OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Epistasis arises from shifting the rate-limiting step during enzyme evolution of a β-lactamase
Christopher Fröhlich, H. Adrian Bunzel, Karol Buda, et al.
Nature Catalysis (2024) Vol. 7, Iss. 5, pp. 499-509
Open Access | Times Cited: 12

Showing 12 citing articles:

Sparse modeling of interactions enables fast detection of genome-wide epistasis in biobank-scale studies
Julian Stamp, Samuel Pattillo Smith, Daniel Weinreich, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access | Times Cited: 1

A combinatorially complete epistatic fitness landscape in an enzyme active site
Kadina E. Johnston, Patrick J. Almhjell, Ella J. Watkins‐Dulaney, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 32
Open Access | Times Cited: 8

Tailoring industrial enzymes for thermostability and activity evolution by the machine learning-based iCASE strategy
Nan Zheng, Yongchao Cai, Zehua Zhang, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access

Active learning-assisted directed evolution
Jason Yang, Ravi Lal, James C. Bowden, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access

Electric Fields Are a Key Determinant of Carbapenemase Activity in Class A β-Lactamases
Hira Jabeen, Michael Beer, James Spencer, et al.
ACS Catalysis (2024) Vol. 14, Iss. 9, pp. 7166-7172
Open Access | Times Cited: 4

Active Learning-Assisted Directed Evolution
Jason Yang, Ravi Lal, James C. Bowden, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 3

Dynamical Responses Predict a Distal Site that Modulates Activity in an Antibiotic Resistance Enzyme
Michael Beer, A. Sofia F. Oliveira, Catherine L. Tooke, et al.
Chemical Science (2024)
Open Access | Times Cited: 1

Order matters in evolution
Gina Dotta, Alejandro J. Vila
Nature Catalysis (2024) Vol. 7, Iss. 5, pp. 467-468
Closed Access | Times Cited: 1

Mechanism-Guided Computational Design Drives meso-Diaminopimelate Dehydrogenase to Efficient Synthesis of Aromatic d-amino Acids
Tianfu Wu, Yihan Chen, Wanqing Wei, et al.
ACS Synthetic Biology (2024) Vol. 13, Iss. 6, pp. 1879-1892
Closed Access | Times Cited: 1

Concluding remarks: biocatalysis
Uwe T. Bornscheuer
Faraday Discussions (2024) Vol. 252, pp. 507-515
Open Access

Nature’s Toolbox for the Hydrolysis of Lactams and Cyclic Imides
Peter Stockinger, Rebecca Buller
ACS Catalysis (2024) Vol. 14, Iss. 21, pp. 16055-16073
Open Access

Structural comparison of substrate-binding pockets of serine β-lactamases in classes A, C, and D
Hyeonmin Lee, Hyunjae Park, Kiwoong Kwak, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry (2024) Vol. 40, Iss. 1
Open Access

Page 1

Scroll to top