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OpenAlex Citation Counts

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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:

High-resolution structural insights into the heliorhodopsin family
Kirill Kovalev, D. Volkov, Roman Astashkin, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 8, pp. 4131-4141
Open Access | Times Cited: 75

Showing 1-25 of 75 citing articles:

Microbial Rhodopsins: The Last Two Decades
Andrey Rozenberg, Keiichi Inoue, Hideki Kandori, et al.
Annual Review of Microbiology (2021) Vol. 75, Iss. 1, pp. 427-447
Open Access | Times Cited: 142
Rhodopsins at a glance
Takashi Nagata, Keiichi Inoue
Journal of Cell Science (2021) Vol. 134, Iss. 22
Open Access | Times Cited: 47
Proton-transporting heliorhodopsins from marine giant viruses
Shoko Hososhima, Ritsu Mizutori, Rei Abe‐Yoshizumi, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 31
Diverse heliorhodopsins detected via functional metagenomics in freshwater Actinobacteria, Chloroflexi and Archaea
Ariel Chazan, Andrey Rozenberg, Kentaro Mannen, et al.
Environmental Microbiology (2022) Vol. 24, Iss. 1, pp. 110-121
Open Access | Times Cited: 29
Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering
Willem J. de Grip, Srividya Ganapathy
Frontiers in Chemistry (2022) Vol. 10
Open Access | Times Cited: 28
Genomes of the “ Candidatus Actinomarinales” Order: Highly Streamlined Marine Epipelagic Actinobacteria
Mario López‐Pérez, Jose M. Haro‐Moreno, Jaime Iranzo, et al.
mSystems (2020) Vol. 5, Iss. 6
Open Access | Times Cited: 50
Structure/Function Study of Photoreceptive Proteins by FTIR Spectroscopy
Hideki Kandori
Bulletin of the Chemical Society of Japan (2020) Vol. 93, Iss. 7, pp. 904-926
Open Access | Times Cited: 42
Enhanced Recovery of Microbial Genes and Genomes From a Marine Water Column Using Long-Read Metagenomics
Jose M. Haro‐Moreno, Mario López‐Pérez, Francisco Rodrı́guez-Valera
Frontiers in Microbiology (2021) Vol. 12
Open Access | Times Cited: 34
Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping
Akimitsu Higuchi, Wataru Shihoya, Masae Konno, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 14
Open Access | Times Cited: 33
Mechanisms of membrane protein crystallization in ‘bicelles’
T. N. Murugova, Oleksandr I. Ivankov, Yury Ryzhykau, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 27
Structural insights into the mechanism of rhodopsin phosphodiesterase
Tatsuya Ikuta, Wataru Shihoya, Masahiro Sugiura, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 37
Microbial Rhodopsins
Valentin Gordeliy, Kirill Kovalev, Ernst Bamberg, et al.
Methods in molecular biology (2022), pp. 1-52
Closed Access | Times Cited: 22
Heliorhodopsin binds and regulates glutamine synthetase activity
Shin‐Gyu Cho, Myungchul Song, Kimleng Chuon, et al.
PLoS Biology (2022) Vol. 20, Iss. 10, pp. e3001817-e3001817
Open Access | Times Cited: 22
Heliorhodopsin Helps Photolyase to Enhance the DNA Repair Capacity
Jin‐gon Shim, Shin‐Gyu Cho, Sehwan Kim, et al.
Microbiology Spectrum (2022) Vol. 10, Iss. 6
Open Access | Times Cited: 19
Picosecond quantum-classical dynamics reveals that the coexistence of light-induced microbial and animal chromophore rotary motion modulates the isomerization quantum yield of heliorhodopsin
Riccardo Palombo, Leonardo Barneschi, Laura Pedraza‐González, et al.
Physical Chemistry Chemical Physics (2024) Vol. 26, Iss. 13, pp. 10343-10356
Closed Access | Times Cited: 4
Cryo-EM structure of a nanobody-bound heliorhodopsin
Ruixue Xia, Mingxia Sun, Lu Yang, et al.
Biochemical and Biophysical Research Communications (2025), pp. 151398-151398
Closed Access
Retinal to Retinal Energy Transfer in a Bistable Microbial Rhodopsin Dimer
Ivo H. M. van Stokkum, Jakub Dostál, Thanh Nhut, et al.
Journal of the American Chemical Society (2025)
Open Access
Structure-based insights into evolution of rhodopsins
Dmitrii Zabelskii, Natalia I. Dmitrieva, Oleksandr Volkov, et al.
Communications Biology (2021) Vol. 4, Iss. 1
Open Access | Times Cited: 25
Heliorhodopsin-mediated light-modulation of ABC transporter
Shin‐Gyu Cho, Ji‐Hyun Kim, Jieun Lee, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 3
Proteorhodopsin insights into the molecular mechanism of vectorial proton transport
Sergey Bukhdruker, Ivan Gushchin, Vitaly Shevchenko, et al.
Science Advances (2025) Vol. 11, Iss. 16
Closed Access
Heliorhodopsin Evolution Is Driven by Photosensory Promiscuity in Monoderms
Paul‐Adrian Bulzu, Vinicius Kavagutti, Cecilia Chiriac, et al.
mSphere (2021) Vol. 6, Iss. 6
Open Access | Times Cited: 22
Specific zinc binding to heliorhodopsin
Masanori Hashimoto, Koichi Miyagawa, Manish Pratap Singh, et al.
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 4, pp. 3535-3543
Closed Access | Times Cited: 8
Calcium Binding Mechanism in TAT Rhodopsin
Teppei Sugimoto, Koichi Miyagawa, Mitsuo Shoji, et al.
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 29, pp. 7102-7111
Closed Access | Times Cited: 3
Proton Pumping and Non-Pumping Terminal Respiratory Oxidases: Active Sites Intermediates of These Molecular Machines and Their Derivatives
Sergey A. Siletsky, Vitaliy B. Borisov
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 19, pp. 10852-10852
Open Access | Times Cited: 20
Conserved hydrogen-bond motifs of membrane transporters and receptors
Michalis Lazaratos, Malte Siemers, Leonid S. Brown, et al.
Biochimica et Biophysica Acta (BBA) - Biomembranes (2022) Vol. 1864, Iss. 6, pp. 183896-183896
Open Access | Times Cited: 13
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