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:

Combining chemistry and protein engineering for new-to-nature biocatalysis
David C. Miller, Soumitra V. Athavale, Frances H. Arnold
Nature Synthesis (2022) Vol. 1, Iss. 1, pp. 18-23
Open Access | Times Cited: 128

Showing 1-25 of 128 citing articles:

The E factor at 30: a passion for pollution prevention
Roger A. Sheldon
Green Chemistry (2023) Vol. 25, Iss. 5, pp. 1704-1728
Open Access | Times Cited: 125

Biocatalysis as Key to Sustainable Industrial Chemistry
Andrés R. Alcántara, Pablo Domı́nguez de Marı́a, Jennifer A. Littlechild, et al.
ChemSusChem (2022) Vol. 15, Iss. 9
Open Access | Times Cited: 100

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: 95

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: 67

Enzymatic Nitrogen Insertion into Unactivated C–H Bonds
Soumitra V. Athavale, Shilong Gao, Anuvab Das, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 41, pp. 19097-19105
Open Access | Times Cited: 66

Engineered enzymes for the synthesis of pharmaceuticals and other high-value products
Manfred T. Reetz, Ge Qu, Zhoutong Sun
Nature Synthesis (2024) Vol. 3, Iss. 1, pp. 19-32
Closed Access | Times Cited: 58

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

Photoenzymatic enantioselective intermolecular radical hydroamination
Zhengyi Zhang, Jianqiang Feng, Chao Yang, et al.
Nature Catalysis (2023) Vol. 6, Iss. 8, pp. 687-694
Open Access | Times Cited: 43

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

Charting the Evolution of Chemoenzymatic Strategies in the Syntheses of Complex Natural Products
Carter N. Stout, Nour Wasfy, Fang Chen, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 33, pp. 18161-18181
Closed Access | Times Cited: 24

Deep Electroreductive Chemistry: Harnessing Carbon- and Silicon-Based Reactive Intermediates in Organic Synthesis
Wen Zhang, Weiyang Guan, Jesus I. Martinez Alvarado, et al.
ACS Catalysis (2023) Vol. 13, Iss. 12, pp. 8038-8048
Open Access | Times Cited: 23

Data‐Driven Protein Engineering for Improving Catalytic Activity and Selectivity
Yu‐Fei Ao, Mark Dörr, Marian J. Menke, et al.
ChemBioChem (2023) Vol. 25, Iss. 3
Open Access | Times Cited: 19

Green chemistry and biocatalysis: Engineering a sustainable future
Roger A. Sheldon
Catalysis Today (2024) Vol. 431, pp. 114571-114571
Closed Access | Times Cited: 11

Learning from Protein Engineering by Deconvolution of Multi‐Mutational Variants
Frank Hollmann, Joaquin Sanchis, Manfred T. Reetz
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 36
Open Access | Times Cited: 10

Enzymatic Stereodivergent Access to Fluorinated β-Lactam Pharmacophores via Triple-Parameter Engineered Ketoreductases
Ze-Long Mei, Congcong Li, Xu Han, et al.
ACS Catalysis (2024) Vol. 14, Iss. 8, pp. 6358-6368
Closed Access | Times Cited: 9

Semirational Design Based on Consensus Sequences to Balance the Enzyme Activity-Stability Trade-Off
Yang Zhao, Kun Chen, Haixia Yang, et al.
Journal of Agricultural and Food Chemistry (2024) Vol. 72, Iss. 12, pp. 6454-6462
Closed Access | Times Cited: 7

Practical Machine Learning-Assisted Design Protocol for Protein Engineering: Transaminase Engineering for the Conversion of Bulky Substrates
Marian J. Menke, Yu‐Fei Ao, Uwe T. Bornscheuer
ACS Catalysis (2024) Vol. 14, Iss. 9, pp. 6462-6469
Closed Access | Times Cited: 7

Developing BioNavi for Hybrid Retrosynthesis Planning
Tao Zeng, Zhehao Jin, Shuangjia Zheng, et al.
JACS Au (2024) Vol. 4, Iss. 7, pp. 2492-2502
Open Access | Times Cited: 7

A parallel bioreactor strategy to rapidly determine growth-coupling relationships for bioproduction: a mevalonate case study
Alec Banner, Joseph P. Webb, Nigel S. Scrutton
Biotechnology for Biofuels and Bioproducts (2025) Vol. 18, Iss. 1
Open Access

Exploiting Enzymes: Technology and Applications
Narayan S. Punekar
(2025), pp. 501-523
Closed Access

Engineered P450 Atom-Transfer Radical Cyclases are Bifunctional Biocatalysts: Reaction Mechanism and Origin of Enantioselectivity
Yue Fu, Heyu Chen, Wen‐Zhen Fu, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 29, pp. 13344-13355
Open Access | Times Cited: 30

A Photoenzymatic Strategy for Radical‐Mediated Stereoselective Hydroalkylation with Diazo Compounds
Xinyu Duan, Dong Cui, Zhiguo Wang, et al.
Angewandte Chemie International Edition (2022) Vol. 62, Iss. 5
Closed Access | Times Cited: 29

Ultrahigh-Throughput Directed Evolution of a Metal-Free α/β-Hydrolase with a Cys-His-Asp Triad into an Efficient Phosphotriesterase
J. David Schnettler, Oskar James Klein, Tomasz S. Kamiński, et al.
Journal of the American Chemical Society (2022) Vol. 145, Iss. 2, pp. 1083-1096
Open Access | Times Cited: 28

Catalytic, asymmetric carbon–nitrogen bond formation using metal nitrenoids: from metal–ligand complexes via metalloporphyrins to enzymes
Alexander Fanourakis, Robert J. Phipps
Chemical Science (2023) Vol. 14, Iss. 44, pp. 12447-12476
Open Access | Times Cited: 18

Structure‐ and Data‐Driven Protein Engineering of Transaminases for Improving Activity and Stereoselectivity
Yu‐Fei Ao, Shuxin Pei, Chao Xiang, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 23
Open Access | Times Cited: 17

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