Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

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

Showing 1-25 of 94 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
Protein degraders enter the clinic — a new approach to cancer therapy
Deborah Chirnomas, Keith R. Hornberger, Craig M. Crews
Nature Reviews Clinical Oncology (2023) Vol. 20, Iss. 4, pp. 265-278
Closed Access | Times Cited: 329
Molecular Glues: The Adhesive Connecting Targeted Protein Degradation to the Clinic
Janet M. Sasso, Rumiana Tenchov, Dasheng Wang, et al.
Biochemistry (2022) Vol. 62, Iss. 3, pp. 601-623
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
Small-molecule discovery through DNA-encoded libraries
Alexander A. Peterson, David R. Liu
Nature Reviews Drug Discovery (2023) Vol. 22, Iss. 9, pp. 699-722
Closed Access | Times Cited: 87
Emerging degrader technologies engaging lysosomal pathways
Yu Ding, Dong Xing, Yiyan Fei, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 21, pp. 8832-8876
Open Access | Times Cited: 76
Expanding PROTACtable genome universe of E3 ligases
Yuan Liu, Jingwen Yang, Tianlu Wang, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 71
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
Large-scale chemoproteomics expedites ligand discovery and predicts ligand behavior in cells
Fabian Offensperger, Gary Tin, Miquel Duran‐Frigola, et al.
Science (2024) Vol. 384, Iss. 6694
Closed Access | Times Cited: 23
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
Target protein localization and its impact on PROTAC-mediated degradation
Luke M. Simpson, Lorraine Glennie, Abigail Brewer, et al.
Cell chemical biology (2022) Vol. 29, Iss. 10, pp. 1482-1504.e7
Open Access | Times Cited: 47
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
Antiviral PROTACs: Opportunity borne with challenge
Jinsen Liang, Yihe Wu, Ke Lan, et al.
Cell Insight (2023) Vol. 2, Iss. 3, pp. 100092-100092
Open Access | Times Cited: 32
Current advances of small molecule E3 ligands for proteolysis-targeting chimeras design
Dazhao Mi, Yuzhan Li, Haijun Gu, et al.
European Journal of Medicinal Chemistry (2023) Vol. 256, pp. 115444-115444
Closed Access | Times Cited: 27
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
Mathematical Model for Covalent Proteolysis Targeting Chimeras: Thermodynamics and Kinetics Underlying Catalytic Efficiency
Charu Chaudhry
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 9, pp. 6239-6250
Closed Access | Times Cited: 26
Degraders upgraded: the rise of PROTACs in hematological malignancies
Joshua Casan, John F. Seymour
Blood (2024) Vol. 143, Iss. 13, pp. 1218-1230
Closed Access | Times Cited: 15
Exploiting the Cullin E3 Ligase Adaptor Protein SKP1 for Targeted Protein Degradation
Seong Ho Hong, Anand Divakaran, Akane Osa, et al.
ACS Chemical Biology (2024) Vol. 19, Iss. 2, pp. 442-450
Open Access | Times Cited: 14
A CRISPR activation screen identifies FBXO22 supporting targeted protein degradation
Ananya A. Basu, Chenlu Zhang, Isabella A. Riha, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 12, pp. 1608-1616
Closed Access | Times Cited: 11
The impact of E3 ligase choice on PROTAC effectiveness in protein kinase degradation
Tomasz Sobierajski, Joanna Małolepsza, Marta Pichlak, et al.
Drug Discovery Today (2024) Vol. 29, Iss. 7, pp. 104032-104032
Open Access | Times Cited: 9
Targeted Protein Degradation: Current and Emerging Approaches for E3 Ligase Deconvolution
Yufeng Xiao, Yaxia Yuan, Yi Liu, et al.
Journal of Medicinal Chemistry (2024)
Closed Access | Times Cited: 8
Optimized mammalian expression system for the ubiquitin E3 ligase E6AP/UBE3A
Johanna M. Schafer, Christine S. Muli, Rehab A Heikal, et al.
Protein Expression and Purification (2025), pp. 106661-106661
Closed Access | Times Cited: 1
A direct high-throughput protein quantification strategy facilitates discovery and characterization of a celastrol-derived BRD4 degrader
N. Connor Payne, Semer Maksoud, Bakhos A. Tannous, et al.
Cell chemical biology (2022) Vol. 29, Iss. 8, pp. 1333-1340.e5
Open Access | Times Cited: 29
Proteomic approaches advancing targeted protein degradation
Gajanan Sathe, Gopal P. Sapkota
Trends in Pharmacological Sciences (2023) Vol. 44, Iss. 11, pp. 786-801
Open Access | Times Cited: 21
Page 1 - Next Page

Scroll to top