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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:
Automated Design of Efficient and Functionally Diverse Enzyme Repertoires
Olga Khersonsky, Rosalie Lipsh‐Sokolik, Ziv Avizemer, et al.
Molecular Cell (2018) Vol. 72, Iss. 1, pp. 178-186.e5
Open Access | Times Cited: 219
Olga Khersonsky, Rosalie Lipsh‐Sokolik, Ziv Avizemer, et al.
Molecular Cell (2018) Vol. 72, Iss. 1, pp. 178-186.e5
Open Access | Times Cited: 219
Showing 1-25 of 219 citing articles:
Machine learning-assisted directed protein evolution with combinatorial libraries
Zachary Wu, S. B. Jennifer Kan, Russell D. Lewis, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 18, pp. 8852-8858
Open Access | Times Cited: 492
Zachary Wu, S. B. Jennifer Kan, Russell D. Lewis, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 18, pp. 8852-8858
Open Access | Times Cited: 492
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
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
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: 231
Bernhard Hauer
ACS Catalysis (2020) Vol. 10, Iss. 15, pp. 8418-8427
Closed Access | Times Cited: 231
Automated in Silico Design of Homogeneous Catalysts
Marco Foscato, Vidar R. Jensen
ACS Catalysis (2020) Vol. 10, Iss. 3, pp. 2354-2377
Open Access | Times Cited: 172
Marco Foscato, Vidar R. Jensen
ACS Catalysis (2020) Vol. 10, Iss. 3, pp. 2354-2377
Open Access | Times Cited: 172
Engineering cytokine therapeutics
Jeroen Deckers, Tom Anbergen, Ayla M. Hokke, et al.
Nature Reviews Bioengineering (2023) Vol. 1, Iss. 4, pp. 286-303
Open Access | Times Cited: 103
Jeroen Deckers, Tom Anbergen, Ayla M. Hokke, et al.
Nature Reviews Bioengineering (2023) Vol. 1, Iss. 4, pp. 286-303
Open Access | Times Cited: 103
Machine Learning-Guided Protein Engineering
Petr Kouba, Pavel Kohout, Faraneh Haddadi, et al.
ACS Catalysis (2023) Vol. 13, Iss. 21, pp. 13863-13895
Open Access | Times Cited: 65
Petr Kouba, Pavel Kohout, Faraneh Haddadi, et al.
ACS Catalysis (2023) Vol. 13, Iss. 21, pp. 13863-13895
Open Access | Times Cited: 65
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
Manfred T. Reetz, Ge Qu, Zhoutong Sun
Nature Synthesis (2024) Vol. 3, Iss. 1, pp. 19-32
Closed Access | Times Cited: 58
Combinatorial assembly and design of enzymes
Rosalie Lipsh‐Sokolik, Olga Khersonsky, Sybrin P. Schröder, et al.
Science (2023) Vol. 379, Iss. 6628, pp. 195-201
Open Access | Times Cited: 55
Rosalie Lipsh‐Sokolik, Olga Khersonsky, Sybrin P. Schröder, et al.
Science (2023) Vol. 379, Iss. 6628, pp. 195-201
Open Access | Times Cited: 55
Opportunities and Challenges for Machine Learning-Assisted Enzyme Engineering
Jason Yang, Francesca-Zhoufan Li, Frances H. Arnold
ACS Central Science (2024) Vol. 10, Iss. 2, pp. 226-241
Open Access | Times Cited: 51
Jason Yang, Francesca-Zhoufan Li, Frances H. Arnold
ACS Central Science (2024) Vol. 10, Iss. 2, pp. 226-241
Open Access | Times Cited: 51
Recent advances in the biocatalytic mitigation of emerging pollutants: A comprehensive review
Bernard Chukwuemeka Ekeoma, Leonard Nnamdi Ekeoma, Mohammad Yusuf, et al.
Journal of Biotechnology (2023) Vol. 369, pp. 14-34
Closed Access | Times Cited: 44
Bernard Chukwuemeka Ekeoma, Leonard Nnamdi Ekeoma, Mohammad Yusuf, et al.
Journal of Biotechnology (2023) Vol. 369, pp. 14-34
Closed Access | Times Cited: 44
Joint Generation of Protein Sequence and Structure with RoseTTAFold Sequence Space Diffusion
Sidney Lyayuga Lisanza, Jake Merle Gershon, S. Tipps, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 36
Sidney Lyayuga Lisanza, Jake Merle Gershon, S. Tipps, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 36
Opportunities and challenges in design and optimization of protein function
Dina Listov, Casper A. Goverde, Bruno E. Correia, et al.
Nature Reviews Molecular Cell Biology (2024) Vol. 25, Iss. 8, pp. 639-653
Closed Access | Times Cited: 33
Dina Listov, Casper A. Goverde, Bruno E. Correia, et al.
Nature Reviews Molecular Cell Biology (2024) Vol. 25, Iss. 8, pp. 639-653
Closed Access | Times Cited: 33
Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development
Kwangho Nam, Yihan Shao, Dan Thomas Major, et al.
ACS Omega (2024)
Open Access | Times Cited: 15
Kwangho Nam, Yihan Shao, Dan Thomas Major, et al.
