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:

Systematic engineering of artificial metalloenzymes for new-to-nature reactions
Tobias Vornholt, Fadri Christoffel, Michela M. Pellizzoni, et al.
Science Advances (2021) Vol. 7, Iss. 4
Open Access | Times Cited: 65

Showing 1-25 of 65 citing articles:

Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere
Casey Van Stappen, Yunling Deng, Yiwei Liu, et al.
Chemical Reviews (2022) Vol. 122, Iss. 14, pp. 11974-12045
Open Access | Times Cited: 95

Algorithm-aided engineering of aliphatic halogenase WelO5* for the asymmetric late-stage functionalization of soraphens
Johannes Büchler, Sumire Honda Malca, David Patsch, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 61

Engineering and emerging applications of artificial metalloenzymes with whole cells
Malte Wittwer, Ulrich Markel, Johannes Schiffels, et al.
Nature Catalysis (2021) Vol. 4, Iss. 10, pp. 814-827
Closed Access | Times Cited: 58

Prodrug Activation by Gold Artificial Metalloenzyme‐Catalyzed Synthesis of Phenanthridinium Derivatives via Hydroamination
Tsung‐Che Chang, Kenward Vong, Tomoya Yamamoto, et al.
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 22, pp. 12446-12454
Closed Access | Times Cited: 56

Synthetic prodrug design enables biocatalytic activation in mice to elicit tumor growth suppression
Igor Nasibullin, Ivan Smirnov, Peni Ahmadi, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 50

Learning from Protein Engineering by Deconvolution of Multi‐Mutational Variants
Frank Hollmann, Joaquin Sanchis, Manfred T. Reetz
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 36
Open Access | Times Cited: 10

Enhanced Sequence-Activity Mapping and Evolution of Artificial Metalloenzymes by Active Learning
Tobias Vornholt, Mojmír Mutný, Gregor W. Schmidt, et al.
ACS Central Science (2024) Vol. 10, Iss. 7, pp. 1357-1370
Open Access | Times Cited: 7

Accessing iridium Cp* as a cofactor for artificial metalloenzymes
Oskar James Klein, Armando Albert-Flores, Matthew L. Wheeler, et al.
Journal of Inorganic Biochemistry (2025) Vol. 265, pp. 112820-112820
Closed Access

Artificial metalloenzyme assembly in cellular compartments for enhanced catalysis
Tong Wu, Xianhui Chen, Yating Fei, et al.
Nature Chemical Biology (2025)
Closed Access

Engineering carbon assimilation in plants
Kezhen Qin, Xingyan Ye, Shanshan Luo, et al.
Journal of Integrative Plant Biology (2025)
Closed Access

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

Cell-Free Systems to Mimic and Expand Metabolism
Blake J. Rasor, Tobias J. Erb
ACS Synthetic Biology (2025)
Open Access

Design and evolution of chimeric streptavidin for protein-enabled dual gold catalysis
Fadri Christoffel, Nico V. Igareta, Michela M. Pellizzoni, et al.
Nature Catalysis (2021) Vol. 4, Iss. 8, pp. 643-653
Open Access | Times Cited: 48

Artificial Metalloenzyme-Catalyzed Enantioselective Amidation via Nitrene Insertion in Unactivated C(sp3)–H Bonds
Kun Yu, Zhi Zou, Nico V. Igareta, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 30, pp. 16621-16629
Open Access | Times Cited: 18

Machine Learning: A Suitable Method for Biocatalysis
Pedro Sampaio, Pedro Fernandes
Catalysts (2023) Vol. 13, Iss. 6, pp. 961-961
Open Access | Times Cited: 15

Effective engineering of a ketoreductase for the biocatalytic synthesis of an ipatasertib precursor
Sumire Honda Malca, Nadine Duss, Jasmin Meierhofer, et al.
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 5

An Artificial Metalloenzyme Based on a Copper Heteroscorpionate Enables sp3 C–H Functionalization via Intramolecular Carbene Insertion
Corentin Rumo, Alina Stein, Juliane Klehr, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 26, pp. 11676-11684
Open Access | Times Cited: 23

A Dual‐Metal‐Catalyzed Sequential Cascade Reaction in an Engineered Protein Cage**
Paul Ebensperger, Mariia Zmyslia, Philipp Lohner, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 16
Open Access | Times Cited: 13

Peptides and metal ions: A successful marriage for developing artificial metalloproteins
Linda Leone, Maria De Fenza, Alessandra Esposito, et al.
Journal of Peptide Science (2024)
Closed Access | Times Cited: 3

Exporting Metal‐Carbene Chemistry to Live Mammalian Cells: Copper‐Catalyzed Intracellular Synthesis of Quinoxalines Enabled by N−H Carbene Insertions
Sara Gutiérrez, María Tomás‐Gamasa, José L. Mascareñas
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 40, pp. 22017-22025
Open Access | Times Cited: 27

MeDBA: the Metalloenzyme Data Bank and Analysis platform
Junlin Yu, Song Wu, Cong Zhou, et al.
Nucleic Acids Research (2022) Vol. 51, Iss. D1, pp. D593-D602
Open Access | Times Cited: 19

Creating new-to-nature carbon fixation: A guide
Helena Schulz-Mirbach, Beau Dronsella, Hai He, et al.
Metabolic Engineering (2023) Vol. 82, pp. 12-28
Closed Access | Times Cited: 9

Enhanced Sequence-Activity Mapping and Evolution of Artificial Metalloenzymes by Active Learning
Tobias Vornholt, Mojmír Mutný, Gregor W. Schmidt, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2

Combining an artificial metathase with a fatty acid decarboxylase in a whole cell for cycloalkene synthesis
Zhi Zou, Shuke Wu, Daniel Gerngross, et al.
Nature Synthesis (2024) Vol. 3, Iss. 9, pp. 1113-1123
Open Access | Times Cited: 2

The potential of RuBisCO in CO2 capture and utilization
Kamyll Dawn Cocon, Patricia Luis
Progress in Energy and Combustion Science (2024) Vol. 105, pp. 101184-101184
Closed Access | Times Cited: 2

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