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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:

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

Showing 1-25 of 231 citing articles:

Recent advances in transition-metal-catalyzed carbene insertion to C–H bonds
Yuan He, Zilong Huang, Kaikai Wu, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 7, pp. 2759-2852
Closed Access | Times Cited: 209
From nature to industry: Harnessing enzymes for biocatalysis
Rebecca Buller, Stefan Lutz, Romas J. Kazlauskas, et al.
Science (2023) Vol. 382, Iss. 6673
Open Access | Times Cited: 169
Stereodivergent atom-transfer radical cyclization by engineered cytochromes P450
Qi Zhou, M. A. Chin, Yue Fu, et al.
Science (2021) Vol. 374, Iss. 6575, pp. 1612-1616
Open Access | Times Cited: 133
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: 133
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: 129
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
Stereoselective amino acid synthesis by synergistic photoredox-pyridoxal radical biocatalysis
Lei Cheng, Dian Li, Binh Khanh, et al.
Science (2023) Vol. 381, Iss. 6656, pp. 444-451
Open Access | Times Cited: 69
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
Using enzymes to tame nitrogen-centred radicals for enantioselective hydroamination
Yuxuan Ye, Jingzhe Cao, Daniel G. Oblinsky, et al.
Nature Chemistry (2022) Vol. 15, Iss. 2, pp. 206-212
Closed Access | Times Cited: 66
Machine learning for functional protein design
Pascal Notin, Nathan Rollins, Yarin Gal, et al.
Nature Biotechnology (2024) Vol. 42, Iss. 2, pp. 216-228
Closed 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
A light-driven enzymatic enantioselective radical acylation
Yuanyuan Xu, Hongwei Chen, Lu Yu, et al.
Nature (2023) Vol. 625, Iss. 7993, pp. 74-78
Closed Access | Times Cited: 55
Iron(III)-based metalloradical catalysis for asymmetric cyclopropanation via a stepwise radical mechanism
Wan-Chen Cindy Lee, Duo‐Sheng Wang, Yiling Zhu, et al.
Nature Chemistry (2023) Vol. 15, Iss. 11, pp. 1569-1580
Closed Access | Times Cited: 47
Biocatalytic amide bond formation
Max Lubberink, William Finnigan, Sabine L. Flitsch
Green Chemistry (2023) Vol. 25, Iss. 8, pp. 2958-2970
Open Access | Times Cited: 41
Asymmetric C-Alkylation of Nitroalkanes via Enzymatic Photoredox Catalysis
Haigen Fu, Tianzhang Qiao, J. M. Carceller, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 2, pp. 787-793
Open Access | Times Cited: 39
Design of Heme Enzymes with a Tunable Substrate Binding Pocket Adjacent to an Open Metal Coordination Site
Indrek Kalvet, Mary Ortmayer, Jingming Zhao, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 26, pp. 14307-14315
Open Access | Times Cited: 38
Iron- and Ruthenium-Catalyzed C–N Bond Formation Reactions. Reactive Metal Imido/Nitrene Intermediates
Yungen Liu, Ka‐Pan Shing, Vanessa Kar‐Yan Lo, et al.
ACS Catalysis (2023) Vol. 13, Iss. 2, pp. 1103-1124
Closed Access | Times Cited: 36
Enzymatic Assembly of Diverse Lactone Structures: An Intramolecular C–H Functionalization Strategy
Daniel J. Wackelin, Runze Mao, Kathleen M. Sicinski, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 2, pp. 1580-1587
Closed Access | Times Cited: 14
Machine learning-guided co-optimization of fitness and diversity facilitates combinatorial library design in enzyme engineering
Kerr Ding, M. A. Chin, Yunlong Zhao, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 13
Streamlining Design, Engineering, and Applications of Enzymes for Sustainable Biocatalysis
Roger A. Sheldon, Dean Brady
ACS Sustainable Chemistry & Engineering (2021) Vol. 9, Iss. 24, pp. 8032-8052
Closed Access | Times Cited: 76
Thioether-Directed NiH-Catalyzed Remote γ-C(sp3)–H Hydroamidation of Alkenes by 1,4,2-Dioxazol-5-ones
Bingnan Du, Yuxin Ouyang, Qishu Chen, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 37, pp. 14962-14968
Open Access | Times Cited: 75
An Enzymatic Platform for Primary Amination of 1-Aryl-2-alkyl Alkynes
Zhen Liu, Ziyang Qin, Ledong Zhu, et al.
Journal of the American Chemical Society (2021) Vol. 144, Iss. 1, pp. 80-85
Open Access | Times Cited: 61
Biocatalytic One-Carbon Ring Expansion of Aziridines to Azetidines via a Highly Enantioselective [1,2]-Stevens Rearrangement
David C. Miller, Ravi Lal, Luca Marchetti, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 11, pp. 4739-4745
Open Access | Times Cited: 53
Making Enzymes Suitable for Organic Chemistry by Rational Protein Design
Manfred T. Reetz
ChemBioChem (2022) Vol. 23, Iss. 14
Open Access | Times Cited: 50
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
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