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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:

The function and regulation of OTU deubiquitinases
Jiansen Du, Lin Fu, Yingli Sui, et al.
Frontiers of Medicine (2019) Vol. 14, Iss. 5, pp. 542-563
Open Access | Times Cited: 55

Showing 1-25 of 55 citing articles:

Pharmaceutical targeting of OTUB2 sensitizes tumors to cytotoxic T cells via degradation of PD-L1
W. Ren, Zilong Xu, Yating Chang, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 17
Regulation of Wnt Signaling through Ubiquitination and Deubiquitination in Cancers
Hong‐Beom Park, Ju-Won Kim, Kwang‐Hyun Baek
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 11, pp. 3904-3904
Open Access | Times Cited: 117
Pharmacological suppression of the OTUD4/CD73 proteolytic axis revives antitumor immunity against immune-suppressive breast cancers
Yueming Zhu, Anupam Banerjee, Ping Xie, et al.
Journal of Clinical Investigation (2024) Vol. 134, Iss. 10
Open Access | Times Cited: 9
Identification and characterization of diverse OTU deubiquitinases in bacteria
Alexander F. Schubert, Justine Nguyen, Tyler G. Franklin, et al.
The EMBO Journal (2020) Vol. 39, Iss. 15
Open Access | Times Cited: 63
Deubiquitinating enzyme OTUB1 in immunity and cancer: Good player or bad actor?
Yihao Liao, Mengyue Yang, Keke Wang, et al.
Cancer Letters (2021) Vol. 526, pp. 248-258
Closed Access | Times Cited: 41
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: 19
Divergence of Legionella Effectors Reversing Conventional and Unconventional Ubiquitination
Tomoe Kitao, Hiroki Nagai, Tomoko Kubori
Frontiers in Cellular and Infection Microbiology (2020) Vol. 10
Open Access | Times Cited: 37
The structure and function of deubiquitinases: lessons from budding yeast
Harsha Garadi Suresh, Natasha Pascoe, Brenda Andrews
Open Biology (2020) Vol. 10, Iss. 10
Open Access | Times Cited: 36
Pleiotropic Roles of a KEAP1-Associated Deubiquitinase, OTUD1
Daisuke Oikawa, Kouhei Shimizu, Fuminori Tokunaga
Antioxidants (2023) Vol. 12, Iss. 2, pp. 350-350
Open Access | Times Cited: 12
Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2
Ken Ikeuchi, Nives Ivić, Robert Buschauer, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 11
TRIM21/USP15 balances ACSL4 stability and the imatinib resistance of gastrointestinal stromal tumors
Zhiwei Cui, Haoyu Sun, Zhishuang Gao, et al.
British Journal of Cancer (2024) Vol. 130, Iss. 4, pp. 526-541
Closed Access | Times Cited: 4
Dapagliflozin suppressed gastric cancer growth via regulating OTUD5 mediated YAP1 deubiquitination
Kaijie Ren, Xueni Wang, Rulan Ma, et al.
European Journal of Pharmacology (2024), pp. 177002-177002
Open Access | Times Cited: 4
Activation and Reactivity of the Deubiquitinylase OTU Cezanne-2 from MD Simulations and QM/MM Calculations
Metehan Ilter, Andrés M. Escorcia, Eric Schulze, et al.
Journal of Chemical Information and Modeling (2025)
Open Access
Enantioselective OTUD7B fragment discovery through chemoproteomics screening and high-throughput optimisation
Aini Vuorinen, Cassandra R. Kennedy, Katherine McPhie, et al.
Communications Chemistry (2025) Vol. 8, Iss. 1
Open Access
The ubiquitin–proteasome system: A potential target for the MASLD
Zhaoyu Li, Meijia Qian, Yonghao Li, et al.
Acta Pharmaceutica Sinica B (2025)
Open Access
Otud6a Knockout Leads to Male Subfertility in Mice
Fu-Chen Yang, Zhuangfei Wang, Danyang Li, et al.
Molecular Reproduction and Development (2025) Vol. 92, Iss. 3
Closed Access
Bourbon and Mycbp function with Otu to promote Sxl protein expression in the Drosophila female germline
Marianne Mercer, Anirban Dasgupta, Krzysztof Pawłowski, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 15
Open Access
The deubiquitinase YOD1 suppresses tumor progression by stabilizing ZNF24 in clear cell renal carcinoma
Ji Liu, Ying Lu, Rui Zhu, et al.
Cell Death and Disease (2025) Vol. 16, Iss. 1
Open Access
Zebrafish otud6b Negatively Regulates Antiviral Responses by Suppressing K63-Linked Ubiquitination of irf3 and irf7
Ziwen Zhou, Xiaolian Cai, Junji Zhu, et al.
The Journal of Immunology (2021) Vol. 207, Iss. 1, pp. 244-256
Open Access | Times Cited: 24
OTUD6A promotes prostate tumorigenesis via deubiquitinating Brg1 and AR
Xuhong Fu, Junjie Zhao, Guopeng Yu, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 17
The Regulation and Double-Edged Roles of the Deubiquitinase OTUD5
Lin Fu, Kun Lu, Qian Jiao, et al.
Cells (2023) Vol. 12, Iss. 8, pp. 1161-1161
Open Access | Times Cited: 10
Exploring the Role of Ubiquitin-Proteasome System in the Pathogenesis of Parkinson’s Disease
Yiting Zhao, Man Lin, Fengguang Zhai, et al.
Pharmaceuticals (2024) Vol. 17, Iss. 6, pp. 782-782
Open Access | Times Cited: 3
The role of USP1 deubiquitinase in the pathogenesis and therapy of cancer
Svitlana Antonenko, М.П. Завелевич, Г. Д. Телегеев
Acta Biochimica Polonica (2023)
Open Access | Times Cited: 9
Plant deubiquitinases: from structure and activity to biological functions
Runbang Luo, Kun Yang, Wei Xiao
Plant Cell Reports (2022) Vol. 42, Iss. 3, pp. 469-486
Closed Access | Times Cited: 13
Characterisation of the OTU domain deubiquitinase complement ofToxoplasma gondii
Mary‐Louise Wilde, Ushma Ruparel, Theresa Klemm, et al.
Life Science Alliance (2023) Vol. 6, Iss. 6, pp. e202201710-e202201710
Open Access | Times Cited: 7
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