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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:

True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins
Valentin Borshchevskiy, Kirill Kovalev, Ekaterina Round, et al.
Nature Structural & Molecular Biology (2022) Vol. 29, Iss. 5, pp. 440-450
Open Access | Times Cited: 35

Showing 1-25 of 35 citing articles:

The Realm of Unconventional Noncovalent Interactions in Proteins: Their Significance in Structure and Function
Vishal Annasaheb Adhav, K. Saikrishnan
ACS Omega (2023) Vol. 8, Iss. 25, pp. 22268-22284
Open Access | Times Cited: 54
Hybrid Quantum Mechanical/Molecular Mechanical Methods For Studying Energy Transduction in Biomolecular Machines
Tomáš Kubař, Marcus Elstner, Qiang Cui
Annual Review of Biophysics (2023) Vol. 52, Iss. 1, pp. 525-551
Open Access | Times Cited: 23
From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons
Nicolas Caramello, Antoine Royant
Acta Crystallographica Section D Structural Biology (2024) Vol. 80, Iss. 2, pp. 60-79
Open Access | Times Cited: 9
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
Mechanisms of membrane protein crystallization in ‘bicelles’
Tatiana N. Murugova, Oleksandr I. Ivankov, Yury L. Ryzhykau, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 26
Tubulin degradation: Principles, agents, and applications
Yifan Zhang, Jiao Huang, Weixin Zhang, et al.
Bioorganic Chemistry (2023) Vol. 139, pp. 106684-106684
Closed Access | Times Cited: 15
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
Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography
Robert Bosman, Giorgia Ortolani, Swagatha Ghosh, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Chemical Reactivity and Molecular Interactions
Narayan S. Punekar
(2025), pp. 313-331
Closed Access
Mechanisms of inward transmembrane proton translocation
Kirill Kovalev, Fedor Tsybrov, Alexey Alekseev, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 7, pp. 970-979
Closed Access | Times Cited: 9
Enhancing the thermostability of the leucine dehydrogenase from Planifilum fimeticola through rational design of the flexible region
Xiang-Zhang, Xichuan Zhang, Hongling Shi, et al.
Molecular Catalysis (2024) Vol. 559, pp. 114048-114048
Closed Access | Times Cited: 3
Combining Flexible Region Design and Automatic Design to Enhance the Thermal Stability and Catalytic Efficiency of Leucine Dehydrogenase
Xiang Zhang, Xichuan Zhang, Hongling Shi, et al.
Journal of Agricultural and Food Chemistry (2024) Vol. 72, Iss. 24, pp. 13801-13811
Closed Access | Times Cited: 3
Structural Models of the First Molecular Events in the Heliorhodopsin Photocycle
Kithmini Wijesiri, José A. Gascón
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 25, pp. 5966-5972
Closed Access | Times Cited: 2
Hydrogen-Bonding and Hydrophobic Interaction Networks as Structural Determinants of Microbial Rhodopsin Function
Éva Bertalan, Masae Konno, Marı́a del Carmen Marı́n, et al.
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 30, pp. 7407-7426
Closed Access | Times Cited: 2
The TR-icOS setup at the ESRF: time-resolved microsecond UV–Vis absorption spectroscopy on protein crystals
Sylvain Engilberge, Nicolas Caramello, Sergey Bukhdruker, et al.
Acta Crystallographica Section D Structural Biology (2023) Vol. 80, Iss. 1, pp. 16-25
Open Access | Times Cited: 6
Contribution of the Collective Excitations to the Coupled Proton and Energy Transport along Mitochondrial Cristae Membrane in Oxidative Phosphorylation System
Semen V. Nesterov, L. S. Yaguzhinsky, Р. Г. Василов, et al.
Entropy (2022) Vol. 24, Iss. 12, pp. 1813-1813
Open Access | Times Cited: 8
Detailed analysis of distorted retinal and its interaction with surrounding residues in the K intermediate of bacteriorhodopsin
Shoun Taguchi, Satomi Niwa, Hoang-Anh Dao, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 4
Substrate-Assisted Mechanism for the Degradation of N-Glycans by a Gut Bacterial Mannoside Phosphorylase
Mercedes Alfonso‐Prieto, Irene Cuxart, Gabrielle Potocki‐Véronèse, et al.
ACS Catalysis (2023) Vol. 13, Iss. 7, pp. 4283-4289
Open Access | Times Cited: 4
A DFTB study on the electronic response of encapsulated DNA nucleobases onto chiral CNTs as a sequencer
Seyyed Mostafa Monavari, Nafiseh Memarian
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 1
Flexibility and Hydration of the QoSite Determine Multiple Pathways for Proton Transfer in Cytochromebc1
Sofia R. G. Camilo, Guilherme M. Arantes
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Mechanism of Absorption Wavelength Shift of Bacteriorhodopsin During Photocycle
Tomoyasu Noji, Hiroshi Ishikita
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 48, pp. 9945-9955
Closed Access | Times Cited: 6
Graphs of protein-water hydrogen bond networks to dissect structural movies of ion-transfer microbial rhodopsins
Éva Bertalan, Ana‐Nicoleta Bondar
Frontiers in Chemistry (2023) Vol. 10
Open Access | Times Cited: 3
Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases—United in Diversity
Maria I. Kozlova, Daria N. Shalaeva, Daria V. Dibrova, et al.
Biomolecules (2022) Vol. 12, Iss. 10, pp. 1346-1346
Open Access | Times Cited: 4
Common mechanism of activated catalysis in P-loop fold nucleoside triphosphatases -in varietate concordia
Maria I. Kozlova, Daria N. Shalaeva, Daria V. Dibrova, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 3
CryoRhodopsins: a comprehensive characterization of a new clade of microbial rhodopsins from cold environments
Gerrit H. U. Lamm, Egor Marin, Alexey Alekseev, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
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