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:

Development of selective small molecule MDM2 degraders based on nutlin
Bo Wang, Suzhen Wu, Jin Liu, et al.
European Journal of Medicinal Chemistry (2019) Vol. 176, pp. 476-491
Closed Access | Times Cited: 64

Showing 26-50 of 64 citing articles:

PROTACs, molecular glues and bifunctionals from bench to bedside: Unlocking the clinical potential of catalytic drugs
Marı́a Maneiro, Elena De Vita, Daniel Conole, et al.
Progress in medicinal chemistry (2021), pp. 67-190
Closed Access | Times Cited: 35

Identification of probe-quality degraders for Poly(ADP-ribose) polymerase-1 (PARP-1)
Zhimin Zhang, Xinyue Chang, Chixiao Zhang, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry (2020) Vol. 35, Iss. 1, pp. 1606-1615
Open Access | Times Cited: 34

Targeted Degradation of the Oncogenic Phosphatase SHP2
Vidyasiri Vemulapalli, Katherine A. Donovan, T.C.M. Seegar, et al.
Biochemistry (2021) Vol. 60, Iss. 34, pp. 2593-2609
Open Access | Times Cited: 31

An MDM2 degrader for treatment of acute leukemias
Bridget K. Marcellino, Xiaobao Yang, H. Ümit Kanıskan, et al.
Leukemia (2022) Vol. 37, Iss. 2, pp. 370-378
Open Access | Times Cited: 18

Design and linkage optimization of ursane-thalidomide-based PROTACs and identification of their targeted-degradation properties to MDM2 protein
Zhiwen Qi, Yang Gu-liang, Tao Deng, et al.
Bioorganic Chemistry (2021) Vol. 111, pp. 104901-104901
Closed Access | Times Cited: 25

Therapeutic Strategies to Activate p53
Angelo Aguilar, Shaomeng Wang
Pharmaceuticals (2022) Vol. 16, Iss. 1, pp. 24-24
Open Access | Times Cited: 17

Synthetic Design and Biological Evaluation of New p53-MDM2 Interaction Inhibitors Based on Imidazoline Core
Daniil R. Bazanov, Nikolay V. Pervushin, Egor V. Savin, et al.
Pharmaceuticals (2022) Vol. 15, Iss. 4, pp. 444-444
Open Access | Times Cited: 16

Small-Molecule Approaches to Target Transcription Factors
Huarui Cui, Morgan Stilgenbauer, Angela N. Koehler
Annual Review of Cancer Biology (2024) Vol. 8, Iss. 1, pp. 395-415
Closed Access | Times Cited: 2

Anticancer strategies by upregulating p53 through inhibition of its ubiquitination by MDM2
Abiodun Anifowose, Ayodeji A. Agbowuro, Xiaoxiao Yang, et al.
Medicinal Chemistry Research (2020) Vol. 29, Iss. 7, pp. 1105-1121
Closed Access | Times Cited: 20

Sulfonamide derivatives of cis-imidazolines as potent p53-MDM2/MDMX protein-protein interaction inhibitors
Daniil R. Bazanov, Nikolay V. Pervushin, Egor V. Savin, et al.
Medicinal Chemistry Research (2021) Vol. 30, Iss. 12, pp. 2216-2227
Closed Access | Times Cited: 16

Proteolysis-targeting chimeras in biotherapeutics: Current trends and future applications
Qiong Li, Li Zhou, Siyuan Qin, et al.
European Journal of Medicinal Chemistry (2023) Vol. 257, pp. 115447-115447
Closed Access | Times Cited: 6

Synthesis and Antineoplastic Activity of a Dimer, Spiroindolinone Pyrrolidinecarboxamide
Jingyi Cui, Yujie Wang, Xiaoxin Li, et al.
Molecules (2023) Vol. 28, Iss. 9, pp. 3912-3912
Open Access | Times Cited: 6

MDM2-BCL-XL PROTACs enable degradation of BCL-XL and stabilization of p53
Mengyang Chang, Feng Gao, Jing Chen, et al.
Acta Materia Medica (2022) Vol. 1, Iss. 3
Open Access | Times Cited: 10

Heterobifunctional Ligase Recruiters Enable pan-Degradation of Inhibitor of Apoptosis Proteins
Yuen Lam Dora Ng, Aleša Bricelj, Jacqueline A. Jansen, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 7, pp. 4703-4733
Open Access | Times Cited: 5

Methods for computer-assisted PROTAC design
Evianne Rovers, Matthieu Schapira
Methods in enzymology on CD-ROM/Methods in enzymology (2023), pp. 311-340
Closed Access | Times Cited: 5

Dlx3 Ubiquitination by Nuclear Mdm2 Is Essential for Dentinogenesis in Mice
Huiwen Zheng, Jian Fu, Zhi Chen, et al.
Journal of Dental Research (2022) Vol. 101, Iss. 9, pp. 1064-1074
Closed Access | Times Cited: 9

Design, synthesis, and anti-tumor activity of cyclic peptide–lenalidomide conjugated small molecules
Tingting Li, Tong Li, Xiong Zhang, et al.
New Journal of Chemistry (2024) Vol. 48, Iss. 11, pp. 4717-4725
Closed Access | Times Cited: 1

PROteolysis‐Targeting Chimeras (PROTACs) in leukemia: overview and future perspectives
André T. S. Vicente, Jorge A. R. Salvador
MedComm (2024) Vol. 5, Iss. 6
Open Access | Times Cited: 1

An update patent review of MDM2-p53 interaction inhibitors (2019–2023)
Aleksandra Twarda‐Clapa
Expert Opinion on Therapeutic Patents (2024)
Closed Access | Times Cited: 1

Chimera induced protein degradation: PROTACs and beyond
Lina Yin, Qingzhong Hu
European Journal of Medicinal Chemistry (2020) Vol. 206, pp. 112494-112494
Closed Access | Times Cited: 13

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

Manifold role of ubiquitin in Helicobacter pylori infection and gastric cancer
Olga Sokolova, Michael Naumann
Cellular and Molecular Life Sciences (2021) Vol. 78, Iss. 10, pp. 4765-4783
Open Access | Times Cited: 11

Targeted Protein Degradation: An Important Tool for Drug Discovery for “Undruggable” Tumor Transcription Factors
Mengyuan Dai, R. Sridhar, Rui Li, et al.
Technology in Cancer Research & Treatment (2022) Vol. 21
Open Access | Times Cited: 6

PROTACs: Novel approach for cancer breakdown by breaking proteins
Humera Memon, Bhoomika M. Patel
Life Sciences (2022) Vol. 300, pp. 120577-120577
Closed Access | Times Cited: 6

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