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:

Stereodivergent Protein Engineering of a Lipase To Access All Possible Stereoisomers of Chiral Esters with Two Stereocenters
Jian Xu, Yixin Cen, Warispreet Singh, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 19, pp. 7934-7945
Open Access | Times Cited: 143

Showing 1-25 of 143 citing articles:

Directed Evolution: Methodologies and Applications
Yajie Wang, Pu Xue, Mingfeng Cao, et al.
Chemical Reviews (2021) Vol. 121, Iss. 20, pp. 12384-12444
Closed Access | Times Cited: 394

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: 387

Enantioselective [2+2]-cycloadditions with triplet photoenzymes
Ningning Sun, Jianjian Huang, Junyi Qian, et al.
Nature (2022) Vol. 611, Iss. 7937, pp. 715-720
Closed Access | Times Cited: 114

Photoinduced chemomimetic biocatalysis for enantioselective intermolecular radical conjugate addition
Xiaoqiang Huang, Jianqiang Feng, Jiawen Cui, et al.
Nature Catalysis (2022) Vol. 5, Iss. 7, pp. 586-593
Closed Access | Times Cited: 79

Thermal stability enhancement: Fundamental concepts of protein engineering strategies to manipulate the flexible structure
Mahdie Rahban, Samaneh Zolghadri, Najmeh Salehi, et al.
International Journal of Biological Macromolecules (2022) Vol. 214, pp. 642-654
Closed Access | Times Cited: 69

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

Design of novel enzyme biocatalysts for industrial bioprocess: Harnessing the power of protein engineering, high throughput screening and synthetic biology
Aravind Madhavan, K. B. Arun, Parameswaran Binod, et al.
Bioresource Technology (2020) Vol. 325, pp. 124617-124617
Closed Access | Times Cited: 105

Stereodivergent Carbon–Carbon Bond Formation between Iminium and Enolate Intermediates by Synergistic Organocatalysis
Byungjun Kim, Yong‐Jae Kim, Sarah Yunmi Lee
Journal of the American Chemical Society (2020) Vol. 143, Iss. 1, pp. 73-79
Closed Access | Times Cited: 104

Current perspectives for microbial lipases from extremophiles and metagenomics
Swati Verma, Gautam Kumar Meghwanshi, Rajender Kumar
Biochimie (2021) Vol. 182, pp. 23-36
Open Access | Times Cited: 90

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: 89

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

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

Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET
Rita P. Magalhães, Jorge M. Cunha, Sérgio F. Sousa
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 20, pp. 11257-11257
Open Access | Times Cited: 68

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

Unlocking the Stereoselectivity and Substrate Acceptance of Enzymes: Proline‐Induced Loop Engineering Test
Ge Qu, Yuexin Bi, Beibei Liu, et al.
Angewandte Chemie International Edition (2021) Vol. 61, Iss. 1
Closed Access | Times Cited: 64

Predicting enzymatic reactions with a molecular transformer
David Kreutter, Philippe Schwaller, Jean‐Louis Reymond
Chemical Science (2021) Vol. 12, Iss. 25, pp. 8648-8659
Open Access | Times Cited: 60

Enabling highly (R)-enantioselective epoxidation of styrene by engineering unique non-natural P450 peroxygenases
Panxia Zhao, Jie Chen, Nana Ma, et al.
Chemical Science (2021) Vol. 12, Iss. 18, pp. 6307-6314
Open Access | Times Cited: 54

Making Enzymes Suitable for Organic Chemistry by Rational Protein Design
Manfred T. Reetz
ChemBioChem (2022) Vol. 23, Iss. 14
Open Access | Times Cited: 50

E/Z Photoisomerization of Olefins as an Emergent Strategy for the Control of Stereodivergence in Catalysis
Javier Corpas, Pablo Mauleón, Ramón Goméz Arrayás, et al.
Advanced Synthesis & Catalysis (2022) Vol. 364, Iss. 8, pp. 1348-1370
Open Access | Times Cited: 41

Tuning an Imine Reductase for the Asymmetric Synthesis of Azacycloalkylamines by Concise Structure‐Guided Engineering
Jun Zhang, Daohong Liao, Rongchang Chen, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 24
Closed Access | Times Cited: 37

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

Solvent tolerant enzymes in extremophiles: Adaptations and applications
Bhavtosh A. Kikani, Rajesh Patel, Jignasha T. Thumar, et al.
International Journal of Biological Macromolecules (2023) Vol. 238, pp. 124051-124051
Closed Access | Times Cited: 22

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

Emerging Strategies for Modifying Cytochrome P450 Monooxygenases into Peroxizymes
Shengxian Fan, Zhiqi Cong
Accounts of Chemical Research (2024)
Closed Access | Times Cited: 11

Enzyme engineering for biocatalysis
Caroline E. Paul, Ulf Hanefeld, Frank Hollmann, et al.
Molecular Catalysis (2024) Vol. 555, pp. 113874-113874
Open Access | Times Cited: 9

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