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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:

SUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage
Ivo A. Hendriks, Louise W. Treffers, Matty Verlaan–de Vries, et al.
Cell Reports (2015) Vol. 10, Iss. 10, pp. 1778-1791
Open Access | Times Cited: 131

Showing 1-25 of 131 citing articles:

A comprehensive compilation of SUMO proteomics
Ivo A. Hendriks, Alfred C.O. Vertegaal
Nature Reviews Molecular Cell Biology (2016) Vol. 17, Iss. 9, pp. 581-595
Closed Access | Times Cited: 442
SUMO and the robustness of cancer
Jacob-S. Seeler, Anne Dejean
Nature reviews. Cancer (2017) Vol. 17, Iss. 3, pp. 184-197
Closed Access | Times Cited: 364
Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation
Ivo A. Hendriks, David Lyon, Clifford Young, et al.
Nature Structural & Molecular Biology (2017) Vol. 24, Iss. 3, pp. 325-336
Closed Access | Times Cited: 336
Regulation of DNA double-strand break repair by ubiquitin and ubiquitin-like modifiers
Petra Schwertman, Simon Bekker‐Jensen, Niels Mailand
Nature Reviews Molecular Cell Biology (2016) Vol. 17, Iss. 6, pp. 379-394
Closed Access | Times Cited: 327
SUMOylation-Mediated Regulation of Cell Cycle Progression and Cancer
Karolin Eifler, Alfred C.O. Vertegaal
Trends in Biochemical Sciences (2015) Vol. 40, Iss. 12, pp. 779-793
Open Access | Times Cited: 260
Histone demethylases in chromatin biology and beyond
Emilia Dimitrova, Anne H. Turberfield, Robert J. Klose
EMBO Reports (2015) Vol. 16, Iss. 12, pp. 1620-1639
Open Access | Times Cited: 197
Histone methylation and the DNA damage response
Fade Gong, Kyle M. Miller
Mutation Research/Reviews in Mutation Research (2017) Vol. 780, pp. 37-47
Open Access | Times Cited: 192
Site-specific characterization of endogenous SUMOylation across species and organs
Ivo A. Hendriks, David Lyon, Dan Su, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 187
Spatiotemporal regulation of posttranslational modifications in the DNA damage response
Nico P. Dantuma, Haico van Attikum
The EMBO Journal (2015) Vol. 35, Iss. 1, pp. 6-23
Open Access | Times Cited: 183
Sumo and the cellular stress response
Jorrit M. Enserink
Cell Division (2015) Vol. 10, Iss. 1
Open Access | Times Cited: 165
A proteomics landscape of circadian clock in mouse liver
Yunzhi Wang, Lei Song, Mingwei Liu, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 142
Uncovering the SUMOylation and ubiquitylation crosstalk in human cells using sequential peptide immunopurification
Frédéric Lamoliatte, Francis P. McManus, Ghizlane Maarifi, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 133
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
Structural Insights Into TDP-43 and Effects of Post-translational Modifications
Liberty François‐Moutal, Samantha Perez‐Miller, David D. Scott, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 123
The STUbL RNF4 regulates protein group SUMOylation by targeting the SUMO conjugation machinery
Ramesh Kumar, Román González‐Prieto, Zhenyu Xiao, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 107
JARID1 Histone Demethylases: Emerging Targets in Cancer
Kayla M. Harmeyer, Nicole D. Facompre, Meenhard Herlyn, et al.
Trends in cancer (2017) Vol. 3, Iss. 10, pp. 713-725
Open Access | Times Cited: 90
Preserving genome integrity and function: the DNA damage response and histone modifications
Jae Jin Kim, Seo Yun Lee, Kyle M. Miller
Critical Reviews in Biochemistry and Molecular Biology (2019) Vol. 54, Iss. 3, pp. 208-241
Open Access | Times Cited: 85
A Chain of Events: Regulating Target Proteins by SUMO Polymers
Nicolette S. Jansen, Alfred C.O. Vertegaal
Trends in Biochemical Sciences (2020) Vol. 46, Iss. 2, pp. 113-123
Open Access | Times Cited: 72
SUMO and Transcriptional Regulation: The Lessons of Large-Scale Proteomic, Modifomic and Genomic Studies
Mathias Boulanger, Mehuli Chakraborty, Denis Tempé, et al.
Molecules (2021) Vol. 26, Iss. 4, pp. 828-828
Open Access | Times Cited: 62
Dynamic SUMOylation of MORC2 orchestrates chromatin remodelling and DNA repair in response to DNA damage and drives chemoresistance in breast cancer
Fanglin Zhang, Shao‐Ying Yang, Li Liao, et al.
Theranostics (2023) Vol. 13, Iss. 3, pp. 973-990
Open Access | Times Cited: 24
Deubiquitinase USP7 stabilizes KDM5B and promotes tumor progression and cisplatin resistance in nasopharyngeal carcinoma through the ZBTB16/TOP2A axis
Bin Zhang, Jie Li, Yijun Wang, et al.
Cell Death and Differentiation (2024) Vol. 31, Iss. 3, pp. 309-321
Open Access | Times Cited: 15
Immune regulation by the SUMO family
M.D. Neranjan Tharuka, Asimina S. Courelli, Yuan Chen
Nature reviews. Immunology (2025)
Closed Access | Times Cited: 1
The functional roles of PML nuclear bodies in genome maintenance
Hae Ryung Chang, Anudari Munkhjargal, Myung-Jin Kim, et al.
Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis (2017) Vol. 809, pp. 99-107
Closed Access | Times Cited: 87
Global Reprogramming of Host SUMOylation during Influenza Virus Infection
Patricia Domingues, Filip Gołębiowski, Michael H. Tatham, et al.
Cell Reports (2015) Vol. 13, Iss. 7, pp. 1467-1480
Open Access | Times Cited: 85
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
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