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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:

Layers of DUB regulation
Danny D. Sahtoe, Titia K. Sixma
Trends in Biochemical Sciences (2015) Vol. 40, Iss. 8, pp. 456-467
Closed Access | Times Cited: 120

Showing 1-25 of 120 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: 857
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: 731
Ubiquitylation at the crossroads of development and disease
Michael Rapé
Nature Reviews Molecular Cell Biology (2017) Vol. 19, Iss. 1, pp. 59-70
Closed Access | Times Cited: 515
Deubiquitinating enzymes (DUBs): Regulation, homeostasis, and oxidative stress response
Nathan A. Snyder, Gustavo M. Silva
Journal of Biological Chemistry (2021) Vol. 297, Iss. 3, pp. 101077-101077
Open Access | Times Cited: 178
BAP1/ASXL1 recruitment and activation for H2A deubiquitination
Danny D. Sahtoe, Willem J. van Dijk, Reggy Ekkebus, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 176
Deubiquitinases in cancer
Grant Dewson, Pieter J.A. Eichhorn, David Komander
Nature reviews. Cancer (2023) Vol. 23, Iss. 12, pp. 842-862
Closed Access | Times Cited: 110
USP19 modulates autophagy and antiviral immune responses by deubiquitinating Beclin‐1
Shouheng Jin, Shuo Tian, Yamei Chen, et al.
The EMBO Journal (2016) Vol. 35, Iss. 8, pp. 866-880
Open Access | Times Cited: 154
USP7 and USP47 deubiquitinases regulate NLRP3 inflammasome activation
Pablo Palazón‐Riquelme, Jonathan D. Worboys, Jack Green, et al.
EMBO Reports (2018) Vol. 19, Iss. 10
Open Access | Times Cited: 149
SPATA2 Links CYLD to LUBAC, Activates CYLD, and Controls LUBAC Signaling
P.R. Elliott, Derek Leske, Matouš Hrdinka, et al.
Molecular Cell (2016) Vol. 63, Iss. 6, pp. 990-1005
Open Access | Times Cited: 141
The Interplay of Cofactor Interactions and Post-translational Modifications in the Regulation of the AAA+ ATPase p97
Petra Hänzelmann, Hermann Schindelin
Frontiers in Molecular Biosciences (2017) Vol. 4
Open Access | Times Cited: 131
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: 113
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
USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A
Michael Uckelmann, Ruth M. Densham, Roy Baas, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 92
Dissenting degradation: Deubiquitinases in cell cycle and cancer
Thomas Bonacci, Michael J. Emanuele
Seminars in Cancer Biology (2020) Vol. 67, pp. 145-158
Open Access | Times Cited: 92
Chemical and semisynthetic approaches to study and target deubiquitinases
Pushparathinam Gopinath, Shimrit Ohayon, Mickal Nawatha, et al.
Chemical Society Reviews (2016) Vol. 45, Iss. 15, pp. 4171-4198
Open Access | Times Cited: 87
Assembly and function of branched ubiquitin chains
SriDurgaDevi Kolla, Mengchen Ye, Kevin G. Mark, et al.
Trends in Biochemical Sciences (2022) Vol. 47, Iss. 9, pp. 759-771
Open Access | Times Cited: 65
Post-Translational Modifications of Deubiquitinating Enzymes: Expanding the Ubiquitin Code
Yanfeng Wang, Feng Wang
Frontiers in Pharmacology (2021) Vol. 12
Open Access | Times Cited: 64
UFMylation: A Unique & Fashionable Modification for Life
Ying Wei, Xingzhi Xu
Genomics Proteomics & Bioinformatics (2016) Vol. 14, Iss. 3, pp. 140-146
Open Access | Times Cited: 79
USP4 Auto-Deubiquitylation Promotes Homologous Recombination
Paul W.G. Wijnhoven, Rebecca Konietzny, Andrew N. Blackford, et al.
Molecular Cell (2015) Vol. 60, Iss. 3, pp. 362-373
Open Access | Times Cited: 75
Cezanne/ OTUD 7B is a cell cycle‐regulated deubiquitinase that antagonizes the degradation of APC /C substrates
Thomas Bonacci, Aussie Suzuki, Gavin D. Grant, et al.
The EMBO Journal (2018) Vol. 37, Iss. 16
Open Access | Times Cited: 74
Functional analysis of deubiquitylating enzymes in tumorigenesis and development
Ji Cheng, Jianping Guo, Brian J. North, et al.
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer (2019) Vol. 1872, Iss. 2, pp. 188312-188312
Closed Access | Times Cited: 66
Targeting Pink1-Parkin-mediated mitophagy for treating liver injury
Jessica A. Williams, Wen‐Xing Ding
Pharmacological Research (2015) Vol. 102, pp. 264-269
Open Access | Times Cited: 59
M1-linked ubiquitination by LUBEL is required for inflammatory responses to oral infection in Drosophila
Anna L. Aalto, Aravind K. Mohan, Lukas Schwintzer, et al.
Cell Death and Differentiation (2018) Vol. 26, Iss. 5, pp. 860-876
Open Access | Times Cited: 58
Ubiquitin Ligases in Cancer Immunotherapy – Balancing Antitumor and Autoimmunity
Yu Fujita, Roberto Tinoco, Yan Li, et al.
Trends in Molecular Medicine (2019) Vol. 25, Iss. 5, pp. 428-443
Open Access | Times Cited: 45
Regulation of Deubiquitinating Enzymes by Post-Translational Modifications
Tanuza Das, Sang Chul Shin, Eun Joo Song, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 11, pp. 4028-4028
Open Access | Times Cited: 43
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