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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:

Breaking Symmetry: Engineering Single-Chain Dimeric Streptavidin as Host for Artificial Metalloenzymes
Shuke Wu, Yi Zhou, Johannes G. Rebelein, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 40, pp. 15869-15878
Open Access | Times Cited: 36

Showing 1-25 of 36 citing articles:

Engineering new catalytic activities in enzymes
Kai Chen, Frances H. Arnold
Nature Catalysis (2020) Vol. 3, Iss. 3, pp. 203-213
Closed Access | Times Cited: 647
Recent trends in biocatalysis
Dong Yi, Thomas Bayer, Christoffel P. S. Badenhorst, et al.
Chemical Society Reviews (2021) Vol. 50, Iss. 14, pp. 8003-8049
Open Access | Times Cited: 265
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: 96
Beyond the Second Coordination Sphere: Engineering Dirhodium Artificial Metalloenzymes To Enable Protein Control of Transition Metal Catalysis
Jared C. Lewis
Accounts of Chemical Research (2019) Vol. 52, Iss. 3, pp. 576-584
Closed Access | Times Cited: 90
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
Design and biocatalytic applications of genetically fused multifunctional enzymes
Dianélis T. Monterrey, Iván Ayuso‐Fernández, Isabel Oroz‐Guinea, et al.
Biotechnology Advances (2022) Vol. 60, pp. 108016-108016
Open Access | Times Cited: 39
Design of Artificial Enzymes: Insights into Protein Scaffolds
Stefanie Hanreich, Elisa Bonandi, Ivana Drienovská
ChemBioChem (2022) Vol. 24, Iss. 6
Open Access | Times Cited: 22
Proteins as diverse, efficient, and evolvable scaffolds for artificial metalloenzymes
Woo Jae Jeong, Jaeseung Yu, Woon Ju Song
Chemical Communications (2020) Vol. 56, Iss. 67, pp. 9586-9599
Open Access | Times Cited: 37
Rational design of allosteric switchable catalysts
Tiezheng Pan, Yaling Wang, Xue Xue, et al.
Exploration (2022) Vol. 2, Iss. 2
Open Access | Times Cited: 18
Gene Fusion and Directed Evolution to Break Structural Symmetry and Boost Catalysis by an Oligomeric C−C Bond‐Forming Enzyme
Guangcai Xu, Andreas Kunzendorf, Michele Crotti, et al.
Angewandte Chemie International Edition (2021) Vol. 61, Iss. 8
Open Access | Times Cited: 23
Artificial metalloenzymes
Tobias Vornholt, Florian Leiss-Maier, Woo Jae Jeong, et al.
Nature Reviews Methods Primers (2024) Vol. 4, Iss. 1
Closed Access | Times Cited: 2
Hetero-Bis-Conjugation of Bioactive Molecules to Half-Sandwich Ruthenium(II) and Iridium(III) Complexes Provides Synergic Effects in Cancer Cell Cytotoxicity
Lorenzo Biancalana, Hana Kostrhunová, Lucinda K. Batchelor, et al.
Inorganic Chemistry (2021) Vol. 60, Iss. 13, pp. 9529-9541
Closed Access | Times Cited: 20
Unified access to up-to-date residue-level annotations from UniProtKB and other biological databases for PDB data
Preeti Choudhary, Stephen Anyango, John M. Berrisford, et al.
Scientific Data (2023) Vol. 10, Iss. 1
Open Access | Times Cited: 7
Artificial Metalloenzymes: From Selective Chemical Transformations to Biochemical Applications
Tomoki Himiyama, Yasunori Okamoto
Molecules (2020) Vol. 25, Iss. 13, pp. 2989-2989
Open Access | Times Cited: 16
Artificial Metalloproteins with Dinuclear Iron–Hydroxido Centers
Kelsey R. Miller, Saborni Biswas, Andrew J. Jasniewski, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 5, pp. 2384-2393
Open Access | Times Cited: 14
Transition Metal Scaffolds Used To Bring New‐to‐Nature Reactions into Biological Systems
Yifei Liu, Ka Lun Lai, Kenward Vong
European Journal of Inorganic Chemistry (2022) Vol. 2022, Iss. 21
Closed Access | Times Cited: 10
Dynamic Ir(III) Photosensors for the Major Human Drug-Metabolizing Enzyme Cytochrome P450 3A4
Madeline Denison, Justin J. Ahrens, Marilyn N. Dunbar, et al.
Inorganic Chemistry (2023) Vol. 62, Iss. 7, pp. 3305-3320
Open Access | Times Cited: 5
Manganese Transfer Hydrogenases Based on the Biotin‐Streptavidin Technology
Weijin Wang, Ryo Tachibana, Zhi Zou, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 43
Open Access | Times Cited: 5
Organoiridium-catalyzed bioorthogonal chemistry
Deepika Chauhan, Puja Prasad, Pijus K. Sasmal
Coordination Chemistry Reviews (2024) Vol. 520, pp. 216139-216139
Closed Access | Times Cited: 1
Exploring and Adapting the Molecular Selectivity of Artificial Metalloenzymes
Kenward Vong, Igor Nasibullin, Katsunori Tanaka
Bulletin of the Chemical Society of Japan (2020) Vol. 94, Iss. 2, pp. 382-396
Open Access | Times Cited: 15
Gene Fusion and Directed Evolution to Break Structural Symmetry and Boost Catalysis by an Oligomeric C−C Bond‐Forming Enzyme
Guangcai Xu, Andreas Kunzendorf, Michele Crotti, et al.
Angewandte Chemie (2021) Vol. 134, Iss. 8
Open Access | Times Cited: 12
Enabling protein-hosted organocatalytic transformations
Alexander R. Nödling, Nicolò Santi, Thomas L. Williams, et al.
RSC Advances (2020) Vol. 10, Iss. 27, pp. 16147-16161
Open Access | Times Cited: 10
Aromatic foldamers as scaffolds for metal second coordination sphere design
Antoine Meunier, Michael L. Singleton, Brice Kauffmann, et al.
Chemical Science (2020) Vol. 11, Iss. 44, pp. 12178-12186
Open Access | Times Cited: 10
Expanding the Potential of the Solvent-Assisted Method to Create Bio-Interfaces from Amphiphilic Block Copolymers
Stefano Leone, Jaicy Vallapurackal, Saziye Yorulmaz Avsar, et al.
Biomacromolecules (2021) Vol. 22, Iss. 7, pp. 3005-3016
Closed Access | Times Cited: 9
Ir(III)-Based Agents for Monitoring the Cytochrome P450 3A4 Active Site Occupancy
Madeline Denison, Sean J. Steinke, Aliza Majeed, et al.
Inorganic Chemistry (2022) Vol. 61, Iss. 35, pp. 13673-13677
Open Access | Times Cited: 5
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