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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:

Comprehensive Transcriptomic Analysis of Novel Class I HDAC Proteolysis Targeting Chimeras (PROTACs)
India M. Baker, Joshua P. Smalley, Khadija A Sabat, et al.
Biochemistry (2022) Vol. 62, Iss. 3, pp. 645-656
Open Access | Times Cited: 20

Showing 20 citing articles:

Targeting histone deacetylases for cancer therapy: Trends and challenges
Liang Tao, Fengli Wang, Reham M. Elhassan, et al.
Acta Pharmaceutica Sinica B (2023) Vol. 13, Iss. 6, pp. 2425-2463
Open Access | Times Cited: 86
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: 17
Degraders in epigenetic therapy: PROTACs and beyond
Xing‐Jie Dai, Shi‐Kun Ji, Meng‐Jie Fu, et al.
Theranostics (2024) Vol. 14, Iss. 4, pp. 1464-1499
Open Access | Times Cited: 11
Restraining the power of Proteolysis Targeting Chimeras in the cage: A necessary and important refinement for therapeutic safety
Renshuai Zhang, Songbo Xie, Jie Ran, et al.
Journal of Cellular Physiology (2024) Vol. 239, Iss. 5
Closed Access | Times Cited: 10
Collateral lethality between HDAC1 and HDAC2 exploits cancer-specific NuRD complex vulnerabilities
Yuxiang Zhang, David Remillard, Ugoma Onubogu, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 8, pp. 1160-1171
Open Access | Times Cited: 17
Histone deacetylases maintain expression of the pluripotent gene network via recruitment of RNA polymerase II to coding and noncoding loci
Richard D. Kelly, Kristy R. Stengel, Aditya Chandru, et al.
Genome Research (2024) Vol. 34, Iss. 1, pp. 34-46
Open Access | Times Cited: 6
HDAC3 and HDAC8 PROTAC dual degrader reveals roles of histone acetylation in gene regulation
Yufeng Xiao, Seth Hale, Nikee Awasthee, et al.
Cell chemical biology (2023) Vol. 30, Iss. 11, pp. 1421-1435.e12
Open Access | Times Cited: 14
An updated patent review of histone deacetylase (HDAC) inhibitors in cancer (2020 – present)
Yimin Liu, Jing‐Ping Liou
Expert Opinion on Therapeutic Patents (2023) Vol. 33, Iss. 5, pp. 349-369
Closed Access | Times Cited: 13
The application of PROTAC in HDAC
Shaoting Chen, Yuxiang Zheng, Benji Liang, et al.
European Journal of Medicinal Chemistry (2023) Vol. 260, pp. 115746-115746
Closed Access | Times Cited: 12
Overview of Class I HDAC Modulators: Inhibitors and Degraders
Ziqian Huang, Limei Zeng, Binbin Cheng, et al.
European Journal of Medicinal Chemistry (2024) Vol. 276, pp. 116696-116696
Closed Access | Times Cited: 4
Chromatin conformation, gene transcription, and nucleosome remodeling as an emergent system
Luay M. Almassalha, Marcelo A. Carignano, Emily M. Pujadas-Liwag, et al.
Science Advances (2025) Vol. 11, Iss. 2
Open Access
PROTAC chemical probes for histone deacetylase enzymes
Urvashi Patel, Joshua P. Smalley, James T. Hodgkinson
RSC Chemical Biology (2023) Vol. 4, Iss. 9, pp. 623-634
Open Access | Times Cited: 9
Targeting reversible post-translational modifications with PROTACs: a focus on enzymes modifying protein lysine and arginine residues
Marta Pichlak, Tomasz Sobierajski, K. M. Błażewska, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry (2023) Vol. 38, Iss. 1
Open Access | Times Cited: 4
Rapid degradation of histone deacetylase 1 (HDAC1) reveals essential roles in both gene repression and active transcription
David M. English, Samuel N Lee, Khadija A Sabat, et al.
Nucleic Acids Research (2024)
Open Access | Times Cited: 1
Probing Class I Histone Deacetylases (Hdac) with Proteolysis Targeting Chimera (Protac) for the Development of Highly Potent and Selective Degraders
Hany S. Ibrahim, Menglu Guo, Sebastian Hilscher, et al.
(2024)
Closed Access
Rapid degradation of Histone Deacetylase 1 (HDAC1) reveals essential roles in both gene repression and active transcription
David M. English, Samuel N Lee, Khadija A Sabat, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Probing class I histone deacetylases (HDAC) with proteolysis targeting chimera (PROTAC) for the development of highly potent and selective degraders
Hany S. Ibrahim, Menglu Guo, Sebatian Hilscher, et al.
Bioorganic Chemistry (2024) Vol. 153, pp. 107887-107887
Open Access
Cereblon-recruiting proteolysis targeting chimeras (PROTACs) can determine the selective degradation of HDAC1 over HDAC3
Aline Renata Pavan, Joshua P. Smalley, Urvashi Patel, et al.
Chemical Communications (2024)
Open Access
Collateral lethality: A unique type of synthetic lethality in cancers
Zichen Zhao, Lingling Zhu, Yu Luo, et al.
Pharmacology & Therapeutics (2024) Vol. 265, pp. 108755-108755
Closed Access
Histone Deacetylases (HDACs) maintain expression of the pluripotent gene network via recruitment of RNA polymerase II to coding and non-coding loci
RDW Kelly, KR Stengel, Aditya Chandru, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
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