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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:

How to Engineer Organic Solvent Resistant Enzymes: Insights from Combined Molecular Dynamics and Directed Evolution Study
Haiyang Cui, Tom H. J. Stadtmüller, Qianjia Jiang, et al.
ChemCatChem (2020) Vol. 12, Iss. 16, pp. 4073-4083
Open Access | Times Cited: 58

Showing 1-25 of 58 citing articles:

Power of Biocatalysis for Organic Synthesis
Christoph K. Winkler, Joerg H. Schrittwieser, Wolfgang Kroutil
ACS Central Science (2021) Vol. 7, Iss. 1, pp. 55-71
Open Access | Times Cited: 272
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Haiyang Cui, Lobna Eltoukhy, Lingling Zhang, et al.
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 20, pp. 11448-11456
Open Access | Times Cited: 54
Computer-aided engineering of lipases solvent tolerance enhanced their applications in sugar esters synthesis: State of the art
Qi Yuan, Mei Chen, Tongtong Jin, et al.
Trends in Food Science & Technology (2024) Vol. 144, pp. 104323-104323
Closed Access | Times Cited: 8
Protein Engineering for Industrial Biocatalysis: Principles, Approaches, and Lessons from Engineered PETases
Konstantinos Grigorakis, Christina Ferousi, Evangelos Topakas
Catalysts (2025) Vol. 15, Iss. 2, pp. 147-147
Open Access
Enzyme Hydration Determines Resistance in Organic Cosolvents
Haiyang Cui, Lingling Zhang, Lobna Eltoukhy, et al.
ACS Catalysis (2020) Vol. 10, Iss. 24, pp. 14847-14856
Closed Access | Times Cited: 63
Ionic liquids for regulating biocatalytic process: Achievements and perspectives
Pei Xu, Shan Liang, Min‐Hua Zong, et al.
Biotechnology Advances (2021) Vol. 51, pp. 107702-107702
Closed Access | Times Cited: 53
Polar Substitutions on the Surface of a Lipase Substantially Improve Tolerance in Organic Solvents
Haiyang Cui, Markus Vedder, Lingling Zhang, et al.
ChemSusChem (2022) Vol. 15, Iss. 9
Open Access | Times Cited: 26
Harnessing solvation-guided engineering to enhance deep eutectic solvent resistance and thermostability in enzymes
Yijie Sheng, Haiyang Cui, Xinyue Wang, et al.
Green Chemistry (2024) Vol. 26, Iss. 16, pp. 9132-9141
Closed Access | Times Cited: 5
Is water the best solvent for biocatalysis?
Dirk Holtmann, Frank Hollmann
Molecular Catalysis (2021) Vol. 517, pp. 112035-112035
Open Access | Times Cited: 35
Understanding the activity of glucose oxidase after exposure to organic solvents
Vygailė Dudkaitė, Visvaldas Kairys, Gintautas Bagdžiūnas
Journal of Materials Chemistry B (2023) Vol. 11, Iss. 11, pp. 2409-2416
Open Access | Times Cited: 12
CompassR Yields Highly Organic‐Solvent‐Tolerant Enzymes through Recombination of Compatible Substitutions
Haiyang Cui, Karl‐Erich Jaeger, Mehdi D. Davari, et al.
Chemistry - A European Journal (2020) Vol. 27, Iss. 8, pp. 2789-2797
Open Access | Times Cited: 35
CompassR-guided recombination unlocks design principles to stabilize lipases in ILs with minimal experimental efforts
Haiyang Cui, Subrata Pramanik, Karl‐Erich Jaeger, et al.
Green Chemistry (2021) Vol. 23, Iss. 9, pp. 3474-3486
Closed Access | Times Cited: 29
Efficient enzyme-catalyzed production of diosgenin: inspired by the biotransformation mechanisms of steroid saponins in Talaromyces stollii CLY-6
Leiyu Cheng, Han Zhang, Haiyang Cui, et al.
Green Chemistry (2021) Vol. 23, Iss. 16, pp. 5896-5910
Closed Access | Times Cited: 27
A novel α-L-Rhamnosidase renders efficient and clean production of icaritin
Leiyu Cheng, Han Zhang, Haiyang Cui, et al.
Journal of Cleaner Production (2022) Vol. 341, pp. 130903-130903
Closed Access | Times Cited: 20
How Does Surface Charge Engineering of Bacillus subtilis Lipase A Improve Ionic Liquid Resistance? Lessons Learned from Molecular Dynamics Simulations
Subrata Pramanik, Haiyang Cui, Gaurao V. Dhoke, et al.
ACS Sustainable Chemistry & Engineering (2022) Vol. 10, Iss. 8, pp. 2689-2698
Closed Access | Times Cited: 20
Effect of Organic Solvents on the Structure and Activity of a Minimal Lipase
Kim N. Ingenbosch, Julio Cesar Vieyto-Nuñez, Yasser B. Ruiz‐Blanco, et al.
The Journal of Organic Chemistry (2021) Vol. 87, Iss. 3, pp. 1669-1678
Closed Access | Times Cited: 23
Evolving Robust and Interpretable Enzymes for the Bioethanol Industry
Jie Qiao, Yijie Sheng, Minghui Wang, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 12
Closed Access | Times Cited: 9
Biological valorization of lignin-derived vanillin to vanillylamine by recombinant E. coli expressing ω-transaminase and alanine dehydrogenase in a petroleum ether-water system
Lei Li, Cuiluan Ma, Haoyu Chai, et al.
Bioresource Technology (2023) Vol. 385, pp. 129453-129453
Closed Access | Times Cited: 8
Engineering All-Round Cellulase for Bioethanol Production
Minghui Wang, Haiyang Cui, Chenlei Gu, et al.
ACS Synthetic Biology (2023) Vol. 12, Iss. 7, pp. 2187-2197
Closed Access | Times Cited: 8
Unraveling the potential of uninvestigated thermoalkaliphilic lipases by molecular docking and molecular dynamic simulation: an in silico characterization study
Havva Esra Tütüncü, Naciye Durmuş İşleyen, Yusuf Sürmeli
3 Biotech (2024) Vol. 14, Iss. 7
Closed Access | Times Cited: 2
Enhancing the organic solvent resistance of ω‐amine transaminase for enantioselective synthesis of (R)‐(+)‐1(1‐naphthyl)‐ethylamine
Chunning Wang, Shuai Qiu, Fangfang Fan, et al.
Biotechnology Journal (2023) Vol. 18, Iss. 10
Closed Access | Times Cited: 7
Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art
Wenjun Cheng, Binbin Nian
Molecules (2023) Vol. 28, Iss. 15, pp. 5848-5848
Open Access | Times Cited: 7
Lipase A from Bacillus subtilis: Substrate Binding, Conformational Dynamics, and Signatures of a Lid
Sudarshan Behera, Sundaram Balasubramanian
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 23, pp. 7545-7556
Closed Access | Times Cited: 7
A green pathway for lignin valorization: Enzymatic lignin depolymerization in biocompatible ionic liquids and deep eutectic solvents
Enshi Liu, M. Mercado, Fernando Segato, et al.
Enzyme and Microbial Technology (2023) Vol. 174, pp. 110392-110392
Closed Access | Times Cited: 7
Aqueous ionic liquids redistribute local enzyme stability via long-range perturbation pathways
Till El Harrar, Benedikt Frieg, Mehdi D. Davari, et al.
Computational and Structural Biotechnology Journal (2021) Vol. 19, pp. 4248-4264
Open Access | Times Cited: 16
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