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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:

Role of Conformational Dynamics in the Evolution of Retro-Aldolase Activity
Adrian Romero‐Rivera, Marc Garcia‐Borràs, Sílvia Osuna
ACS Catalysis (2017) Vol. 7, Iss. 12, pp. 8524-8532
Open Access | Times Cited: 153

Showing 1-25 of 153 citing articles:

Biocatalysis
Elizabeth L. Bell, William Finnigan, Scott P. France, et al.
Nature Reviews Methods Primers (2021) Vol. 1, Iss. 1
Open Access | Times Cited: 439
Conformational dynamics and enzyme evolution
Dušan Petrović, Valeria A. Risso, Shina Caroline Lynn Kamerlin, et al.
Journal of The Royal Society Interface (2018) Vol. 15, Iss. 144, pp. 20180330-20180330
Open Access | Times Cited: 191
Role of conformational dynamics in the evolution of novel enzyme function
Miguel A. Maria‐Solano, Eila Serrano‐Hervás, Adrian Romero‐Rivera, et al.
Chemical Communications (2018) Vol. 54, Iss. 50, pp. 6622-6634
Open Access | Times Cited: 164
Evolution of dynamical networks enhances catalysis in a designer enzyme
H. Adrian Bunzel, J. L. Ross Anderson, Donald Hilvert, et al.
Nature Chemistry (2021) Vol. 13, Iss. 10, pp. 1017-1022
Open Access | Times Cited: 111
Loop dynamics and the evolution of enzyme activity
Marina Corbella, Gaspar Pinto, Shina Caroline Lynn Kamerlin
Nature Reviews Chemistry (2023) Vol. 7, Iss. 8, pp. 536-547
Closed Access | Times Cited: 79
Role of distal sites in enzyme engineering
Jie Gu, Yan Xu, Yao Nie
Biotechnology Advances (2023) Vol. 63, pp. 108094-108094
Closed Access | Times Cited: 52
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: 24
The shortest path method (SPM) webserver for computational enzyme design
Guillem Casadevall, Jordi Casadevall, Cristina Duran, et al.
Protein Engineering Design and Selection (2024) Vol. 37
Closed Access | Times Cited: 19
Noteworthy Consensus Effects of D/E Residues in Umami Peptides Used for Designing the Novel Umami Peptides
Zhiyong Cui, Hengli Meng, Tianxing Zhou, et al.
Journal of Agricultural and Food Chemistry (2024) Vol. 72, Iss. 5, pp. 2789-2800
Closed Access | Times Cited: 18
Epistasis arises from shifting the rate-limiting step during enzyme evolution of a β-lactamase
Christopher Frøhlich, H. Adrian Bunzel, Karol Buda, et al.
Nature Catalysis (2024) Vol. 7, Iss. 5, pp. 499-509
Open Access | Times Cited: 18
The challenge of predicting distal active site mutations in computational enzyme design
Sílvia Osuna
Wiley Interdisciplinary Reviews Computational Molecular Science (2020) Vol. 11, Iss. 3
Open Access | Times Cited: 123
Harnessing Conformational Plasticity to Generate Designer Enzymes
Rory Crean, Jasmine M. Gardner, Shina Caroline Lynn Kamerlin
Journal of the American Chemical Society (2020) Vol. 142, Iss. 26, pp. 11324-11342
Open Access | Times Cited: 116
A Bird’s-Eye View of Enzyme Evolution: Chemical, Physicochemical, and Physiological Considerations
Dan Davidi, Liam M. Longo, Jagoda Jabłońska, et al.
Chemical Reviews (2018) Vol. 118, Iss. 18, pp. 8786-8797
Closed Access | Times Cited: 109
Ensemble-based enzyme design can recapitulate the effects of laboratory directed evolution in silico
Aron Broom, Rojo V. Rakotoharisoa, Michael C. Thompson, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 101
Pervasive cooperative mutational effects on multiple catalytic enzyme traits emerge via long-range conformational dynamics
Carlos G. Acevedo‐Rocha, Aitao Li, Lorenzo D’Amore, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 96
Protein ensembles link genotype to phenotype
Ruth Nussinov, Chung‐Jung Tsai, Hyunbum Jang
PLoS Computational Biology (2019) Vol. 15, Iss. 6, pp. e1006648-e1006648
Open Access | Times Cited: 90
Protein engineering: the potential of remote mutations
Matthew Wilding, Nansook Hong, Matthew A. Spence, et al.
Biochemical Society Transactions (2019) Vol. 47, Iss. 2, pp. 701-711
Open Access | Times Cited: 86
Efficient reductive desymmetrization of bulky 1,3-cyclodiketones enabled by structure-guided directed evolution of a carbonyl reductase
Xi Chen, Hongliu Zhang, Miguel A. Maria‐Solano, et al.
Nature Catalysis (2019) Vol. 2, Iss. 10, pp. 931-941
Closed Access | Times Cited: 83
Mechanism of allosteric activation of SIRT6 revealed by the action of rationally designed activators
Shaoyong Lu, Ying-Yi Chen, Jiacheng Wei, et al.
Acta Pharmaceutica Sinica B (2020) Vol. 11, Iss. 5, pp. 1355-1361
Open Access | Times Cited: 76
Designing better enzymes: Insights from directed evolution
H. Adrian Bunzel, J. L. Ross Anderson, Adrian J. Mulholland
Current Opinion in Structural Biology (2021) Vol. 67, pp. 212-218
Open Access | Times Cited: 74
Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases
Rory Crean, Michal Biler, Marc W. van der Kamp, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 10, pp. 3830-3845
Open Access | Times Cited: 67
Time Evolution of the Millisecond Allosteric Activation of Imidazole Glycerol Phosphate Synthase
Carla Calvó‐Tusell, Miguel A. Maria‐Solano, Sílvia Osuna, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 16, pp. 7146-7159
Open Access | Times Cited: 43
Engineered cytochrome P450 for direct arylalkene-to-ketone oxidation via highly reactive carbocation intermediates
Sebastian Gergel, Jordi Soler Soler, Alina Klein, et al.
Nature Catalysis (2023) Vol. 6, Iss. 7, pp. 606-617
Open Access | Times Cited: 33
Computational design of highly efficient thermostable MHET hydrolases and dual enzyme system for PET recycling
Jun Zhang, Hongzhao Wang, Zhaorong Luo, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 24
Conformational Selection of a Tryptophan Side Chain Drives the Generalized Increase in Activity of PET Hydrolases through a Ser/Ile Double Mutation
Alessandro Crnjar, Aransa Griñén, Shina Caroline Lynn Kamerlin, et al.
ACS Organic & Inorganic Au (2023) Vol. 3, Iss. 2, pp. 109-119
Open Access | Times Cited: 23
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