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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:

Building Enzymes through Design and Evolution
Euan J. Hossack, Florence J. Hardy, Anthony P. Green
ACS Catalysis (2023) Vol. 13, Iss. 19, pp. 12436-12444
Open Access | Times Cited: 31

Showing 1-25 of 31 citing articles:

Microbes Saving Lives and Reducing Suffering
Kenneth N. Timmis, Zeynep Ceren Karahan, Juan L. Ramos, et al.
Microbial Biotechnology (2025) Vol. 18, Iss. 1
Open Access | Times Cited: 3
A non-canonical nucleophile unlocks a new mechanistic pathway in a designed enzyme
Amy E. Hutton, Jake Foster, Rebecca Crawshaw, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 12
Practical Machine Learning-Assisted Design Protocol for Protein Engineering: Transaminase Engineering for the Conversion of Bulky Substrates
Marian J. Menke, Yu‐Fei Ao, Uwe T. Bornscheuer
ACS Catalysis (2024) Vol. 14, Iss. 9, pp. 6462-6469
Closed Access | Times Cited: 11
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: 8
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: 21
Transition Path Sampling Study of Engineered Enzymes That Catalyze the Morita–Baylis–Hillman Reaction: Why Is Enzyme Design so Difficult?
Sree Ganesh Balasubramani, Kseniia Korchagina, Steven D. Schwartz
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 6, pp. 2101-2111
Closed Access | Times Cited: 5
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: 5
Screening Adaptive Microbial Hydrolytic Enzymes for Cleaner Production in Resource-Limited Settings
Tunjung Mahatmanto
Industrial Biotechnology (2025)
Closed Access
Excellent Laccase Mimic Activity of Cu-Melamine and Its Applications in the Degradation of Congo Red
Siyuan Chai, Enze Huang, Jinsheng Zeng, et al.
Applied Biochemistry and Biotechnology (2025)
Open Access
Computer-Aided Design for Enhancing the Tolerance of Ω-Amine Transaminase Against Methanol as a Cosolvent
Jun Huang, Shuai Qiu, Tong Wang, et al.
(2025)
Closed Access
Rational Design of d-hydantoinase from Pseudomonas aeruginosa for Desymmetric Synthesis of Chiral Intermediate for S-Pregabalin
Feixia Liu, Hongxia Zhao, Zhongdong Shang, et al.
Green Carbon (2025)
Open Access
Noncanonical Amino Acids: Bringing New-to-Nature Functionalities to Biocatalysis
Bart Brouwer, Franco Della‐Felice, Jan Hendrik Illies, et al.
Chemical Reviews (2024) Vol. 124, Iss. 19, pp. 10877-10923
Open Access | Times Cited: 4
Revolutionizing Molecular Design for Innovative Therapeutic Applications through Artificial Intelligence
Ahrum Son, Jongham Park, Woojin Kim, et al.
Molecules (2024) Vol. 29, Iss. 19, pp. 4626-4626
Open Access | Times Cited: 4
Using residue interaction networks to understand protein function and evolution and to engineer new proteins
Dariia Yehorova, Bruno Di Geronimo, Michael Robinson, et al.
Current Opinion in Structural Biology (2024) Vol. 89, pp. 102922-102922
Open Access | Times Cited: 3
Machine learning-assisted amidase-catalytic enantioselectivity prediction and rational design of variants for improving enantioselectivity
Zi-Lin Li, Shuxin Pei, Ziying Chen, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 3
Enzymatic synthesis of chiral alcohols using ketoreductases
Quan Yuan, Li Ma, Weixi Kong, et al.
Catalysis Reviews (2024), pp. 1-40
Closed Access | Times Cited: 2
Computational Design of Metallohydrolases
Donghyo Kim, Seth M. Woodbury, Woody Ahern, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2
Discovery and application of food catalysts to promote the coupling of PQQ (quinone) with amines
Kazuto Ikemoto, Satoko Imaruoka, Nur Syafiqah Mohamad Ishak
Frontiers in Nutrition (2024) Vol. 11
Open Access | Times Cited: 1
Evolving ω-amine transaminase At ATA guided by substrate-enzyme binding free energy for enhancing activity and stability against non-natural substrates
Shuai Qiu, Cong-Lin Ju, Tong Wang, et al.
Applied and Environmental Microbiology (2024) Vol. 90, Iss. 7
Closed Access | Times Cited: 1
Creation and optimization of artificial metalloenzymes: Harnessing the power of directed evolution and beyond
Zhi Zou, Bradley Higginson, Thomas R. Ward
Chem (2024) Vol. 10, Iss. 8, pp. 2373-2389
Open Access | Times Cited: 1
Chemical tongues as multipurpose bioanalytical tools for the characterization of complex biological samples
Shunsuke Tomita, Hiroka Sugai
Biophysics and Physicobiology (2024) Vol. 21, Iss. 3, pp. n/a-n/a
Open Access | Times Cited: 1
MetaEnzyme: Meta Pan-Enzyme Learning for Task-Adaptive Redesign
Jiangbin Zheng, Han Zhang, Qianqing Xu, et al.
(2024), pp. 1721-1730
Open Access | Times Cited: 1
Strategies in engineering sustainable biochemical synthesis through microbial systems
Yoseb Song, Kristala L. J. Prather
Current Opinion in Chemical Biology (2024) Vol. 81, pp. 102493-102493
Closed Access
Deep Learning-Based Self-Adaptive Evolution of Enzymes
Shuiqin Jiang, Dong Yi
Pharmaceutical Fronts (2024) Vol. 06, Iss. 03, pp. e252-e264
Open Access
Reaching New Heights in Genetic Code Manipulation with High Throughput Screening
Briana R. Lino, Sean Williams, Michelle E. Castor, et al.
Chemical Reviews (2024) Vol. 124, Iss. 21, pp. 12145-12175
Closed Access
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