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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:

The importance of catalytic promiscuity for enzyme design and evolution
Reuben B. Leveson‐Gower, Clemens Mayer, Gérard Roelfes
Nature Reviews Chemistry (2019) Vol. 3, Iss. 12, pp. 687-705
Closed Access | Times Cited: 255

Showing 1-25 of 255 citing articles:

Navigating the Unnatural Reaction Space: Directed Evolution of Heme Proteins for Selective Carbene and Nitrene Transfer
Yang Yang, Frances H. Arnold
Accounts of Chemical Research (2021) Vol. 54, Iss. 5, pp. 1209-1225
Open Access | Times Cited: 231
Exploiting attractive non-covalent interactions for the enantioselective catalysis of reactions involving radical intermediates
Rupert S. J. Proctor, Avene C. Colgan, Robert J. Phipps
Nature Chemistry (2020) Vol. 12, Iss. 11, pp. 990-1004
Open Access | Times Cited: 170
Single-atom nanozymes catalytically surpassing naturally occurring enzymes as sustained stitching for brain trauma
Shaofang Zhang, Yonghui Li, Si Sun, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 159
Iron- and cobalt-catalyzed C(sp3)–H bond functionalization reactions and their application in organic synthesis
Yungen Liu, Tingjie You, Haixu Wang, et al.
Chemical Society Reviews (2020) Vol. 49, Iss. 15, pp. 5310-5358
Closed Access | Times Cited: 158
Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere
Casey Van Stappen, Yunling Deng, Yiwei Liu, et al.
Chemical Reviews (2022) Vol. 122, Iss. 14, pp. 11974-12045
Open Access | Times Cited: 96
Microbial enzymes will offer limited solutions to the global plastic pollution crisis
Jennifer Chow, Pablo Pérez-García, Robert F. Dierkes, et al.
Microbial Biotechnology (2022) Vol. 16, Iss. 2, pp. 195-217
Open Access | Times Cited: 68
Systems chemistry of peptide-assemblies for biochemical transformations
Ayan Chatterjee, Antara Reja, Sumit Pal, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 8, pp. 3047-3070
Closed Access | Times Cited: 65
Opportunities and Challenges for Machine Learning-Assisted Enzyme Engineering
Jason Yang, Francesca-Zhoufan Li, Frances H. Arnold
ACS Central Science (2024) Vol. 10, Iss. 2, pp. 226-241
Open Access | Times Cited: 51
Direct visible-light-excited flavoproteins for redox-neutral asymmetric radical hydroarylation
Beibei Zhao, Jianqiang Feng, Lu Yu, et al.
Nature Catalysis (2023) Vol. 6, Iss. 11, pp. 996-1004
Closed Access | Times Cited: 36
Boron catalysis in a designer enzyme
Lars Longwitz, Reuben B. Leveson‐Gower, H.J. Rozeboom, et al.
Nature (2024) Vol. 629, Iss. 8013, pp. 824-829
Closed Access | Times Cited: 19
Bioorthogonal Cu Single‐atom Nanozyme for Synergistic Nanocatalytic Therapy, Photothermal Therapy, Cuproptosis, and Immunotherapy
Luyan Wu, Huihui Lin, Xiang Cao, et al.
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 27
Closed Access | Times Cited: 17
Biocatalytic enantioselective C(sp3)–H fluorination enabled by directed evolution of non-haem iron enzymes
Liupeng Zhao, Binh Khanh, Lida Cheng, et al.
Nature Synthesis (2024) Vol. 3, Iss. 8, pp. 967-975
Closed Access | Times Cited: 15
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: 111
Recent Advances in Biocatalysis with Chemical Modification and Expanded Amino Acid Alphabet
Amol D. Pagar, Mahesh D. Patil, Dillon T. Flood, et al.
Chemical Reviews (2021) Vol. 121, Iss. 10, pp. 6173-6245
Closed Access | Times Cited: 91
Chance emergence of catalytic activity and promiscuity in a self-replicator
Jim Ottelé, Andreas S. Hussain, Clemens Mayer, et al.
Nature Catalysis (2020) Vol. 3, Iss. 7, pp. 547-553
Open Access | Times Cited: 82
De novo metalloprotein design
Matthew J. Chalkley, Samuel I. Mann, William F. DeGrado
Nature Reviews Chemistry (2021) Vol. 6, Iss. 1, pp. 31-50
Open Access | Times Cited: 79
Scalable continuous evolution for the generation of diverse enzyme variants encompassing promiscuous activities
Gordon Rix, Ella J. Watkins‐Dulaney, Patrick J. Almhjell, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 78
Engineering Cytochrome P450s for Enantioselective Cyclopropenation of Internal Alkynes
Kai Chen, Frances H. Arnold
Journal of the American Chemical Society (2020) Vol. 142, Iss. 15, pp. 6891-6895
Open Access | Times Cited: 77
In Vivo Assembly of Artificial Metalloenzymes and Application in Whole‐Cell Biocatalysis**
Shreyans Chordia, Siddarth Narasimhan, Alessandra Lucini Paioni, et al.
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 11, pp. 5913-5920
Open Access | Times Cited: 71
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
Development of a versatile and efficient C–N lyase platform for asymmetric hydroamination via computational enzyme redesign
Yinglu Cui, Yinghui Wang, Wenya Tian, et al.
Nature Catalysis (2021) Vol. 4, Iss. 5, pp. 364-373
Open Access | Times Cited: 57
Making Enzymes Suitable for Organic Chemistry by Rational Protein Design
Manfred T. Reetz
ChemBioChem (2022) Vol. 23, Iss. 14
Open Access | Times Cited: 50
Enzyme-controlled stereoselective radical cyclization to arenes enabled by metalloredox biocatalysis
Wen‐Zhen Fu, Natalia M. Neris, Yue Fu, et al.
Nature Catalysis (2023) Vol. 6, Iss. 7, pp. 628-636
Closed Access | Times Cited: 29
An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
Pablo Pérez-García, Jennifer Chow, Elisa Costanzi, et al.
Communications Chemistry (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 26
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: 10
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