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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:

Fragment-Based Covalent Ligand Screening Enables Rapid Discovery of Inhibitors for the RBR E3 Ubiquitin Ligase HOIP
Henrik Johansson, Yi‐Chun Isabella Tsai, Ken G. M. Fantom, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 6, pp. 2703-2712
Open Access | Times Cited: 111

Showing 1-25 of 111 citing articles:

Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease
A. Douangamath, D. Fearon, Paul Gehrtz, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 486
Advances in covalent drug discovery
Lydia Boike, Nathaniel J. Henning, Daniel K. Nomura
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 12, pp. 881-898
Open Access | Times Cited: 475
Rapid Covalent-Probe Discovery by Electrophile-Fragment Screening
Efrat Resnick, A.R. Bradley, Jinrui Gan, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 22, pp. 8951-8968
Open Access | Times Cited: 279
The emerging role of mass spectrometry-based proteomics in drug discovery
Felix Meissner, Jennifer Geddes‐McAlister, Matthias Mann, et al.
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 9, pp. 637-654
Closed Access | Times Cited: 229
Recent Advances in Selective and Irreversible Covalent Ligand Development and Validation
Tinghu Zhang, John M. Hatcher, Mingxing Teng, et al.
Cell chemical biology (2019) Vol. 26, Iss. 11, pp. 1486-1500
Open Access | Times Cited: 148
Fragment-based covalent ligand discovery
Wenchao Lu, Milka Kostić, Tinghu Zhang, et al.
RSC Chemical Biology (2021) Vol. 2, Iss. 2, pp. 354-367
Open Access | Times Cited: 106
The roles of E3 ubiquitin ligases in cancer progression and targeted therapy
Chibuzo Sampson, Qiuping Wang, Wuxiyar Otkur, et al.
Clinical and Translational Medicine (2023) Vol. 13, Iss. 3
Open Access | Times Cited: 67
Profiling Sulfur(VI) Fluorides as Reactive Functionalities for Chemical Biology Tools and Expansion of the Ligandable Proteome
Katharine Gilbert, Aini Vuorinen, Arron Aatkar, et al.
ACS Chemical Biology (2023) Vol. 18, Iss. 2, pp. 285-295
Open Access | Times Cited: 43
Robust proteome profiling of cysteine-reactive fragments using label-free chemoproteomics
George S. Biggs, Emma E. Cawood, Aini Vuorinen, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 2
Overview of Recent Strategic Advances in Medicinal Chemistry
Gaochan Wu, Tong Zhao, Dongwei Kang, et al.
Journal of Medicinal Chemistry (2019) Vol. 62, Iss. 21, pp. 9375-9414
Open Access | Times Cited: 144
10 Years Into the Resurgence of Covalent Drugs
Elena De Vita
Future Medicinal Chemistry (2020) Vol. 13, Iss. 2, pp. 193-210
Open Access | Times Cited: 99
Covalent fragment libraries in drug discovery
Aaron Keeley, László Petri, Péter Ábrányi‐Balogh, et al.
Drug Discovery Today (2020) Vol. 25, Iss. 6, pp. 983-996
Open Access | Times Cited: 89
Covalent Small Molecules as Enabling Platforms for Drug Discovery
Samuel E. Dalton, Sébastien Campos
ChemBioChem (2019) Vol. 21, Iss. 8, pp. 1080-1100
Closed Access | Times Cited: 81
An automatic pipeline for the design of irreversible derivatives identifies a potent SARS-CoV-2 Mpro inhibitor
Daniel Zaidman, Paul Gehrtz, Mihajlo Filep, et al.
Cell chemical biology (2021) Vol. 28, Iss. 12, pp. 1795-1806.e5
Open Access | Times Cited: 73
A Comprehensive Guide for Assessing Covalent Inhibition in Enzymatic Assays Illustrated with Kinetic Simulations
Elma Mons, Sander Roet, Robbert Q. Kim, et al.
Current Protocols (2022) Vol. 2, Iss. 6
Open Access | Times Cited: 68
Advances in high‐throughput mass spectrometry in drug discovery
María Emilia Dueñas, Rachel E. Heap, Melanie Leveridge, et al.
EMBO Molecular Medicine (2022) Vol. 15, Iss. 1
Open Access | Times Cited: 62
The rise of covalent proteolysis targeting chimeras
Ronen Gabizon, Nir London
Current Opinion in Chemical Biology (2021) Vol. 62, pp. 24-33
Closed Access | Times Cited: 61
Targeting the Ubiquitin-Proteasome System for Cancer Therapeutics by Small-Molecule Inhibitors
Gabriel LaPlante, Wei Zhang
Cancers (2021) Vol. 13, Iss. 12, pp. 3079-3079
Open Access | Times Cited: 58
E3 Ligases Meet Their Match: Fragment-Based Approaches to Discover New E3 Ligands and to Unravel E3 Biology
Iacovos N. Michaelides, Gavin W. Collie
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 5, pp. 3173-3194
Open Access | Times Cited: 26
Efficient Ligand Discovery Using Sulfur(VI) Fluoride Reactive Fragments
Arron Aatkar, Aini Vuorinen, Oliver Longfield, et al.
ACS Chemical Biology (2023) Vol. 18, Iss. 9, pp. 1926-1937
Open Access | Times Cited: 23
Novel WRN Helicase Inhibitors Selectively Target Microsatellite-Unstable Cancer Cells
Gabriele Picco, Yanhua Rao, Angham Al Saedi, et al.
Cancer Discovery (2024) Vol. 14, Iss. 8, pp. 1457-1475
Closed Access | Times Cited: 15
High-Throughput Hit Identification with Acoustic Ejection Mass Spectrometry
Xiujuan Wen, David G. McLaren
SLAS TECHNOLOGY (2025), pp. 100245-100245
Closed Access | Times Cited: 1
Fragment-to-Lead Medicinal Chemistry Publications in 2019
Wolfgang Jahnke, Daniel A. Erlanson, Iwan J. P. de Esch, et al.
Journal of Medicinal Chemistry (2020) Vol. 63, Iss. 24, pp. 15494-15507
Open Access | Times Cited: 58
Chain reactions: molecular mechanisms of RBR ubiquitin ligases
Thomas R. Cotton, Bernhard C. Lechtenberg
Biochemical Society Transactions (2020) Vol. 48, Iss. 4, pp. 1737-1750
Open Access | Times Cited: 57
Exploring the Versatility of the Covalent Thiol–Alkyne Reaction with Substituted Propargyl Warheads: A Deciding Role for the Cysteine Protease
Elma Mons, Robbert Q. Kim, Bjorn R. van Doodewaerd, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 17, pp. 6423-6433
Open Access | Times Cited: 53
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