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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:

Structure‐ and Data‐Driven Protein Engineering of Transaminases for Improving Activity and Stereoselectivity
Yu‐Fei Ao, Shuxin Pei, Chao Xiang, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 23
Open Access | Times Cited: 17

Showing 17 citing articles:

Accelerated enzyme engineering by machine-learning guided cell-free expression
Grant M. Landwehr, Jonathan W. Bogart, Carol Magalhaes, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
Accelerating Biocatalysis Discovery with Machine Learning: A Paradigm Shift in Enzyme Engineering, Discovery, and Design
Braun Markus, Gruber Christian C, Krassnigg Andreas, et al.
ACS Catalysis (2023) Vol. 13, Iss. 21, pp. 14454-14469
Open Access | Times Cited: 29
Guide to serial synchrotron crystallography
Ki Hyun Nam
Current Research in Structural Biology (2024) Vol. 7, pp. 100131-100131
Open Access | Times Cited: 8
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: 7
Structural Basis of High-Precision Protein Ligation and Its Application
Kelvin Han Chung Chong, Lichao Liu, Rae Chua, et al.
Journal of the American Chemical Society (2025)
Closed Access
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: 19
Engineering the next-generation synthetic cell factory driven by protein engineering
Ailin Guan, Zixi He, Xin Wang, et al.
Biotechnology Advances (2024) Vol. 73, pp. 108366-108366
Closed Access | Times Cited: 4
Enhanced stereodivergent evolution of carboxylesterase for efficient kinetic resolution of near-symmetric esters through machine learning
Guochao Xu, Zhe Dou, Xuanzao Chen, et al.
Research Square (Research Square) (2024)
Open Access | Times Cited: 3
Multifunctionality of arginine residues in the active sites of non-canonical d-amino acid transaminases
Alina K. Bakunova, Ilya O. Matyuta, Mikhail E. Minyaev, et al.
Archives of Biochemistry and Biophysics (2024) Vol. 756, pp. 110011-110011
Closed Access | Times Cited: 3
Understanding the stability of a plastic‐degrading Rieske iron oxidoreductase system
Jessica Lusty Beech, Anjani K. Maurya, Ronivaldo Rodrigues da Silva, et al.
Protein Science (2024) Vol. 33, Iss. 6
Open Access | Times Cited: 2
Cutting-edge Computational Approaches in Enzyme Design and Activity Enhancement
Ruobin Sun, Dan Wu, Pengcheng Chen, et al.
Biochemical Engineering Journal (2024) Vol. 212, pp. 109510-109510
Closed Access | Times Cited: 2
Advancing microbial production through artificial intelligence-aided biology
Xinyu Gong, Jianli Zhang, Qi Gan, et al.
Biotechnology Advances (2024) Vol. 74, pp. 108399-108399
Closed Access | Times Cited: 1
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: 1
Enhanced stereodivergent evolution of carboxylesterase for efficient kinetic resolution of near-symmetric esters through machine learning
Zhe Dou, Xuanzao Chen, Ledong Zhu, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 1
Reprogramming biocatalytic futile cycles through computational engineering of stereochemical promiscuity to create an amine racemase
Sang‐Woo Han, Youngho Jang, Jihyun Kook, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access
Exemplifying Natural (R)-β-Transamination Potential of Fold Type-IV Transaminase for Kinetic Resolution of rac-β-Amino Acids Synthesized from Aldehydes
Amol D. Pagar, Taresh P. Khobragade, Pritam Giri, et al.
ACS Sustainable Chemistry & Engineering (2024) Vol. 12, Iss. 19, pp. 7226-7234
Closed Access
Application of Directed Evolution and Machine Learning to Enhance the Diastereoselectivity of Ketoreductase for Dihydrotetrabenazine Synthesis
Chenming Huang, Li Zhang, Tong Tang, et al.
JACS Au (2024) Vol. 4, Iss. 7, pp. 2547-2556
Open Access
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