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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-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

Showing 1-25 of 216 citing articles:

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: 212
Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts
Arda Celen, Umut Şahin
FEBS Journal (2020) Vol. 287, Iss. 15, pp. 3110-3140
Open Access | Times Cited: 184
Targeting protein modifications in metabolic diseases: molecular mechanisms and targeted therapies
Xiumei Wu, Mengyun Xu, M. Geng, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 103
Mechanisms and functions of SUMOylation in health and disease: a review focusing on immune cells
Chien-Hsin Huang, Tsan-Tzu Yang, Kuo‐I Lin
Journal of Biomedical Science (2024) Vol. 31, Iss. 1
Open Access | Times Cited: 35
SUMO proteases: from cellular functions to disease
Laura A. Claessens, Alfred C.O. Vertegaal
Trends in Cell Biology (2024) Vol. 34, Iss. 11, pp. 901-912
Closed Access | Times Cited: 19
The Nuclear SUMO-Targeted Ubiquitin Quality Control Network Regulates the Dynamics of Cytoplasmic Stress Granules
Jan Keiten‐Schmitz, Kristina Wagner, Tanja Piller, et al.
Molecular Cell (2020) Vol. 79, Iss. 1, pp. 54-67.e7
Closed Access | Times Cited: 102
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
Sumoylation in Physiology, Pathology and Therapy
Umut Şahin, Hugues de Thé, Valérie Lallemand-Breitenbach
Cells (2022) Vol. 11, Iss. 5, pp. 814-814
Open Access | Times Cited: 52
Activated SUMOylation restricts MHC class I antigen presentation to confer immune evasion in cancer
Uta M. Demel, Marlitt Böger, Schayan Yousefian, et al.
Journal of Clinical Investigation (2022) Vol. 132, Iss. 9
Open Access | Times Cited: 51
Glioblastoma upregulates SUMOylation of hnRNP A2/B1 to eliminate the tumor suppressor miR-204-3p, accelerating angiogenesis under hypoxia
Qindong Guo, Fan Yang, Qingtong Wang, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 2
Open Access | Times Cited: 33
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
The multiple roles of interferon regulatory factor family in health and disease
Luyao Wang, Yanghui Zhu, Nan Zhang, et al.
Signal Transduction and Targeted Therapy (2024) Vol. 9, Iss. 1
Open Access | Times Cited: 15
SUMO4 promotes SUMO deconjugation required for DNA double-strand-break repair
Alexander J. Garvin, Alexander J. Lanz, George E. Ronson, et al.
Molecular Cell (2025) Vol. 85, Iss. 5, pp. 877-893.e9
Open Access | Times Cited: 1
Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility
Chongyang Li, Francis P. McManus, Cédric Plutoni, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 64
The SUMO Isopeptidase SENP6 Functions as a Rheostat of Chromatin Residency in Genome Maintenance and Chromosome Dynamics
Kristina Wagner, Kathrin Kunz, Tanja Piller, et al.
Cell Reports (2019) Vol. 29, Iss. 2, pp. 480-494.e5
Open Access | Times Cited: 58
The COP9 Signalosome: A Multi-DUB Complex
Wolfgang Dubiel, Supattra Chaithongyot, Dawadschargal Dubiel, et al.
Biomolecules (2020) Vol. 10, Iss. 7, pp. 1082-1082
Open Access | Times Cited: 58
SUMOylation modification-mediated cell death
Zenghua Sheng, Jing Zhu, Yanan Deng, et al.
Open Biology (2021) Vol. 11, Iss. 7
Open Access | Times Cited: 56
SUMO: Glue or Solvent for Phase-Separated Ribonucleoprotein Complexes and Molecular Condensates?
Jan Keiten‐Schmitz, Linda Röder, Eran Hornstein, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 53
Therapeutic Potential of Targeting the SUMO Pathway in Cancer
Antti Kukkula, Veera K. Ojala, Lourdes M. Mendez, et al.
Cancers (2021) Vol. 13, Iss. 17, pp. 4402-4402
Open Access | Times Cited: 49
Hepatic Small Ubiquitin‐Related Modifier (SUMO)–Specific Protease 2 Controls Systemic Metabolism Through SUMOylation‐Dependent Regulation of Liver–Adipose Tissue Crosstalk
Yang Liu, Xin Dou, Wei-Yu Zhou, et al.
Hepatology (2021) Vol. 74, Iss. 4, pp. 1864-1883
Closed Access | Times Cited: 44
Fatty acids produced by the gut microbiota dampen host inflammatory responses by modulating intestinal SUMOylation
Chaima Ezzine, Léa Loison, Nadine Montbrion, et al.
Gut Microbes (2022) Vol. 14, Iss. 1
Open Access | Times Cited: 34
SUMOylation of HNRNPA2B1 modulates RPA dynamics during unperturbed replication and genotoxic stress responses
Shouhai Zhu, Jing Hou, Huanyao Gao, et al.
Molecular Cell (2023) Vol. 83, Iss. 4, pp. 539-555.e7
Open Access | Times Cited: 21
Identification and classification of papain-like cysteine proteinases
Fatih Ozhelvaci, Kamil Steczkiewicz
Journal of Biological Chemistry (2023) Vol. 299, Iss. 6, pp. 104801-104801
Open Access | Times Cited: 20
SENP6 regulates localization and nuclear condensation of DNA damage response proteins by group deSUMOylation
Laura A. Claessens, Matty Verlaan–de Vries, Ilona J. de Graaf, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 20
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