2022) Vol. 8, Iss. 49
Open Access | Times Cited: 56
Johannes Vierock, Enrico Peter, Christiane Grimm, et al.
Science Advances (2022) Vol. 8, Iss. 49
Open Access | Times Cited: 56
Structural basis for ion selectivity in potassium-selective channelrhodopsins
Seiya Tajima, Yoon Seok Kim, Masahiro Fukuda, et al.
Cell (2023) Vol. 186, Iss. 20, pp. 4325-4344.e26
Open Access | Times Cited: 32
Seiya Tajima, Yoon Seok Kim, Masahiro Fukuda, et al.
Cell (2023) Vol. 186, Iss. 20, pp. 4325-4344.e26
Open Access | Times Cited: 32
MerMAIDs: a family of metagenomically discovered marine anion-conducting and intensely desensitizing channelrhodopsins
Johannes Oppermann, P. Fischer, Arita Silapētere, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 65
Johannes Oppermann, P. Fischer, Arita Silapētere, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 65
RubyACRs, nonalgal anion channelrhodopsins with highly red-shifted absorption
Elena G. Govorunova, Oleg A. Sineshchekov, Hai Li, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 37, pp. 22833-22840
Open Access | Times Cited: 60
Elena G. Govorunova, Oleg A. Sineshchekov, Hai Li, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 37, pp. 22833-22840
Open Access | Times Cited: 60
Viral rhodopsins 1 are an unique family of light-gated cation channels
Dmitrii Zabelskii, Alexey Alekseev, Kirill Kovalev, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 54
Dmitrii Zabelskii, Alexey Alekseev, Kirill Kovalev, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 54
Emerging Diversity of Channelrhodopsins and Their Structure-Function Relationships
Elena G. Govorunova, Oleg A. Sineshchekov, John L. Spudich
Frontiers in Cellular Neuroscience (2022) Vol. 15
Open Access | Times Cited: 37
Elena G. Govorunova, Oleg A. Sineshchekov, John L. Spudich
Frontiers in Cellular Neuroscience (2022) Vol. 15
Open Access | Times Cited: 37
Proton-transporting heliorhodopsins from marine giant viruses
Shoko Hososhima, Ritsu Mizutori, Rei Abe‐Yoshizumi, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 30
Shoko Hososhima, Ritsu Mizutori, Rei Abe‐Yoshizumi, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 30
A subgroup of light-driven sodium pumps with an additional Schiff base counterion
Elizaveta Podoliak, Gerrit H. U. Lamm, Egor Marin, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 7
Elizaveta Podoliak, Gerrit H. U. Lamm, Egor Marin, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 7
Light-driven proton transfers and proton transport by microbial rhodopsins – A biophysical perspective
Leonid S. Brown
Biochimica et Biophysica Acta (BBA) - Biomembranes (2022) Vol. 1864, Iss. 5, pp. 183867-183867
Open Access | Times Cited: 26
Leonid S. Brown
Biochimica et Biophysica Acta (BBA) - Biomembranes (2022) Vol. 1864, Iss. 5, pp. 183867-183867
Open Access | Times Cited: 26
Cryo-EM structures of the channelrhodopsin ChRmine in lipid nanodiscs
Kyle Tucker, Savitha Sridharan, Hillel Adesnik, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 26
Kyle Tucker, Savitha Sridharan, Hillel Adesnik, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 26
Structures of channelrhodopsin paralogs in peptidiscs explain their contrasting K+ and Na+ selectivities
Takefumi Morizumi, Kyumhyuk Kim, Hai Li, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 15
Takefumi Morizumi, Kyumhyuk Kim, Hai Li, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 15
Mechanism of Inward Proton Transport in an Antarctic Microbial Rhodopsin
Andrew L. Harris, Michalis Lazaratos, Malte Siemers, et al.
The Journal of Physical Chemistry B (2020) Vol. 124, Iss. 24, pp. 4851-4872
Closed Access | Times Cited: 35
Andrew L. Harris, Michalis Lazaratos, Malte Siemers, et al.
The Journal of Physical Chemistry B (2020) Vol. 124, Iss. 24, pp. 4851-4872
Closed Access | Times Cited: 35
Structural insights into light-gating of potassium-selective channelrhodopsin
Takefumi Morizumi, Kyumhyuk Kim, Hai Li, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Takefumi Morizumi, Kyumhyuk Kim, Hai Li, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Ion-conducting and gating molecular mechanisms of channelrhodopsin revealed by true-atomic-resolution structures of open and closed states
Dmitrii Zabelskii, Sergey Bukhdruker, Siarhei Bukhalovich, et al.
Nature Structural & Molecular Biology (2025)
Closed Access
Dmitrii Zabelskii, Sergey Bukhdruker, Siarhei Bukhalovich, et al.
Nature Structural & Molecular Biology (2025)
Closed Access
Conductance Mechanisms of Rapidly Desensitizing Cation Channelrhodopsins from Cryptophyte Algae
Oleg A. Sineshchekov, Elena G. Govorunova, Hai Li, et al.
mBio (2020) Vol. 11, Iss. 2
Open Access | Times Cited: 29
Oleg A. Sineshchekov, Elena G. Govorunova, Hai Li, et al.
mBio (2020) Vol. 11, Iss. 2
Open Access | Times Cited: 29
Structural Foundations of Potassium Selectivity in Channelrhodopsins
Elena G. Govorunova, Oleg A. Sineshchekov, Leonid S. Brown, et al.
mBio (2022) Vol. 13, Iss. 6
Open Access | Times Cited: 17
Elena G. Govorunova, Oleg A. Sineshchekov, Leonid S. Brown, et al.
mBio (2022) Vol. 13, Iss. 6
Open Access | Times Cited: 17
Design of a light-gated proton channel based on the crystal structure of Coccomyxa rhodopsin
Roman Fudim, Michal Szczepek, Johannes Vierock, et al.
Science Signaling (2019) Vol. 12, Iss. 573
Open Access | Times Cited: 26
Roman Fudim, Michal Szczepek, Johannes Vierock, et al.
Science Signaling (2019) Vol. 12, Iss. 573
Open Access | Times Cited: 26
A light-gated cation channel with high reactivity to weak light
Shoko Hososhima, Shinji Ueno, Satoshi Okado, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 8
Shoko Hososhima, Shinji Ueno, Satoshi Okado, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 8
WiChR, a highly potassium selective channelrhodopsin for low-light two-photon neuronal inhibition
Johannes Vierock, Enrico Peter, Christiane Grimm, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 13
Johannes Vierock, Enrico Peter, Christiane Grimm, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 13
Ion Channel Properties of a Cation Channelrhodopsin, Gt_CCR4
Shunta Shigemura, Shoko Hososhima, Hideki Kandori, et al.
Applied Sciences (2019) Vol. 9, Iss. 17, pp. 3440-3440
Open Access | Times Cited: 22
Shunta Shigemura, Shoko Hososhima, Hideki Kandori, et al.
Applied Sciences (2019) Vol. 9, Iss. 17, pp. 3440-3440
Open Access | Times Cited: 22
Potassium-selective channelrhodopsins
Elena G. Govorunova, Oleg A. Sineshchekov, John L. Spudich
Biophysics and Physicobiology (2023) Vol. 20, Iss. Supplemental, pp. n/a-n/a
Open Access | Times Cited: 6
Elena G. Govorunova, Oleg A. Sineshchekov, John L. Spudich
Biophysics and Physicobiology (2023) Vol. 20, Iss. Supplemental, pp. n/a-n/a
Open Access | Times Cited: 6