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:

Computational redesign of enzymes for regio- and enantioselective hydroamination
Ruifeng Li, Hein J. Wijma, Song Lu, et al.
Nature Chemical Biology (2018) Vol. 14, Iss. 7, pp. 664-670
Closed Access | Times Cited: 172

Showing 1-25 of 172 citing articles:

Biocatalysis: Enzymatic Synthesis for Industrial Applications
Shuke Wu, Radka Šnajdrová, Jeffrey C. Moore, et al.
Angewandte Chemie International Edition (2020) Vol. 60, Iss. 1, pp. 88-119
Open Access | Times Cited: 1065

Computational Redesign of a PETase for Plastic Biodegradation under Ambient Condition by the GRAPE Strategy
Yinglu Cui, Yanchun Chen, Xinyue Liu, et al.
ACS Catalysis (2021) Vol. 11, Iss. 3, pp. 1340-1350
Closed Access | Times Cited: 437

The Crucial Role of Methodology Development in Directed Evolution of Selective Enzymes
Ge Qu, Aitao Li, Carlos G. Acevedo‐Rocha, et al.
Angewandte Chemie International Edition (2019) Vol. 59, Iss. 32, pp. 13204-13231
Closed Access | Times Cited: 399

Broadening the Scope of Biocatalysis in Sustainable Organic Synthesis
Roger A. Sheldon, Dean Brady
ChemSusChem (2019) Vol. 12, Iss. 13, pp. 2859-2881
Closed Access | Times Cited: 275

Embracing Nature’s Catalysts: A Viewpoint on the Future of Biocatalysis
Bernhard Hauer
ACS Catalysis (2020) Vol. 10, Iss. 15, pp. 8418-8427
Closed Access | Times Cited: 236

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: 207

Recognition in the Domain of Molecular Chirality: From Noncovalent Interactions to Separation of Enantiomers
Paola Peluso, Bezhan Chankvetadze
Chemical Reviews (2022) Vol. 122, Iss. 16, pp. 13235-13400
Closed Access | Times Cited: 170

Rational design of enzyme activity and enantioselectivity
Zhongdi Song, Qunfeng Zhang, Wenhui Wu, et al.
Frontiers in Bioengineering and Biotechnology (2023) Vol. 11
Open Access | Times Cited: 68

Opportunities of CO2-based biorefineries for production of fuels and chemicals
Zihe Liu, Shuobo Shi, Yuchao Ji, et al.
Green Carbon (2023) Vol. 1, Iss. 1, pp. 75-84
Open Access | Times Cited: 52

Enantioselective Transformations in the Synthesis of Therapeutic Agents
Yang He, Hanxiao Yu, I. Stolarzewicz, et al.
Chemical Reviews (2023) Vol. 123, Iss. 15, pp. 9397-9446
Closed Access | Times Cited: 43

Engineering enzymes for noncanonical amino acid synthesis
Patrick J. Almhjell, Christina Smith, Frances H. Arnold
Chemical Society Reviews (2018) Vol. 47, Iss. 24, pp. 8980-8997
Open Access | Times Cited: 140

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

Cofactor-free oxidase-mimetic nanomaterials from self-assembled histidine-rich peptides
Qing Liu, Kaiwei Wan, Yingxu Shang, et al.
Nature Materials (2020) Vol. 20, Iss. 3, pp. 395-402
Closed Access | Times Cited: 112

Biokatalyse: Enzymatische Synthese für industrielle Anwendungen
Shuke Wu, Radka Šnajdrová, Jeffrey C. Moore, et al.
Angewandte Chemie (2020) Vol. 133, Iss. 1, pp. 89-123
Open Access | Times Cited: 94

Modeling Enzymatic Enantioselectivity using Quantum Chemical Methodology
Xiang Sheng, Masoud Kazemi, Ferran Planas, et al.
ACS Catalysis (2020) Vol. 10, Iss. 11, pp. 6430-6449
Open Access | Times Cited: 91

Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase
Vasilis Tseliou, Tanja Knaus, Marcelo F. Masman, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 84

Near-perfect control of the regioselective glucosylation enabled by rational design of glycosyltransferases
Jiao Li, Ge Qu, Na Shang, et al.
Green Synthesis and Catalysis (2021) Vol. 2, Iss. 1, pp. 45-53
Open Access | Times Cited: 79

Machine-Directed Evolution of an Imine Reductase for Activity and Stereoselectivity
J Gilbert Eric, Elina Siirola, Charles M. Moore, et al.
ACS Catalysis (2021) Vol. 11, Iss. 20, pp. 12433-12445
Closed Access | Times Cited: 78

Enzymatic strategies for asymmetric synthesis
Mélanie Hall
RSC Chemical Biology (2021) Vol. 2, Iss. 4, pp. 958-989
Open Access | Times Cited: 66

SYNBIP: synthetic binding proteins for research, diagnosis and therapy
Xiaona Wang, Fengcheng Li, Wenqi Qiu, et al.
Nucleic Acids Research (2021) Vol. 50, Iss. D1, pp. D560-D570
Open 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: 62

A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values
Roberto Morellon‐Sterling, Olga Luisa Tavano, Juan M. Bolívar, et al.
International Journal of Biological Macromolecules (2022) Vol. 210, pp. 682-702
Open Access | Times Cited: 50

Focused rational iterative site-specific mutagenesis (FRISM): A powerful method for enzyme engineering
Yuyan Bao, Yuanyuan Xu, Xiaoqiang Huang
Molecular Catalysis (2023) Vol. 553, pp. 113755-113755
Closed Access | Times Cited: 25

Unlocking the potential of enzyme engineering via rational computational design strategies
Lei Zhou, Chunmeng Tao, Xiaolin Shen, et al.
Biotechnology Advances (2024) Vol. 73, pp. 108376-108376
Closed Access | Times Cited: 15

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