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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:

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: 168

Showing 26-50 of 168 citing articles:

Biocatalytic enantioselective formation and ring-opening of oxetanes
Xia Hua, Yuanfei Wang, Xiao Jin, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Ground-state flavin-dependent enzymes catalyzed enantioselective radical trifluoromethylation
Xinyu Duan, Dong Cui, Mengdi Wang, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Salt-driven dynamic folding of halophile-origin enzymes: Insights into evolution and protein exploitation
Yu‐Ke Cen, Lin Zhang, M Liu, et al.
International Journal of Biological Macromolecules (2025), pp. 140527-140527
Closed Access
Single-Layer MnO2 Nanosheets for Immobilization of Agrobacterium radiobacter Halohydrin Dehalogenase via Adsorption
Kongliang Xu, Yi Tian, Hongpeng Pan, et al.
ACS Applied Nano Materials (2025)
Closed Access
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
Effective engineering of a ketoreductase for the biocatalytic synthesis of an ipatasertib precursor
Sumire Honda Malca, Nadine Duss, Jasmin Meierhofer, et al.
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 5
Reshaping Phosphatase Substrate Preference for Controlled Biosynthesis Using a “Design–Build–Test–Learn” Framework
Jiangong Lu, Xueqin Lv, Wenwen Yu, et al.
Advanced Science (2024) Vol. 11, Iss. 22
Open Access | Times Cited: 5
Immobilized Multi‐Enzyme/Nanozyme Biomimetic Cascade Catalysis for Biosensing Applications
Xiaoli Cai, Yuteng Huang, Chengzhou Zhu
Advanced Healthcare Materials (2024)
Closed Access | Times Cited: 5
Cryptic enzymatic assembly of peptides armed with β-lactone warheads
Guangcai Xu, Daniele Torri, Sebastian Cuesta-Hoyos, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 10, pp. 1371-1379
Open Access | Times Cited: 5
A De Novo Metalloenzyme for Cerium Photoredox Catalysis
Andreas Klein, Florian Leiss-Maier, Rahel Mühlhofer, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 38, pp. 25976-25985
Open Access | Times Cited: 5
A de novo metalloenzyme for cerium photoredox catalysis
Andreas Klein, Florian Leiss-Maier, Rahel Mühlhofer, et al.
(2024)
Open Access | Times Cited: 4
The Impact of Metagenomics on Biocatalysis
Bethany N. Hogg, Christian Schnepel, James Finnigan, et al.
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 21
Open Access | Times Cited: 4
Microdroplet screening rapidly profiles a biocatalyst to enable its AI-assisted engineering
Maximilian Gantz, Simon V. Mathis, Friederike E. H. Nintzel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Computation-guided engineering of distal mutations in an artificial enzyme
Fabrizio Casilli, Miquel Canyelles-Niño, Gérard Roelfes, et al.
Faraday Discussions (2024) Vol. 252, pp. 262-278
Open Access | Times Cited: 4
An In Vitro Hybrid Biocatalytic System Enabled by a Combination of Surface-Displayed, Purified, and Cell-Free Expressed Enzymes
Ying Liu, Shuhui Huang, Wan‐Qiu Liu, et al.
ACS Synthetic Biology (2024) Vol. 13, Iss. 5, pp. 1434-1441
Closed Access | Times Cited: 4
Computational design of highly active de novo enzymes
M. J. BRAUN, Adrian Tripp, Morakot Chakatok, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Rational enzyme design by reducing the number of hotspots and library size
Zongmin Qin, Bo Yuan, Ge Qu, et al.
Chemical Communications (2024) Vol. 60, Iss. 76, pp. 10451-10463
Closed Access | Times Cited: 4
Enhancing the Imine Reductase Activity of a Promiscuous Glucose Dehydrogenase for Scalable Manufacturing of a Chiral Neprilysin Inhibitor Precursor
Xiang Yi, Florian Kleinbeck, Charlene Ching, et al.
ACS Catalysis (2024) Vol. 14, Iss. 9, pp. 7087-7096
Closed Access | Times Cited: 4
Biocatalytic Regio‐ and Enantiocomplementary Synthesis of Chiral Aryloxazolidinones
Xiaoying Zhou, Yuanfei Wang, Hong‐Kang Fu, et al.
Advanced Synthesis & Catalysis (2024) Vol. 366, Iss. 11, pp. 2461-2467
Closed Access | Times Cited: 3
Directed Evolution and Immobilization of Lactobacillus brevis Alcohol Dehydrogenase for Chemo‐Enzymatic Synthesis of Rivastigmine
Guorong Su, Ran Lu, Chang Liu, et al.
Chemistry - A European Journal (2024) Vol. 30, Iss. 32
Closed Access | Times Cited: 3
The Development and Opportunities of Predictive Biotechnology
Bettina M. Nestl, Bernd A. Nebel, Verena Resch, et al.
ChemBioChem (2024) Vol. 25, Iss. 13
Open Access | Times Cited: 3
Divergent Protein Engineering of Transaminase for the Synthesis of Chiral Rivastigmine and Apremilast Precursors†
Langyu Tang, Xinjie Yang, Ningning Sun, et al.
Chinese Journal of Chemistry (2024) Vol. 42, Iss. 19, pp. 2335-2340
Closed Access | Times Cited: 3
A refined picture of the native amine dehydrogenase family revealed by extensive biodiversity screening
Eddy Elisée, Laurine Ducrot, Raphaël Méheust, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 3
Deciphering the Key Loop: Enhancing l-Threonine Transaldolase’s Catalytic Potential
Zhiwen Xi, Jingxin Rao, Xinyi Zhang, et al.
ACS Catalysis (2024) Vol. 14, Iss. 14, pp. 10462-10474
Closed Access | Times Cited: 3
Atroposelective Synthesis of Axial Biaryls by Dynamic Kinetic Resolution Using Engineered Imine Reductases
Xinyue Hao, Zhuangfei Tian, Zhouchang Yao, et al.
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 41
Closed Access | Times Cited: 3

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