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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:

USP7 is a SUMO deubiquitinase essential for DNA replication
Emilio Lecona, Sara Rodríguez‐Acebes, Julia Specks, et al.
Nature Structural & Molecular Biology (2016) Vol. 23, Iss. 4, pp. 270-277
Open Access | Times Cited: 131

Showing 1-25 of 131 citing articles:

Mechanisms of Deubiquitinase Specificity and Regulation
Tycho E.T. Mevissen, David Komander
Annual Review of Biochemistry (2017) Vol. 86, Iss. 1, pp. 159-192
Open Access | Times Cited: 861
Deubiquitylating enzymes and drug discovery: emerging opportunities
Jeanine A. Harrigan, Xavier Jacq, Niall M.B. Martin, et al.
Nature Reviews Drug Discovery (2017) Vol. 17, Iss. 1, pp. 57-78
Open Access | Times Cited: 734
The post-translational modification, SUMOylation, and cancer (Review)
Zhi‐Jian Han, Yan-Hu Feng, Bao-Hong Gu, et al.
International Journal of Oncology (2018)
Open Access | Times Cited: 292
SUMO-specific proteases and isopeptidases of the SENP family at a glance
Kathrin Kunz, Tanja Piller, Stefan Müller
Journal of Cell Science (2018) Vol. 131, Iss. 6
Open Access | Times Cited: 216
Signalling mechanisms and cellular functions of SUMO
Alfred C.O. Vertegaal
Nature Reviews Molecular Cell Biology (2022) Vol. 23, Iss. 11, pp. 715-731
Closed Access | Times Cited: 211
SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes
Xiaolan Zhao
Molecular Cell (2018) Vol. 71, Iss. 3, pp. 409-418
Open Access | Times Cited: 205
DNA replication fork speed underlies cell fate changes and promotes reprogramming
Tsunetoshi Nakatani, Jiangwei Lin, Fei Ji, et al.
Nature Genetics (2022) Vol. 54, Iss. 3, pp. 318-327
Open Access | Times Cited: 71
USP7 - a crucial regulator of cancer hallmarks
Gouranga Saha, Srija Roy, Malini Basu, et al.
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer (2023) Vol. 1878, Iss. 3, pp. 188903-188903
Closed Access | Times Cited: 47
USP1 Is Required for Replication Fork Protection in BRCA1-Deficient Tumors
Kah Suan Lim, Heng Li, Emma A. Roberts, et al.
Molecular Cell (2018) Vol. 72, Iss. 6, pp. 925-941.e4
Open Access | Times Cited: 140
Hemi-methylated DNA regulates DNA methylation inheritance through allosteric activation of H3 ubiquitylation by UHRF1
Joseph S. Harrison, Evan M. Cornett, Dennis Goldfarb, et al.
eLife (2016) Vol. 5
Open Access | Times Cited: 133
USP7: Structure, substrate specificity, and inhibition
Alexandra Pozhidaeva, Irina Bezsonova
DNA repair (2019) Vol. 76, pp. 30-39
Open Access | Times Cited: 121
Advances in Deubiquitinating Enzyme Inhibition and Applications in Cancer Therapeutics
Ainsley Mike Antao, Apoorvi Tyagi, Kye-Seong Kim, et al.
Cancers (2020) Vol. 12, Iss. 6, pp. 1579-1579
Open Access | Times Cited: 115
A Systems-Level Study Reveals Regulators of Membrane-less Organelles in Human Cells
Doris Berchtold, Nico Battich, Lucas Pelkmans
Molecular Cell (2018) Vol. 72, Iss. 6, pp. 1035-1049.e5
Open Access | Times Cited: 108
Functional Analysis of the Replication Fork Proteome Identifies BET Proteins as PCNA Regulators
Sarah R. Wessel, Kareem N. Mohni, Jessica W. Luzwick, et al.
Cell Reports (2019) Vol. 28, Iss. 13, pp. 3497-3509.e4
Open Access | Times Cited: 108
USP7: Novel Drug Target in Cancer Therapy
Zhiru Wang, Wen-Ting Kang, Yinghua You, et al.
Frontiers in Pharmacology (2019) Vol. 10
Open Access | Times Cited: 106
Regulation of USP7: A High Incidence of E3 Complexes
Robbert Q. Kim, Titia K. Sixma
Journal of Molecular Biology (2017) Vol. 429, Iss. 22, pp. 3395-3408
Open Access | Times Cited: 93
Mechanisms of DNA Damage Tolerance: Post-Translational Regulation of PCNA
Wendy Leung, Ryan M. Baxley, George‐Lucian Moldovan, et al.
Genes (2018) Vol. 10, Iss. 1, pp. 10-10
Open Access | Times Cited: 90
Modulation of the p53/MDM2 interplay by HAUSP inhibitors
Omid Tavana, Wei Gu
Journal of Molecular Cell Biology (2016) Vol. 9, Iss. 1, pp. 45-52
Open Access | Times Cited: 89
Post-translational Modifications of Key Machinery in the Control of Mitophagy
Liming Wang, Hao Qi, Yancheng Tang, et al.
Trends in Biochemical Sciences (2019) Vol. 45, Iss. 1, pp. 58-75
Closed Access | Times Cited: 88
USP7 Is a Master Regulator of Genome Stability
Gabrielle J. Valles, Irina Bezsonova, Roger Woodgate, et al.
Frontiers in Cell and Developmental Biology (2020) Vol. 8
Open Access | Times Cited: 84
Global non-covalent SUMO interaction networks reveal SUMO-dependent stabilization of the non-homologous end joining complex
Román González‐Prieto, Karolin Eifler-Olivi, Laura A. Claessens, et al.
Cell Reports (2021) Vol. 34, Iss. 4, pp. 108691-108691
Open Access | Times Cited: 59
Insights in Post-Translational Modifications: Ubiquitin and SUMO
Daniel Salas‐Lloret, Román González‐Prieto
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 6, pp. 3281-3281
Open Access | Times Cited: 54
Concerted SUMO-targeted ubiquitin ligase activities of TOPORS and RNF4 are essential for stress management and cell proliferation
Julio C.Y. Liu, Leena Ackermann, Saskia Hoffmann, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 9, pp. 1355-1367
Open Access | Times Cited: 11
Ubiquitin-dependent and independent roles of SUMO in proteostasis
Frauke Liebelt, Alfred C.O. Vertegaal
AJP Cell Physiology (2016) Vol. 311, Iss. 2, pp. C284-C296
Open Access | Times Cited: 83
Identification and Characterization of MCM3 as a Kelch-like ECH-associated Protein 1 (KEAP1) Substrate
Kathleen M. Mulvaney, Jacob P. Matson, Priscila F. Siesser, et al.
Journal of Biological Chemistry (2016) Vol. 291, Iss. 45, pp. 23719-23733
Open Access | Times Cited: 79
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