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:

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

Showing 26-50 of 69 citing articles:

Recent advances in biocatalytic C–N bond-forming reactions
Hong-Ning Yin, Pengcheng Wang, Zhen Liu
Bioorganic Chemistry (2024) Vol. 144, pp. 107108-107108
Closed Access | Times Cited: 2

Utopia Point Bayesian Optimization Finds Condition-Dependent Selectivity for N-Methyl Pyrazole Condensation
Derek M. Dalton, Richard C. Walroth, Caroline Rouget-Virbel, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 23, pp. 15779-15786
Open Access | Times Cited: 2

Addressing epistasis in the design of protein function
Rosalie Lipsh‐Sokolik, Sarel J. Fleishman
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 34
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

From Natural Methylation to Versatile Alkylations Using Halide Methyltransferases
Qingyun Tang, Ιoannis V. Pavlidis, Christoffel P. S. Badenhorst, et al.
ChemBioChem (2021) Vol. 22, Iss. 16, pp. 2584-2590
Open Access | Times Cited: 21

What Have We Learned from Design of Function in Large Proteins?
Olga Khersonsky, Sarel J. Fleishman
BioDesign Research (2022) Vol. 2022
Open Access | Times Cited: 14

Rational and mechanistic approaches for improving biocatalyst performance
Aisaraphon Phintha, Pimchai Chaiyen
Chem Catalysis (2022) Vol. 2, Iss. 10, pp. 2614-2643
Open Access | Times Cited: 13

Curse and Blessing of Non‐Proteinogenic Parts in Computational Enzyme Engineering
Kerlen T. Korbeld, Maximilian J. L. J. Fürst
ChemBioChem (2023) Vol. 24, Iss. 12
Open Access | Times Cited: 6

Biocatalytic Alkylation Chemistry: Building Molecular Complexity with High Selectivity
Felipe Ospina, Kai H. Schülke, Stephan C. Hammer
ChemPlusChem (2021) Vol. 87, Iss. 1
Open Access | Times Cited: 14

N-Trifluoropropylation of Azoles through N-Vinylation and Sequential Hydrogenation
Shujie Chen, Jiahui Li, Zhiqing He, et al.
The Journal of Organic Chemistry (2022) Vol. 87, Iss. 22, pp. 15703-15712
Closed Access | Times Cited: 10

Scalable Atroposelective Synthesis of MRTX1719: An Inhibitor of the PRMT5/MTA Complex
Michał Achmatowicz, Thomas Scattolin, David R. Snead, et al.
Organic Process Research & Development (2023) Vol. 27, Iss. 5, pp. 954-971
Open Access | Times Cited: 5

Regioselective N-Trideuteromethylation of Tautomeric Polyaza Heterocycles
Zhang Jian-xin, Bowen Lei, Mingrui Qin, et al.
The Journal of Organic Chemistry (2024) Vol. 89, Iss. 11, pp. 7780-7789
Closed Access | Times Cited: 1

Enzymkatalysierte späte Modifizierungen: Besser spät als nie
Elvira Romero, Bethan S. Jones, Bethany N. Hogg, et al.
Angewandte Chemie (2021) Vol. 133, Iss. 31, pp. 16962-16993
Open Access | Times Cited: 12

Expanding the Substrate Scope of N‐ and O‐Methyltransferases from Plants for Chemoselective Alkylation**
Emely Jockmann, Fabiana Subrizi, Michael K. F. Mohr, et al.
ChemCatChem (2023) Vol. 15, Iss. 22
Open Access | Times Cited: 4

From Stoichiometric Reagents to Catalytic Partners: Selenonium Salts as Alkylating Agents for Nucleophilic Displacement Reactions in Water
Nayara Silva Martins, Alix Y. Bastidas Ángel, João M. Anghinoni, et al.
Advanced Synthesis & Catalysis (2021) Vol. 364, Iss. 1, pp. 87-93
Closed Access | Times Cited: 9

FluorinatedS‐Adenosylmethionine as a Reagent for Enzyme‐Catalyzed Fluoromethylation
Jiaming Peng, Cangsong Liao, Carsten Bauer, et al.
Angewandte Chemie (2021) Vol. 133, Iss. 52, pp. 27384-27389
Closed Access | Times Cited: 8

Non-Native Site-Selective Enzyme Catalysis
Dibyendu Mondal, Harrison M. Snodgrass, Christian A. Gomez, et al.
(2023)
Open Access | Times Cited: 2

Enzymatic S‐Methylation of Thiols Catalyzed by Different O‐Methyltransferases
Eman M. M. Abdelraheem, Emely Jockmann, Jianyu Li, et al.
ChemCatChem (2023) Vol. 16, Iss. 2
Open Access | Times Cited: 2

One-step synthesis of cyclic polypyrazole and the self-assembly vesicles driven by hydrogen bond
Zhen Lu, Bogeng Guo, Yulai Zhao, et al.
Chinese Chemical Letters (2021) Vol. 33, Iss. 2, pp. 825-829
Closed Access | Times Cited: 6

Insights into E. coli Cyclopropane Fatty Acid Synthase (CFAS) Towards Enantioselective Carbene Free Biocatalytic Cyclopropanation.
Iman Omar, Michele Crotti, Chuhan Li, et al.
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 29
Open Access

Methyltransferases from RiPP pathways: shaping the landscape of natural product chemistry
M. Schröder, I. Pfeiffer, Silja Mordhorst
Beilstein Journal of Organic Chemistry (2024) Vol. 20, pp. 1652-1670
Open Access

Directed evolution of C-methyltransferase PsmD for enantioselective pyrroloindole derivative production
Diana A. Amariei, Julia Tenhaef, Thomas Claßen, et al.
Catalysis Science & Technology (2024) Vol. 14, Iss. 21, pp. 6298-6306
Open Access

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