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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:

Structural insight into the substrate specificity of PLP fold type IV transaminases
Ekaterina Yu. Bezsudnova, Vladimir O. Popov, Konstantin M. Boyko
Applied Microbiology and Biotechnology (2020) Vol. 104, Iss. 6, pp. 2343-2357
Closed Access | Times Cited: 42

Showing 1-25 of 42 citing articles:

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: 20
Engineering an ω-transaminase for chemoenzymatically synthesizing key intermediate 5-hydroxymethyl-2-furfurylamine
Heng Yang, J. H. Jiang, Cuiluan Ma, et al.
Fuel (2025) Vol. 388, pp. 134429-134429
Closed 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
Structure and Cooperativity in Substrate–Enzyme Interactions: Perspectives on Enzyme Engineering and Inhibitor Design
Eerappa Rajakumara, Suman Abhishek, Kulhar Nitin, et al.
ACS Chemical Biology (2022) Vol. 17, Iss. 2, pp. 266-280
Closed Access | Times Cited: 22
Non-Canonical Amino Acid-Based Engineering of (R)-Amine Transaminase
Amol D. Pagar, Hyunwoo Jeon, Taresh P. Khobragade, et al.
Frontiers in Chemistry (2022) Vol. 10
Open Access | Times Cited: 18
To the Understanding of Catalysis by D-Amino Acid Transaminases: A Case Study of the Enzyme from Aminobacterium colombiense
Sofia A. Shilova, Maria G. Khrenova, Ilya O. Matyuta, et al.
Molecules (2023) Vol. 28, Iss. 5, pp. 2109-2109
Open Access | Times Cited: 9
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
The Uncommon Active Site of D-Amino Acid Transaminase from Haliscomenobacter hydrossis: Biochemical and Structural Insights into the New Enzyme
Alina K. Bakunova, A.Y. Nikolaeva, Tatiana V. Rakitina, et al.
Molecules (2021) Vol. 26, Iss. 16, pp. 5053-5053
Open Access | Times Cited: 22
Shifting the pH Optima of (R)-Selective Transaminases by Protein Engineering
Chao Xiang, Yu‐Fei Ao, Matthias Höhne, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 23, pp. 15347-15347
Open Access | Times Cited: 15
Pocket Modification of ω-Amine Transaminase AtATA for Overcoming the Trade-Off Between Activity and Stability Toward 1-Acetonaphthone
Jia-Ren Cao, Fangfang Fan, Changjiang Lyu, et al.
Engineering (2023) Vol. 30, pp. 203-214
Open Access | Times Cited: 8
Structural Basis for Allostery in PLP-dependent Enzymes
Jenny U. Tran, Breann L. Brown
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 11
Expanding the Toolbox of R‐Selective Amine Transaminases by Identification and Characterization of New Members
Aline Telzerow, Juraj Paris, M. Håkansson, et al.
ChemBioChem (2020) Vol. 22, Iss. 7, pp. 1232-1242
Open Access | Times Cited: 17
Creation of a (R)-β-Transaminase by Directed Evolution of d-Amino Acid Aminotransferase
Hyunwoo Jeon, Amol D. Pagar, Hyeona Kang, et al.
ACS Catalysis (2022) Vol. 12, Iss. 21, pp. 13207-13214
Closed Access | Times Cited: 9
Asymmetric Synthesis of Enantiomerically Pure Aliphatic and Aromatic D-Amino Acids Catalyzed by Transaminase from Haliscomenobacter hydrossis
Alina K. Bakunova, Tatiana Y. Isaikina, Vladimir O. Popov, et al.
Catalysts (2022) Vol. 12, Iss. 12, pp. 1551-1551
Open Access | Times Cited: 8
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 | 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
Biochemical and Structural Characterization of an (R)‐Selective Transaminase in the Asymmetric Synthesis of Chiral Hydroxy Amines
Fulong Li, Youxiang Liang, Yuwen Wei, et al.
Advanced Synthesis & Catalysis (2021) Vol. 363, Iss. 19, pp. 4582-4589
Closed Access | Times Cited: 10
Redesign of (R)-Omega-Transaminase and Its Application for Synthesizing Amino Acids with Bulky Side Chain
Dongxu Jia, Peng Chen, Junliang Li, et al.
Applied Biochemistry and Biotechnology (2021) Vol. 193, Iss. 11, pp. 3624-3640
Closed Access | Times Cited: 10
Rational engineering ofLuminiphilus syltensis(R)-selective amine transaminase for the acceptance of bulky substrates
Eleni Konia, Constantinos Chatzicharalampous, Athina Drakonaki, et al.
Chemical Communications (2021) Vol. 57, Iss. 96, pp. 12948-12951
Open Access | Times Cited: 10
In search for structural targets for engineering d-amino acid transaminase: modulation of pH optimum and substrate specificity
Sofia A. Shilova, Ilya O. Matyuta, Maria G. Khrenova, et al.
Biochemical Journal (2023) Vol. 480, Iss. 16, pp. 1267-1284
Open Access | Times Cited: 3
Designing a novel (R)-ω-transaminase for asymmetric synthesis of sitagliptin intermediate via motif swapping and semi-rational design
Fang-Ying Zhu, Mengyu Huang, Ken Zheng, et al.
International Journal of Biological Macromolecules (2023) Vol. 253, pp. 127348-127348
Closed Access | Times Cited: 3
Stereoselective synthesis of (R)-(+)−1-(1-naphthyl)ethylamine by ω-amine transaminase immobilized on amino modified multi-walled carbon nanotubes and biocatalyst recycling
Shuai Qiu, Yu-Tong Cui, Tongtong Wang, et al.
Enzyme and Microbial Technology (2023) Vol. 174, pp. 110378-110378
Closed Access | Times Cited: 3
Construction and Application of PLP Self-sufficient Biocatalysis System for Threonine Aldolase
Wenlong Zheng, Kaitong Chen, Sai Fang, et al.
Enzyme and Microbial Technology (2020) Vol. 141, pp. 109667-109667
Closed Access | Times Cited: 8
Effects of pH and temperature on (S)-amine activity of transaminase from the cold-adapted bacterium Psychrobacter cryohalolentis
Ekaterina Yu. Bezsudnova, Tatiana N. Stekhanova, Aleksandr O. Ruzhitskiy, et al.
Extremophiles (2020) Vol. 24, Iss. 4, pp. 537-549
Closed Access | Times Cited: 7
Efficient Synthesis of Key Chiral Intermediate in Painkillers (R)-1-[3,5-Bis(trifluoromethyl)phenyl]ethanamine by Bienzyme Cascade System with R-ω-Transaminase and Alcohol Dehydrogenase Functions
Lu Yuan, Jinmei Wang, Haobo Xu, et al.
Molecules (2022) Vol. 27, Iss. 21, pp. 7331-7331
Open Access | Times Cited: 4
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