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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:

Transaminases and their Applications
Sarah‐Marie Dold, Christoph Syldatk, Jens Rudat
(2016), pp. 715-746
Closed Access | Times Cited: 13

Showing 13 citing articles:

Discovery, Engineering, and Synthetic Application of Transaminase Biocatalysts
Iustina Slabu, James L. Galman, Richard C. Lloyd, et al.
ACS Catalysis (2017) Vol. 7, Iss. 12, pp. 8263-8284
Open Access | Times Cited: 310
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
Improvement in the Thermostability of a β‐Amino Acid Converting ω‐Transaminase by Using FoldX
O. Buß, Delphine Muller, Sven Jäger, et al.
ChemBioChem (2017) Vol. 19, Iss. 4, pp. 379-387
Open Access | Times Cited: 36
Donor Amine Salt‐Based Continuous in situ‐Product Crystallization in Amine Transaminase‐Catalyzed Reactions
Dennis Hülsewede, Jan‐Niklas Dohm, Jan von Langermann
Advanced Synthesis & Catalysis (2019) Vol. 361, Iss. 11, pp. 2727-2733
Open Access | Times Cited: 20
Integration of ion exchange resin materials for a downstream‐processing approach of an imine reductase‐catalyzed reaction
Lars‐Erik Meyer, Henrike Brundiek, Jan von Langermann
Biotechnology Progress (2020) Vol. 36, Iss. 5
Open Access | Times Cited: 12
Engineering of Reductive Aminases for Asymmetric Synthesis of Enantiopure Rasagiline
Kai Zhang, Yuanzhi He, Jiawei Zhu, et al.
Frontiers in Bioengineering and Biotechnology (2021) Vol. 9
Open Access | Times Cited: 5
Identification, Heterologous Expression and Characterization of a Transaminase from Rhizobium sp.
Kexin Tang, Yunfei Yi, Zhen Gao, et al.
Catalysis Letters (2020) Vol. 150, Iss. 8, pp. 2415-2426
Closed Access | Times Cited: 4
The Promising Role of Amine Transaminase Cascades in the Synthesis of Non-Canonical Amino Acids
Najme Gord Noshahri, Jens Rudat
Processes (2024) Vol. 12, Iss. 11, pp. 2566-2566
Open Access
Growth optimization and identification of an ω-transaminase by a novel native PAGE activity staining method in a Bacillus sp. strain BaH isolated from Iranian soil
Najme Gord Noshahri, Jamshid Fooladi, Ulrike Engel, et al.
AMB Express (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 2
Engineering ofωTransaminase for Effective Production of Chiral Amines
Mitra Mirzaei, Per Berglund
Journal of Computational and Theoretical Nanoscience (2020) Vol. 17, Iss. 6, pp. 2827-2832
Closed Access | Times Cited: 1
Prospects of Application of D-amino Acid Transaminase from Aminobacterium colombiense for (R)-selective Amination of α‑Keto Acids
Sofia A. Shilova, Tatiana V. Rakitina, Vladimir O. Popov, et al.
Moscow University Chemistry Bulletin (2023) Vol. 78, Iss. 1, pp. 10-19
Closed Access
PROSPECTS OF APPLICATION OF D-AMINO ACID TRANSAMINASE FROM AMINOBACTERIUM COLOMBIENSE FOR (R)-SELECTIVE AMINATION OF α-KETOACIDS
Sofia A. Shilova, Tatiana V. Rakitin, Vladimir O. Popov, et al.
Lomonosov chemistry journal (2023) Vol. 64, Iss. №2, 2023, pp. 85-98
Open Access
Transaminases
Birgit Kosjek
(2020), pp. 165-191
Closed Access
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