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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:

Development of Halogenase Enzymes for Use in Synthesis
Jonathan Latham, Eileen Brandenburger, Sarah A. Shepherd, et al.
Chemical Reviews (2017) Vol. 118, Iss. 1, pp. 232-269
Open Access | Times Cited: 298

Showing 1-25 of 298 citing articles:

3d Transition Metals for C–H Activation
Parthasarathy Gandeepan, Thomas Müller, Daniel Zell, et al.
Chemical Reviews (2018) Vol. 119, Iss. 4, pp. 2192-2452
Closed Access | Times Cited: 1970
Biocatalysis: Enzymatic Synthesis for Industrial Applications
Shuke Wu, Radka Šnajdrová, Jeffrey C. Moore, et al.
Angewandte Chemie International Edition (2020) Vol. 60, Iss. 1, pp. 88-119
Open Access | Times Cited: 1068
Biocatalytic Oxidation Reactions: A Chemist's Perspective
Jiajia Dong, Elena Fernández‐Fueyo, Frank Hollmann, et al.
Angewandte Chemie International Edition (2018) Vol. 57, Iss. 30, pp. 9238-9261
Open Access | Times Cited: 416
Embracing Nature’s Catalysts: A Viewpoint on the Future of Biocatalysis
Bernhard Hauer
ACS Catalysis (2020) Vol. 10, Iss. 15, pp. 8418-8427
Closed Access | Times Cited: 236
A Perspective on Late-Stage Aromatic C–H Bond Functionalization
Li Zhang, Tobias Ritter
Journal of the American Chemical Society (2022) Vol. 144, Iss. 6, pp. 2399-2414
Open Access | Times Cited: 230
Biocatalysis: A Pharma Perspective
Joseph P. Adams, Murray J. B. Brown, Alba Díaz‐Rodríguez, et al.
Advanced Synthesis & Catalysis (2019) Vol. 361, Iss. 11, pp. 2421-2432
Open Access | Times Cited: 203
Enzyme function prediction using contrastive learning
Tianhao Yu, Haiyang Cui, Jianan Canal Li, et al.
Science (2023) Vol. 379, Iss. 6639, pp. 1358-1363
Closed Access | Times Cited: 193
Biocatalysis making waves in organic chemistry
Ulf Hanefeld, Frank Hollmann, Caroline E. Paul
Chemical Society Reviews (2021) Vol. 51, Iss. 2, pp. 594-627
Open Access | Times Cited: 176
Electrochemical Late-Stage Functionalization
Yulei Wang, Suman Dana, Hao Long, et al.
Chemical Reviews (2023) Vol. 123, Iss. 19, pp. 11269-11335
Open Access | Times Cited: 141
Flavoprotein monooxygenases: Versatile biocatalysts
Caroline E. Paul, Daniel Eggerichs, Adrie H. Westphal, et al.
Biotechnology Advances (2021) Vol. 51, pp. 107712-107712
Open Access | Times Cited: 123
Enzymatic Late‐Stage Modifications: Better Late Than Never
Elvira Romero, Bethan S. Jones, Bethany N. Hogg, et al.
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 31, pp. 16824-16855
Open Access | Times Cited: 116
Mechanism-guided tunnel engineering to increase the efficiency of a flavin-dependent halogenase
Kridsadakorn Prakinee, Aisaraphon Phintha, Surawit Visitsatthawong, et al.
Nature Catalysis (2022) Vol. 5, Iss. 6, pp. 534-544
Closed Access | Times Cited: 86
The Evolving Nature of Biocatalysis in Pharmaceutical Research and Development
Scott P. France, Russell D. Lewis, Carlos A. Martínez
JACS Au (2023) Vol. 3, Iss. 3, pp. 715-735
Open Access | Times Cited: 75
Naturally Occurring Organohalogen Compounds—A Comprehensive Review
Gordon W. Gribble
Fortschritte der Chemie Organischer Naturstoffe/Fortschritte der Chemie organischer Naturstoffe/Progress in the chemistry of organic natural products (2023), pp. 1-546
Closed Access | Times Cited: 49
Regioisomeric effect of heteroatoms and functional groups of organic ligands: Impacts on coordination bonding and corrosion protection performance
Chandrabhan Verma, Ambrish Singh, Prashant Singh, et al.
Coordination Chemistry Reviews (2024) Vol. 515, pp. 215966-215966
Open Access | Times Cited: 34
Expanding chemistry through in vitro and in vivo biocatalysis
Elijah N. Kissman, Max B. Sosa, Douglas C Millar, et al.
Nature (2024) Vol. 631, Iss. 8019, pp. 37-48
Closed Access | Times Cited: 28
Copper-dependent halogenase catalyses unactivated C−H bond functionalization
Chen‐Yu Chiang, M. Ohashi, Jessie Le, et al.
Nature (2025)
Closed Access | Times Cited: 2
A family of radical halogenases for the engineering of amino-acid-based products
Monica E. Neugebauer, Kiera H. Sumida, Jeffrey G. Pelton, et al.
Nature Chemical Biology (2019) Vol. 15, Iss. 10, pp. 1009-1016
Closed Access | Times Cited: 139
Efficient Electrocatalysis for the Preparation of (Hetero)aryl Chlorides and Vinyl Chloride with 1,2‐Dichloroethane
Yujie Liang, Fengguirong Lin, Yeerlan Adeli, et al.
Angewandte Chemie International Edition (2019) Vol. 58, Iss. 14, pp. 4566-4570
Closed Access | Times Cited: 134
Biokatalytische Oxidationsreaktionen – aus der Sicht eines Chemikers
Jiajia Dong, Elena Fernández‐Fueyo, Frank Hollmann, et al.
Angewandte Chemie (2018) Vol. 130, Iss. 30, pp. 9380-9404
Open Access | Times Cited: 105
Second‐Coordination Sphere Effects on Selectivity and Specificity of Heme and Nonheme Iron Enzymes
Sam P. de Visser
Chemistry - A European Journal (2019) Vol. 26, Iss. 24, pp. 5308-5327
Open Access | Times Cited: 98
Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities
Thomas Heine, Willem J. H. van Berkel, George Gassner, et al.
Biology (2018) Vol. 7, Iss. 3, pp. 42-42
Open Access | Times Cited: 95
Biokatalyse: Enzymatische Synthese für industrielle Anwendungen
Shuke Wu, Radka Šnajdrová, Jeffrey C. Moore, et al.
Angewandte Chemie (2020) Vol. 133, Iss. 1, pp. 89-123
Open Access | Times Cited: 94
Site-Selective C–H Halogenation Using Flavin-Dependent Halogenases Identified via Family-Wide Activity Profiling
Brian F. Fisher, Harrison M. Snodgrass, Krysten A. Jones, et al.
ACS Central Science (2019) Vol. 5, Iss. 11, pp. 1844-1856
Open Access | Times Cited: 92
Understanding and Improving the Activity of Flavin-Dependent Halogenases via Random and Targeted Mutagenesis
Mary C. Andorfer, Jared C. Lewis
Annual Review of Biochemistry (2018) Vol. 87, Iss. 1, pp. 159-185
Open Access | Times Cited: 87
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