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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 26-50 of 120 citing articles:

Linkage-specific deubiquitylation by OTUD5 defines an embryonic pathway intolerant to genomic variation
David B. Beck, Mohammed A. Basar, Anthony J. Asmar, et al.
Science Advances (2021) Vol. 7, Iss. 4
Open Access | Times Cited: 40
Mechanisms orchestrating the enzymatic activity and cellular functions of deubiquitinases
Benjamin Estavoyer, Clémence Messmer, Mohamed Echbicheb, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 8, pp. 102198-102198
Open Access | Times Cited: 24
Deubiquitinating enzymes: potential regulators of the tumor microenvironment and implications for immune evasion
Sheng‐Kai Hsu, Chon‐Kit Chou, I‐Ling Lin, et al.
Cell Communication and Signaling (2024) Vol. 22, Iss. 1
Open Access | Times Cited: 5
Decision for cell fate: deubiquitinating enzymes in cell cycle checkpoint
Key‐Hwan Lim, Myoung-Hyun Song, Kwang‐Hyun Baek
Cellular and Molecular Life Sciences (2016) Vol. 73, Iss. 7, pp. 1439-1455
Open Access | Times Cited: 47
Intracellular Dynamics of the Ubiquitin-Proteasome-System
Maisha Chowdhury, Cordula Enenkel
F1000Research (2015) Vol. 4, pp. 367-367
Open Access | Times Cited: 46
Structure of USP7 catalytic domain and three Ubl-domains reveals a connector α-helix with regulatory role
Robbert Q. Kim, Willem J. van Dijk, Titia K. Sixma
Journal of Structural Biology (2016) Vol. 195, Iss. 1, pp. 11-18
Open Access | Times Cited: 45
Deubiquitinase OTUD6B Isoforms Are Important Regulators of Growth and Proliferation
Anna Sobol, Caroline Askonas, Sara Alani, et al.
Molecular Cancer Research (2016) Vol. 15, Iss. 2, pp. 117-127
Open Access | Times Cited: 42
The Functional Deubiquitinating Enzymes in Control of Innate Antiviral Immunity
Zhi Zong, Zhengkui Zhang, Liming Wu, et al.
Advanced Science (2020) Vol. 8, Iss. 2
Open Access | Times Cited: 38
Small molecules that target the ubiquitin system
Hai Qiu Wu, D.A. Baker, Huib Ovaa
Biochemical Society Transactions (2020) Vol. 48, Iss. 2, pp. 479-497
Open Access | Times Cited: 36
Deubiquitylases in developmental ubiquitin signaling and congenital diseases
Mohammed A. Basar, David B. Beck, Achim Werner
Cell Death and Differentiation (2020) Vol. 28, Iss. 2, pp. 538-556
Open Access | Times Cited: 35
Mechanism of activation and regulation of deubiquitinase activity in MINDY1 and MINDY2
S.A. Abdul Rehman, Lee A. Armstrong, Sven M. Lange, et al.
Molecular Cell (2021) Vol. 81, Iss. 20, pp. 4176-4190.e6
Open Access | Times Cited: 32
Regulation of CYLD activity and specificity by phosphorylation and ubiquitin-binding CAP-Gly domains
P.R. Elliott, Derek Leske, Jane L. Wagstaff, et al.
Cell Reports (2021) Vol. 37, Iss. 1, pp. 109777-109777
Open Access | Times Cited: 31
Ubiquitin‐dependent regulation of transcription in development and disease
Kevin G. Mark, Michael Rapé
EMBO Reports (2021) Vol. 22, Iss. 4
Open Access | Times Cited: 29
The emerging role of ubiquitin-specific protease 20 in tumorigenesis and cancer therapeutics
Qiong Li, Chanqi Ye, Tian Tian, et al.
Cell Death and Disease (2022) Vol. 13, Iss. 5
Open Access | Times Cited: 22
The DUB Club: Deubiquitinating Enzymes and Neurodevelopmental Disorders
Lachlan A. Jolly, Raman Kumar, Peter Penzes, et al.
Biological Psychiatry (2022) Vol. 92, Iss. 8, pp. 614-625
Open Access | Times Cited: 21
A ubiquitin‐specific protease functions in regulating cell death and immune responses in rice
Ting Zou, Gongwen Li, Miaomiao Liu, et al.
Plant Cell & Environment (2023) Vol. 46, Iss. 4, pp. 1312-1326
Open Access | Times Cited: 11
Molecular basis for ubiquitin/Fubi cross-reactivity in USP16 and USP36
Rachel O’Dea, Nafizul Haque Kazi, Alicia Hoffmann-Benito, et al.
Nature Chemical Biology (2023) Vol. 19, Iss. 11, pp. 1394-1405
Open Access | Times Cited: 11
Regulation of Salmonella-host cell interactions via the ubiquitin system
Lina Herhaus, Ivan Ðikić
International Journal of Medical Microbiology (2017) Vol. 308, Iss. 1, pp. 176-184
Closed Access | Times Cited: 39
Intracellular Dynamics of the Ubiquitin-Proteasome-System
Maisha Chowdhury, Cordula Enenkel
F1000Research (2015) Vol. 4, pp. 367-367
Open Access | Times Cited: 38
Molecular Basis for K63-Linked Ubiquitination Processes in Double-Strand DNA Break Repair: A Focus on Kinetics and Dynamics
Brian L. Lee, Anamika Singh, J. N. Mark Glover, et al.
Journal of Molecular Biology (2017) Vol. 429, Iss. 22, pp. 3409-3429
Open Access | Times Cited: 38
USP15 regulates dynamic protein–protein interactions of the spliceosome through deubiquitination of PRP31
Tanuza Das, Joon Kyu Park, Jin‐Young Park, et al.
Nucleic Acids Research (2017), pp. gkw1365-gkw1365
Open Access | Times Cited: 37
A conserved two-step binding for the UAF1 regulator to the USP12 deubiquitinating enzyme
Shreya Dharadhar, Marcello Clerici, Willem J. van Dijk, et al.
Journal of Structural Biology (2016) Vol. 196, Iss. 3, pp. 437-447
Open Access | Times Cited: 35
Regulation of the cell cycle and centrosome biology by deubiquitylases
Sarah Darling, Andrew B. Fielding, Dorota Sabat‐Pośpiech, et al.
Biochemical Society Transactions (2017) Vol. 45, Iss. 5, pp. 1125-1136
Open Access | Times Cited: 35
The deubiquitylase USP15 regulates topoisomerase II alpha to maintain genome integrity
Andrew B. Fielding, Matthew J. Concannon, Sarah Darling, et al.
Oncogene (2018) Vol. 37, Iss. 17, pp. 2326-2342
Open Access | Times Cited: 35
Phosphorylated E2F1 is stabilized by nuclear USP11 to drive Peg10 gene expression and activate lung epithelial cells
Dan Wang, Jing Zhao, Shuang Li, et al.
Journal of Molecular Cell Biology (2017) Vol. 10, Iss. 1, pp. 60-73
Open Access | Times Cited: 34

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