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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:

Enzyme Dynamics: Looking Beyond a Single Structure
Pratul K. Agarwal, David N. Bernard, Khushboo Bafna, et al.
ChemCatChem (2020) Vol. 12, Iss. 19, pp. 4704-4720
Open Access | Times Cited: 42

Showing 1-25 of 42 citing articles:

Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development
Kwangho Nam, Yihan Shao, Dan Thomas Major, et al.
ACS Omega (2024)
Open Access | Times Cited: 15
Unlocking the Stereoselectivity and Substrate Acceptance of Enzymes: Proline‐Induced Loop Engineering Test
Ge Qu, Yuexin Bi, Beibei Liu, et al.
Angewandte Chemie International Edition (2021) Vol. 61, Iss. 1
Closed Access | Times Cited: 64
Enzymes in a human cytoplasm model organize into submetabolon complexes
Premila P. Samuel, Meredith M. Rickard, Taras V. Pogorelov, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 5
Closed Access
From random to rational: improving enzyme design through electric fields, second coordination sphere interactions, and conformational dynamics
Shobhit S. Chaturvedi, Daniel Bím, Christo Christov, et al.
Chemical Science (2023) Vol. 14, Iss. 40, pp. 10997-11011
Open Access | Times Cited: 15
Protein Representations: Encoding Biological Information for Machine Learning in Biocatalysis
David Harding-Larsen, Jonathan Funk, Niklas Gesmar Madsen, et al.
(2024)
Open Access | Times Cited: 3
The evolution and engineering of enzyme activity through tuning conformational landscapes
Adam M. Damry, Colin J. Jackson
Protein Engineering Design and Selection (2021) Vol. 34
Closed Access | Times Cited: 26
Unravelling Enzymatic Features in a Supramolecular Iridium Catalyst by Computational Calculations
Michele Tomasini, Lucia Caporaso, Jonathan Trouvé, et al.
Chemistry - A European Journal (2022) Vol. 28, Iss. 57
Open Access | Times Cited: 14
The Conformational Transitions and Dynamics of Burkholderia cepacia Lipase Regulated by Water–Oil Interfaces
Kuan Liang, Wanqian Dong, Jiamin Gao, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 12, pp. 3854-3864
Closed Access | Times Cited: 7
Unifying Catalysis Framework to Dissect Proteasomal Degradation Paradigms
Frances P. Rodriguez‐Rivera, Samuel M. Levi
ACS Central Science (2021) Vol. 7, Iss. 7, pp. 1117-1125
Open Access | Times Cited: 18
Towards the energy landscape of adenylate kinase in crowded milieu: Activity, conformation, structure and dynamics in sequence
Harshita Rastogi, Arvind Singh, Pramit K. Chowdhury
Archives of Biochemistry and Biophysics (2023) Vol. 743, pp. 109658-109658
Closed Access | Times Cited: 6
Non-active Site Residue in Loop L4 Alters Substrate Capture and Product Release in d-Arginine Dehydrogenase
Daniel Ouedraogo, Michael Souffrant, Xin‐Qiu Yao, et al.
Biochemistry (2023) Vol. 62, Iss. 5, pp. 1070-1081
Open Access | Times Cited: 5
Equilibrium Dynamics of a Biomolecular Complex Analyzed at Single-amino Acid Resolution by Cryo-electron Microscopy
Daniel Luque, Álvaro Ortega-Esteban, Alejandro Valbuena, et al.
Journal of Molecular Biology (2023) Vol. 435, Iss. 8, pp. 168024-168024
Open Access | Times Cited: 5
Exploring Oxidoreductases from Extremophiles for Biosynthesis in a Non-Aqueous System
Shizhen Wang, Hangbin Lei, Zhehui Ji
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 7, pp. 6396-6396
Open Access | Times Cited: 5
A Series of Ni Complexes Based on a Versatile ATCUN-Like Tripeptide Scaffold to Decipher Key Parameters for Superoxide Dismutase Activity
Jérémy Domergue, Pawel Guinard, Magali Douillard, et al.
Inorganic Chemistry (2023) Vol. 62, Iss. 23, pp. 8747-8760
Closed Access | Times Cited: 5
Protein representations: Encoding biological information for machine learning in biocatalysis
David Harding-Larsen, Jonathan Funk, Niklas Gesmar Madsen, et al.
Biotechnology Advances (2024) Vol. 77, pp. 108459-108459
Closed Access | Times Cited: 1
Conformational exchange divergence along the evolutionary pathway of eosinophil-associated ribonucleases
David N. Bernard, C. S. Narayanan, Tim Hempel, et al.
Structure (2023) Vol. 31, Iss. 3, pp. 329-342.e4
Open Access | Times Cited: 4
Mutual Protein-Ligand Conformational Selection Drives cGMP vs. cAMP Selectivity in Protein Kinase G
Bryan VanSchouwen, Stephen Boulton, Giuseppe Melacini
Journal of Molecular Biology (2021) Vol. 433, Iss. 21, pp. 167202-167202
Closed Access | Times Cited: 7
Profiling Enzyme Activity of l-Asparaginase II by NMR-Based Methyl Fingerprinting at Natural Abundance
Rachayita Nag, Srishti Joshi, Anurag S. Rathore, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 19, pp. 10826-10838
Open Access | Times Cited: 2
Dynamic self-assembly of supramolecular catalysts from precision macromolecules
Qian Qin, Jie Li, David Dellemme, et al.
Chemical Science (2023) Vol. 14, Iss. 35, pp. 9283-9292
Open Access | Times Cited: 2
Design of motifs interfacial interactions by co‐evolved analysis of D‐amino acid dehydrogenase for stability enhancement
Zhehui Ji, Qian Zhang, Lingxuan Duan, et al.
AIChE Journal (2023) Vol. 69, Iss. 11
Closed Access | Times Cited: 2
Editing Domain Motions Preorganize the Synthetic Active Site of Prolyl-tRNA Synthetase
Quin Hu, Murphi T. Williams, Irina Shulgina, et al.
ACS Catalysis (2020) Vol. 10, Iss. 17, pp. 10229-10242
Open Access | Times Cited: 6
Structural dynamics and computational design of synthetic enzymes
Valerie Vaissier Welborn
Chem Catalysis (2021) Vol. 2, Iss. 1, pp. 19-28
Open Access | Times Cited: 6
Unlocking the Stereoselectivity and Substrate Acceptance of Enzymes: Proline‐Induced Loop Engineering Test
Ge Qu, Yuexin Bi, Beibei Liu, et al.
Angewandte Chemie (2021) Vol. 134, Iss. 1
Closed Access | Times Cited: 6
Structural Dynamics Support Electrostatic Interactions in the Active Site of Adenylate Kinase
Monsurat M. Lawal, Valerie Vaissier Welborn
ChemBioChem (2022) Vol. 23, Iss. 10
Closed Access | Times Cited: 4
Conformational modulation of a mobile loop controls catalysis in the (βα)8-barrel enzyme of histidine biosynthesis HisF
Enrico Hupfeld, Sandra Schlee, Jan Philip Wurm, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
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