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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:

Discovery of a Covalent FEM1B Recruiter for Targeted Protein Degradation Applications
Nathaniel J. Henning, Andrew G. Manford, Jessica N. Spradlin, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 2, pp. 701-708
Open Access | Times Cited: 157

Showing 1-25 of 157 citing articles:

PROTAC targeted protein degraders: the past is prologue
Miklós Békés, David R. Langley, Craig M. Crews
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 3, pp. 181-200
Open Access | Times Cited: 1824
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: 472
Chemistries of bifunctional PROTAC degraders
Chao-Guo Cao, Ming He, Liguo Wang, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 16, pp. 7066-7114
Closed Access | Times Cited: 168
E3 Ligase Ligands in Successful PROTACs: An Overview of Syntheses and Linker Attachment Points
Aleša Bricelj, Christian Steinebach, Robert D. Kuchta, et al.
Frontiers in Chemistry (2021) Vol. 9
Open Access | Times Cited: 158
Target and tissue selectivity of PROTAC degraders
Robert G. Guenette, Seung Wook Yang, Jaeki Min, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 14, pp. 5740-5756
Closed Access | Times Cited: 146
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
Rational Chemical Design of Molecular Glue Degraders
Ethan S. Toriki, James W. Papatzimas, Kaila Nishikawa, et al.
ACS Central Science (2023) Vol. 9, Iss. 5, pp. 915-926
Open Access | Times Cited: 87
Targeted Protein Degradation by Electrophilic PROTACs that Stereoselectively and Site-Specifically Engage DCAF1
Yongfeng Tao, David Remillard, Ekaterina V. Vinogradova, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 40, pp. 18688-18699
Open Access | Times Cited: 82
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
Annual review of PROTAC degraders as anticancer agents in 2022
Xiao Wang, Zhao-Long Qin, Na Li, et al.
European Journal of Medicinal Chemistry (2024) Vol. 267, pp. 116166-116166
Closed Access | Times Cited: 53
Advancing Strategies for Proteolysis-Targeting Chimera Design
Minglei Li, Ying Zhi, Bo Liu, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 4, pp. 2308-2329
Closed Access | Times Cited: 45
Piperlongumine conjugates induce targeted protein degradation
Jing Pei, Yufeng Xiao, Xingui Liu, et al.
Cell chemical biology (2023) Vol. 30, Iss. 2, pp. 203-213.e17
Open Access | Times Cited: 43
DCAF16-Based Covalent Handle for the Rational Design of Monovalent Degraders
Melissa Lim, Thang Do Cong, Lauren M. Orr, et al.
ACS Central Science (2024) Vol. 10, Iss. 7, pp. 1318-1331
Open Access | Times Cited: 22
Targeted Protein Degradation through Recruitment of the CUL4 Complex Adaptor Protein DDB1
Margot Meyers, Sabine Cismoski, Anoohya Panidapu, et al.
ACS Chemical Biology (2024) Vol. 19, Iss. 1, pp. 58-68
Open Access | Times Cited: 19
Applications of protein ubiquitylation and deubiquitylation in drug discovery
Yilin Chen, Haoan Xue, Jianping Jin
Journal of Biological Chemistry (2024) Vol. 300, Iss. 5, pp. 107264-107264
Open Access | Times Cited: 16
Cullin-RING ligases employ geometrically optimized catalytic partners for substrate targeting
Jerry Li, Nicholas Purser, Joanna Liwocha, et al.
Molecular Cell (2024) Vol. 84, Iss. 7, pp. 1304-1320.e16
Open Access | Times Cited: 15
BRD4-targeted photodegradation nanoplatform for light activatable melanoma therapy
Shiman Lu, Zhaoqing Shi, Chendi Ding, et al.
Biomaterials (2025) Vol. 317, pp. 123101-123101
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
Discovery of E3 Ligase Ligands for Target Protein Degradation
Jaeseok Lee, Young‐Jun Lee, Young Mee Jung, et al.
Molecules (2022) Vol. 27, Iss. 19, pp. 6515-6515
Open Access | Times Cited: 68
A bibliometric analysis of PROTAC from 2001 to 2021
Deping Li, Dongmin Yu, Yan Li, et al.
European Journal of Medicinal Chemistry (2022) Vol. 244, pp. 114838-114838
Closed Access | Times Cited: 65
Exploring the target scope of KEAP1 E3 ligase-based PROTACs
Guangyan Du, Jie Jiang, Nathaniel J. Henning, et al.
Cell chemical biology (2022) Vol. 29, Iss. 10, pp. 1470-1481.e31
Open Access | Times Cited: 52
PROTAC degraders as chemical probes for studying target biology and target validation
Václav Nêmec, Martin P. Schwalm, Susanne Müller, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 18, pp. 7971-7993
Closed Access | Times Cited: 51
PROTAC degraders with ligands recruiting MDM2 E3 ubiquitin ligase: an updated perspective
Xin Han, Wenyi Wei, Yi Sun
Acta Materia Medica (2022) Vol. 1, Iss. 2
Open Access | Times Cited: 47
Expanding the landscape of E3 ligases for targeted protein degradation
Luke T. Kramer, Xiaoyu Zhang
Current Research in Chemical Biology (2022) Vol. 2, pp. 100020-100020
Open Access | Times Cited: 46
Emerging targeted protein degradation tools for innovative drug discovery: From classical PROTACs to the novel and beyond
Yue Zhong, Fanglian Chi, Hanyu Wu, et al.
European Journal of Medicinal Chemistry (2022) Vol. 231, pp. 114142-114142
Closed Access | Times Cited: 40
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