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:

Deubiquitinase-targeting chimeras for targeted protein stabilization
Nathaniel J. Henning, Lydia Boike, Jessica N. Spradlin, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 4, pp. 412-421
Open Access | Times Cited: 209

Showing 1-25 of 209 citing articles:

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: 469

Deubiquitinases: From mechanisms to their inhibition by small molecules
Sven M. Lange, Lee A. Armstrong, Yogesh Kulathu
Molecular Cell (2021) Vol. 82, Iss. 1, pp. 15-29
Open Access | Times Cited: 185

The therapeutic potential of targeting regulated non-apoptotic cell death
Kamyar Hadian, Brent R. Stockwell
Nature Reviews Drug Discovery (2023) Vol. 22, Iss. 9, pp. 723-742
Closed Access | Times Cited: 162

Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials
Xin Xie, Tingting Yu, Xiang Li, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 151

Chasing molecular glue degraders: screening approaches
Ana Domostegui, Luis Nieto‐Barrado, Carles Perez‐Lopez, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 13, pp. 5498-5517
Open Access | Times Cited: 103

Deubiquitinases in cancer
Grant Dewson, Pieter J.A. Eichhorn, David Komander
Nature reviews. Cancer (2023) Vol. 23, Iss. 12, pp. 842-862
Closed Access | Times Cited: 102

Targeted protein degradation: from mechanisms to clinic
Jonathan M. Tsai, Radosław P. Nowak, Benjamin L. Ebert, et al.
Nature Reviews Molecular Cell Biology (2024) Vol. 25, Iss. 9, pp. 740-757
Closed Access | Times Cited: 87

Proximity-Based Modalities for Biology and Medicine
Xingui Liu, Alessio Ciulli
ACS Central Science (2023) Vol. 9, Iss. 7, pp. 1269-1284
Open Access | Times Cited: 83

Chemoproteomics-enabled discovery of a covalent molecular glue degrader targeting NF-κB
Elizabeth A. King, Yoo Jin Cho, Nathan S. Hsu, et al.
Cell chemical biology (2023) Vol. 30, Iss. 4, pp. 394-402.e9
Open Access | Times Cited: 64

Proteome-scale discovery of protein degradation and stabilization effectors
Juline Poirson, Hanna Cho, Akashdeep Dhillon, et al.
Nature (2024) Vol. 628, Iss. 8009, pp. 878-886
Closed Access | Times Cited: 24

Induced protein degradation for therapeutics: past, present, and future
Hojong Yoon, Justine C. Rutter, Yen-Der Li, et al.
Journal of Clinical Investigation (2024) Vol. 134, Iss. 1
Open Access | Times Cited: 21

DrugMap: A quantitative pan-cancer analysis of cysteine ligandability
Mariko Takahashi, Harrison B. Chong, Siwen Zhang, et al.
Cell (2024) Vol. 187, Iss. 10, pp. 2536-2556.e30
Open Access | Times Cited: 20

Expanding the horizons of targeted protein degradation: A non-small molecule perspective
Xiaowei Huang, Fengbo Wu, Jing Ye, et al.
Acta Pharmaceutica Sinica B (2024) Vol. 14, Iss. 6, pp. 2402-2427
Open Access | Times Cited: 16

Recent Advances in Small Molecule Inhibitors of Deubiquitinating Enzymes
Pengwei Liu, Zhengyang Chen, Yiting Guo, et al.
European Journal of Medicinal Chemistry (2025), pp. 117324-117324
Closed Access | Times Cited: 3

Decoding the functional impact of the cancer genome through protein–protein interactions
Haian Fu, Xiulei Mo, Andrei A. Ivanov
Nature reviews. Cancer (2025)
Closed Access | Times Cited: 2

Targeting Tau Protein with Proximity Inducing Modulators: A New Frontier to Combat Tauopathies
Elisa Uliassi, María Laura Bolognesi, Andrea Milelli
ACS Pharmacology & Translational Science (2025) Vol. 8, Iss. 3, pp. 654-672
Closed Access | Times Cited: 2

Ligandability of E3 Ligases for Targeted Protein Degradation Applications
Bridget P. Belcher, Carl C. Ward, Daniel K. Nomura
Biochemistry (2021) Vol. 62, Iss. 3, pp. 588-600
Open Access | Times Cited: 94

Advancing New Chemical Modalities into Clinical Studies
María‐Jesús Blanco, Kevin M. Gardinier, Mark Namchuk
ACS Medicinal Chemistry Letters (2022) Vol. 13, Iss. 11, pp. 1691-1698
Open Access | Times Cited: 38

DNA-encoded library-enabled discovery of proximity-inducing small molecules
Jeremy W. Mason, Yuen Ting Chow, Liam Hudson, et al.
Nature Chemical Biology (2023) Vol. 20, Iss. 2, pp. 170-179
Open Access | Times Cited: 37

Targeted Protein Degradation through E2 Recruitment
Nafsika Forte, Dustin Dovala, Matthew J. Hesse, et al.
ACS Chemical Biology (2023) Vol. 18, Iss. 4, pp. 897-904
Open Access | Times Cited: 36

Targeted protein posttranslational modifications by chemically induced proximity for cancer therapy
Yunhua Peng, Jing Liu, Hiroyuki Inuzuka, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 4, pp. 104572-104572
Open Access | Times Cited: 31

The rise of degrader drugs
Mingxing Teng, Nathanael S. Gray
Cell chemical biology (2023) Vol. 30, Iss. 8, pp. 864-878
Open Access | Times Cited: 27

Targeted Protein Degradation: Advances, Challenges, and Prospects for Computational Methods
Barmak Mostofian, Holli‐Joi Martin, Asghar M. Razavi, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 17, pp. 5408-5432
Open Access | Times Cited: 27

Cuproptosis and cuproptosis-related genes: Emerging potential therapeutic targets in breast cancer
Xiangdong Liu, Bo Luo, Xinhong Wu, et al.
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer (2023) Vol. 1878, Iss. 6, pp. 189013-189013
Closed Access | Times Cited: 27

Acetylation Targeting Chimera Enables Acetylation of the Tumor Suppressor p53
Md Kabir, Ning Sun, Xiao Hu, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 27, pp. 14932-14944
Closed Access | Times Cited: 26

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