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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:

Focused rational iterative site-specific mutagenesis (FRISM)
Danyang Li, Qi Wu, Manfred T. Reetz
Methods in enzymology on CD-ROM/Methods in enzymology (2020), pp. 225-242
Closed Access | Times Cited: 57

Showing 1-25 of 57 citing articles:

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 primer to directed evolution: current methodologies and future directions
Lara Sellés Vidal, Mark Isalan, John Heap, et al.
RSC Chemical Biology (2023) Vol. 4, Iss. 4, pp. 271-291
Open Access | Times Cited: 43
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: 75
Light-driven decarboxylative deuteration enabled by a divergently engineered photodecarboxylase
Jian Xu, Jiajie Fan, Yujiao Lou, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 65
Repertoire of Computationally Designed Peroxygenases for Enantiodivergent C–H Oxyfunctionalization Reactions
Patricia Gómez de Santos, Ivan Mateljak, Manh Dat Hoang, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 6, pp. 3443-3453
Open Access | Times Cited: 34
Rationally Controlling Selective Steroid Hydroxylation via Scaffold Sampling of a P450 Family
Xiaodong Zhang, Pan‐Pan Shen, Jing Zhao, et al.
ACS Catalysis (2023) Vol. 13, Iss. 2, pp. 1280-1289
Closed Access | Times Cited: 30
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: 22
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
Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles
Xinqi Xu, Fahui Xu, Jingjing Chen, et al.
International Journal of Biological Macromolecules (2025), pp. 139561-139561
Closed Access
Engineering Fatty Acid Photodecarboxylase to Enable Highly Selective Decarboxylation oftransFatty Acids
Danyang Li, Han Tao, Jiadan Xue, et al.
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 38, pp. 20695-20699
Closed Access | Times Cited: 49
Directed Evolution of a Plant Glycosyltransferase for Chemo- and Regioselective Glycosylation of Pharmaceutically Significant Flavonoids
Zexing Wen, Zhimin Zhang, Liang Zhong, et al.
ACS Catalysis (2021) Vol. 11, Iss. 24, pp. 14781-14790
Closed Access | Times Cited: 43
Engineering P450 Monooxygenases for Highly Regioselective and Active p-Hydroxylation of m-Alkylphenols
Ren‐Jie Li, Kaiyuan Tian, Xirui Li, et al.
ACS Catalysis (2022) Vol. 12, Iss. 10, pp. 5939-5948
Closed Access | Times Cited: 28
From Semirational to Rational Design: Developing a Substrate-Coupled System of Glucose Dehydrogenase for Asymmetric Synthesis
Qipeng Yan, Xinhua Zhang, Yingzhuang Chen, et al.
ACS Catalysis (2022) Vol. 12, Iss. 11, pp. 6746-6755
Closed Access | Times Cited: 27
Bioprospecting of microbial enzymes: current trends in industry and healthcare
Eswar Rao Tatta, Madangchanok Imchen, Jamseel Moopantakath, et al.
Applied Microbiology and Biotechnology (2022) Vol. 106, Iss. 5-6, pp. 1813-1835
Closed Access | Times Cited: 26
Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review
Bei Ouyang, Guoping Wang, Nian Zhang, et al.
Molecules (2023) Vol. 28, Iss. 13, pp. 4990-4990
Open Access | Times Cited: 18
In silico design of multipoint mutants for enhanced performance of Thermomyces lanuginosus lipase for efficient biodiesel production
Jinsha Huang, Xiaoman Xie, Wanlin Zheng, et al.
Biotechnology for Biofuels and Bioproducts (2024) Vol. 17, Iss. 1
Open Access | Times Cited: 5
Switching an Artificial P450 Peroxygenase into Peroxidase via Mechanism-Guided Protein Engineering
Nana Ma, Wenhan Fang, Chuanfei Liu, et al.
ACS Catalysis (2021) Vol. 11, Iss. 14, pp. 8449-8455
Closed Access | Times Cited: 35
Photoenzymatic decarboxylation: A promising way to produce sustainable aviation fuels and fine chemicals
Xiaobo Guo, Ao Xia, Wuyuan Zhang, et al.
Bioresource Technology (2022) Vol. 367, pp. 128232-128232
Closed Access | Times Cited: 24
N-terminal truncation (N-) and directional proton transfer in an old yellow enzyme enables tunable efficient producing (R)- or (S)-citronellal
Jie Zhang, Yueshu Li, Hui Gao, et al.
International Journal of Biological Macromolecules (2024) Vol. 262, pp. 130129-130129
Closed Access | Times Cited: 3
Directed Evolution of Artificial Metalloenzymes in Whole Cells
Yang Gu, Brandon J. Bloomer, Zhennan Liu, et al.
Angewandte Chemie International Edition (2021) Vol. 61, Iss. 5
Open Access | Times Cited: 26
Rational design of fatty acid photodecarboxylase enables the efficient decarboxylation of medium- and short-chain fatty acids for the production of gasoline bio-alkanes
Weihua Xu, Yang Chen, Danyang Li, et al.
Molecular Catalysis (2022) Vol. 524, pp. 112261-112261
Closed Access | Times Cited: 18
Engineering substrate specificity of HAD phosphatases and multienzyme systems development for the thermodynamic-driven manufacturing sugars
Chaoyu Tian, Jiangang Yang, Cui Liu, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 18
Structure function relationships in plant UDP-glycosyltransferases
Jinbo Yao, Xiaowen Xing, Luyao Yu, et al.
Industrial Crops and Products (2022) Vol. 189, pp. 115784-115784
Closed Access | Times Cited: 18
Methods for enzyme library creation: Which one will you choose?
Lorea Alejaldre, Joelle N. Pelletier, Daniela Quaglia
BioEssays (2021) Vol. 43, Iss. 8
Open Access | Times Cited: 25
Witnessing the Birth of Directed Evolution of Stereoselective Enzymes as Catalysts in Organic Chemistry
Manfred T. Reetz
Advanced Synthesis & Catalysis (2022) Vol. 364, Iss. 19, pp. 3326-3335
Open Access | Times Cited: 16
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