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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:

An Activity-Guided Map of Electrophile-Cysteine Interactions in Primary Human T Cells
Ekaterina V. Vinogradova, Xiaoyu Zhang, David Remillard, et al.
Cell (2020) Vol. 182, Iss. 4, pp. 1009-1026.e29
Open Access | Times Cited: 272

Showing 1-25 of 272 citing articles:

The cGAS–STING pathway as a therapeutic target in inflammatory diseases
Alexiane Decout, Jason D. Katz, Shankar Venkatraman, et al.
Nature reviews. Immunology (2021) Vol. 21, Iss. 9, pp. 548-569
Open Access | Times Cited: 1224
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: 429
Bioorthogonal chemistry
Samuel L. Scinto, Didier A. Bilodeau, Robert Hincapie, et al.
Nature Reviews Methods Primers (2021) Vol. 1, Iss. 1
Open Access | Times Cited: 321
Reimagining high-throughput profiling of reactive cysteines for cell-based screening of large electrophile libraries
Miljan Kuljanin, Dylan C. Mitchell, Devin K. Schweppe, et al.
Nature Biotechnology (2021) Vol. 39, Iss. 5, pp. 630-641
Open Access | Times Cited: 235
A proteome-wide atlas of lysine-reactive chemistry
Mikail E. Abbasov, Madeline E. Kavanagh, Taka-Aki Ichu, et al.
Nature Chemistry (2021) Vol. 13, Iss. 11, pp. 1081-1092
Open Access | Times Cited: 170
DCAF11 Supports Targeted Protein Degradation by Electrophilic Proteolysis-Targeting Chimeras
Xiaoyu Zhang, Lena Luukkonen, Christie L. Eissler, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 13, pp. 5141-5149
Open Access | Times Cited: 135
Reimagining Druggability Using Chemoproteomic Platforms
Jessica N. Spradlin, Erika Zhang, Daniel K. Nomura
Accounts of Chemical Research (2021) Vol. 54, Iss. 7, pp. 1801-1813
Closed Access | Times Cited: 120
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: 102
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: 79
Systematic identification of anticancer drug targets reveals a nucleus-to-mitochondria ROS-sensing pathway
Junbing Zhang, Claire Simpson, Jacqueline Berner, et al.
Cell (2023) Vol. 186, Iss. 11, pp. 2361-2379.e25
Closed Access | Times Cited: 79
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: 63
Proteomic discovery of chemical probes that perturb protein complexes in human cells
Michael R. Lazear, Jarrett R. Remsberg, Martin G. Jaeger, et al.
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1725-1742.e12
Open Access | Times Cited: 62
CysDB: a human cysteine database based on experimental quantitative chemoproteomics
Lisa M. Boatner, Maria F. Palafox, Devin K. Schweppe, et al.
Cell chemical biology (2023) Vol. 30, Iss. 6, pp. 683-698.e3
Open Access | Times Cited: 51
Expanding Chemical Probe Space: Quality Criteria for Covalent and Degrader Probes
Ingo V. Hartung, Joachim Rudolph, Mary M. Mader, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 14, pp. 9297-9312
Open Access | Times Cited: 47
Remodeling oncogenic transcriptomes by small molecules targeting NONO
Stefan G. Kathman, Seong Joo Koo, Garrett L. Lindsey, et al.
Nature Chemical Biology (2023) Vol. 19, Iss. 7, pp. 825-836
Open Access | Times Cited: 45
Current understanding of the cGAS-STING signaling pathway: Structure, regulatory mechanisms, and related diseases
Jing Pan, Chen-Jie Fei, Yang Hu, et al.
动物学研究 (2023) Vol. 44, Iss. 1, pp. 183-218
Open Access | Times Cited: 43
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: 42
Mechanism and therapeutic potential of targeting cGAS-STING signaling in neurological disorders
Yige Huang, Bangyan Liu, Subhash C. Sinha, et al.
Molecular Neurodegeneration (2023) Vol. 18, Iss. 1
Open Access | Times Cited: 36
cGAS–STING, an important signaling pathway in diseases and their therapy
Qijie Li, Ping Wu, Qiujing Du, et al.
MedComm (2024) Vol. 5, Iss. 4
Open Access | Times Cited: 16
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: 15
DAMP sensing and sterile inflammation: intracellular, intercellular and inter-organ pathways
Yi Huang, Wei Jiang, Rongbin Zhou
Nature reviews. Immunology (2024) Vol. 24, Iss. 10, pp. 703-719
Closed Access | Times Cited: 15
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: 13
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: 13
Global Reactivity Profiling of the Catalytic Lysine in Human Kinome for Covalent Inhibitor Development
Guanghui Tang, Wei Wang, Chengjun Zhu, et al.
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 12
Closed Access | Times Cited: 12
Agonists and Inhibitors of the cGAS-STING Pathway
Xiaoxuan Yu, Linxiang Cai, Jingyue Yao, et al.
Molecules (2024) Vol. 29, Iss. 13, pp. 3121-3121
Open Access | Times Cited: 12
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