ACS Omega (2024)
Open Access | Times Cited: 15
Machine learning-guided co-optimization of fitness and diversity facilitates combinatorial library design in enzyme engineering
Kerr Ding, M. A. Chin, Yunlong Zhao, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 13
Kerr Ding, M. A. Chin, Yunlong Zhao, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 13
Enzymatic Bioremediation of Organophosphate Compounds—Progress and Remaining Challenges
Meghna Thakur, Igor L. Medintz, Scott A. Walper
Frontiers in Bioengineering and Biotechnology (2019) Vol. 7
Open Access | Times Cited: 119
Meghna Thakur, Igor L. Medintz, Scott A. Walper
Frontiers in Bioengineering and Biotechnology (2019) Vol. 7
Open Access | Times Cited: 119
Protein engineers turned evolutionists—the quest for the optimal starting point
Devin L. Trudeau, Dan S. Tawfik
Current Opinion in Biotechnology (2019) Vol. 60, pp. 46-52
Open Access | Times Cited: 115
Devin L. Trudeau, Dan S. Tawfik
Current Opinion in Biotechnology (2019) Vol. 60, pp. 46-52
Open Access | Times Cited: 115
Design and in vitro realization of carbon-conserving photorespiration
Devin L. Trudeau, Christian Edlich‐Muth, Jan Zarzycki, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 49
Open Access | Times Cited: 111
Devin L. Trudeau, Christian Edlich‐Muth, Jan Zarzycki, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 49
Open Access | Times Cited: 111
Harnessing Conformational Plasticity to Generate Designer Enzymes
Rory Crean, Jasmine M. Gardner, Shina Caroline Lynn Kamerlin
Journal of the American Chemical Society (2020) Vol. 142, Iss. 26, pp. 11324-11342
Open Access | Times Cited: 111
Rory Crean, Jasmine M. Gardner, Shina Caroline Lynn Kamerlin
Journal of the American Chemical Society (2020) Vol. 142, Iss. 26, pp. 11324-11342
Open Access | Times Cited: 111
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: 108
Sílvia Osuna
Wiley Interdisciplinary Reviews Computational Molecular Science (2020) Vol. 11, Iss. 3
Open Access | Times Cited: 108
Optimizing antibody affinity and stability by the automated design of the variable light-heavy chain interfaces
Shira Warszawski, A. Katz, Rosalie Lipsh‐Sokolik, et al.
PLoS Computational Biology (2019) Vol. 15, Iss. 8, pp. e1007207-e1007207
Open Access | Times Cited: 93
Shira Warszawski, A. Katz, Rosalie Lipsh‐Sokolik, et al.
PLoS Computational Biology (2019) Vol. 15, Iss. 8, pp. e1007207-e1007207
Open Access | Times Cited: 93
Engineering Robust Cellulases for Tailored Lignocellulosic Degradation Cocktails
Francisca Contreras, Subrata Pramanik, А. М. Рожкова, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 5, pp. 1589-1589
Open Access | Times Cited: 91
Francisca Contreras, Subrata Pramanik, А. М. Рожкова, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 5, pp. 1589-1589
Open Access | Times Cited: 91
The evolution of phosphotriesterase for decontamination and detoxification of organophosphorus chemical warfare agents
Andrew N. Bigley, Frank M. Raushel
Chemico-Biological Interactions (2019) Vol. 308, pp. 80-88
Open Access | Times Cited: 80
Andrew N. Bigley, Frank M. Raushel
Chemico-Biological Interactions (2019) Vol. 308, pp. 80-88
Open Access | Times Cited: 80
Protein engineering: the potential of remote mutations
Matthew Wilding, Nansook Hong, Matthew A. Spence, et al.
Biochemical Society Transactions (2019) Vol. 47, Iss. 2, pp. 701-711
Open Access | Times Cited: 79
Matthew Wilding, Nansook Hong, Matthew A. Spence, et al.
Biochemical Society Transactions (2019) Vol. 47, Iss. 2, pp. 701-711
Open Access | Times Cited: 79
Engineered Enzymes Enable Selective N‐Alkylation of Pyrazoles With Simple Haloalkanes
Ludwig L. Bengel, Benjamin Aberle, Alexander‐N. Egler‐Kemmerer, et al.
Angewandte Chemie International Edition (2020) Vol. 60, Iss. 10, pp. 5554-5560
Open Access | Times Cited: 69
Ludwig L. Bengel, Benjamin Aberle, Alexander‐N. Egler‐Kemmerer, et al.
Angewandte Chemie International Edition (2020) Vol. 60, Iss. 10, pp. 5554-5560
Open Access | Times Cited: 69
Computational enzyme redesign: large jumps in function
Yinglu Cui, Jinyuan Sun, Bian Wu
Trends in Chemistry (2022) Vol. 4, Iss. 5, pp. 409-419
Closed Access | Times Cited: 36
Yinglu Cui, Jinyuan Sun, Bian Wu
Trends in Chemistry (2022) Vol. 4, Iss. 5, pp. 409-419
Closed Access | Times Cited: 36