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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:

Structure-based design of targeted covalent inhibitors
Richard Lonsdale, Richard A. Ward
Chemical Society Reviews (2018) Vol. 47, Iss. 11, pp. 3816-3830
Closed Access | Times Cited: 291

Showing 1-25 of 291 citing articles:

Therapeutic peptides: current applications and future directions
Lei Wang, Nanxi Wang, Wenping Zhang, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 1182
Emerging and Re-Emerging Warheads for Targeted Covalent Inhibitors: Applications in Medicinal Chemistry and Chemical Biology
Matthias Gehringer, Stefan Laufer
Journal of Medicinal Chemistry (2018) Vol. 62, Iss. 12, pp. 5673-5724
Closed Access | Times Cited: 581
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
Put a ring on it: application of small aliphatic rings in medicinal chemistry
Matthias R. Bauer, Paolo Di Fruscia, Simon C. C. Lucas, et al.
RSC Medicinal Chemistry (2021) Vol. 12, Iss. 4, pp. 448-471
Open Access | Times Cited: 295
Advances in covalent kinase inhibitors
Ayah Abdeldayem, Yasir S. Raouf, Stefan N. Constantinescu, et al.
Chemical Society Reviews (2020) Vol. 49, Iss. 9, pp. 2617-2687
Closed Access | Times Cited: 256
Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications
Xiaoran Roger Liu, Mengru Zhang, Michael L. Gross
Chemical Reviews (2020) Vol. 120, Iss. 10, pp. 4355-4454
Open Access | Times Cited: 220
Identification of pyrogallol as a warhead in design of covalent inhibitors for the SARS-CoV-2 3CL protease
Haixia Su, Sheng Yao, Wenfeng Zhao, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 162
Developing Covalent Protein Drugs via Proximity-Enabled Reactive Therapeutics
Qingke Li, Chen Qu, Paul C. Klauser, et al.
Cell (2020) Vol. 182, Iss. 1, pp. 85-97.e16
Open Access | Times Cited: 160
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
Light-driven post-translational installation of reactive protein side chains
Brian Josephson, Charlie Fehl, Patrick G. Isenegger, et al.
Nature (2020) Vol. 585, Iss. 7826, pp. 530-537
Open Access | Times Cited: 146
The long and short non-coding RNAs modulating EZH2 signaling in cancer
Sepideh Mirzaei, Mohammad Gholami, Kiavash Hushmandi, et al.
Journal of Hematology & Oncology (2022) Vol. 15, Iss. 1
Open Access | Times Cited: 138
The Ascension of Targeted Covalent Inhibitors
Juswinder Singh
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 8, pp. 5886-5901
Closed Access | Times Cited: 130
Small molecules and their impact in drug discovery: A perspective on the occasion of the 125th anniversary of the Bayer Chemical Research Laboratory
Hartmut Beck, Michael Härter, B. Hass, et al.
Drug Discovery Today (2022) Vol. 27, Iss. 6, pp. 1560-1574
Open Access | Times Cited: 110
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: 107
E3 ligase ligand chemistries: from building blocks to protein degraders
Izidor Sosič, Aleša Bricelj, Christian Steinebach
Chemical Society Reviews (2022) Vol. 51, Iss. 9, pp. 3487-3534
Closed Access | Times Cited: 92
Potent and selective covalent inhibition of the papain-like protease from SARS-CoV-2
Brian Sanders, Suman Pokhrel, Audrey Labbé, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 64
An update on the discovery and development of reversible covalent inhibitors
Faridoon Faridoon, Raymond Ng, Guiping Zhang, et al.
Medicinal Chemistry Research (2023) Vol. 32, Iss. 6, pp. 1039-1062
Open Access | Times Cited: 46
Recent Advances in Covalent Drug Discovery
D. M. Schaefer, Xinlai Cheng
Pharmaceuticals (2023) Vol. 16, Iss. 5, pp. 663-663
Open Access | Times Cited: 45
Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development
Kwangho Nam, Yihan Shao, Dan Thomas Major, et al.
ACS Omega (2024)
Open Access | Times Cited: 24
Covalent Inhibitors of Protein–Protein Interactions Targeting Lysine, Tyrosine, or Histidine Residues
Luca Gambini, Carlo Baggio, Parima Udompholkul, et al.
Journal of Medicinal Chemistry (2019) Vol. 62, Iss. 11, pp. 5616-5627
Open Access | Times Cited: 114
TAS‐120 Cancer Target Binding: Defining Reactivity and Revealing the First Fibroblast Growth Factor Receptor 1 (FGFR1) Irreversible Structure
Maria Kalyukina, Y. Yosaatmadja, Martin Middleditch, et al.
ChemMedChem (2019) Vol. 14, Iss. 4, pp. 494-500
Closed Access | Times Cited: 112
Characterising covalent warhead reactivity
James S. Martin, Claire J. Mackenzie, Daniel A. Fletcher, et al.
Bioorganic & Medicinal Chemistry (2019) Vol. 27, Iss. 10, pp. 2066-2074
Open Access | Times Cited: 107
What coronavirus 3C‐like protease tells us: From structure, substrate selectivity, to inhibitor design
Muya Xiong, Haixia Su, Wenfeng Zhao, et al.
Medicinal Research Reviews (2021) Vol. 41, Iss. 4, pp. 1965-1998
Open Access | Times Cited: 103
Discovery of Branebrutinib (BMS-986195): A Strategy for Identifying a Highly Potent and Selective Covalent Inhibitor Providing Rapid in Vivo Inactivation of Bruton’s Tyrosine Kinase (BTK)
Scott H. Watterson, Qingjie Liu, Myra Beaudoin Bertrand, et al.
Journal of Medicinal Chemistry (2019) Vol. 62, Iss. 7, pp. 3228-3250
Open Access | Times Cited: 93
Loss of heterozygosity of essential genes represents a widespread class of potential cancer vulnerabilities
Caitlin A. Nichols, William J. Gibson, Meredith S. Brown, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 93
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