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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:

Deubiquitinating enzyme amino acid profiling reveals a class of ubiquitin esterases
Virginia De Cesare, Daniel Carbajo, Peter D. Mabbitt, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 4
Open Access | Times Cited: 74

Showing 1-25 of 74 citing articles:

An expanded lexicon for the ubiquitin code
Ivan Đikić, Brenda A. Schulman
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 4, pp. 273-287
Open Access | Times Cited: 225
Deubiquitinases: From mechanisms to their inhibition by small molecules
Sven M. Lange, Lee A. Armstrong, Yogesh Kulathu
Molecular Cell (2021) Vol. 82, Iss. 1, pp. 15-29
Open Access | Times Cited: 190
Ubiquitin is directly linked via an ester to protein-conjugated mono-ADP-ribose
Daniel S. Bejan, Rachel E. Lacoursiere, Jonathan N. Pruneda, et al.
The EMBO Journal (2025)
Open Access | Times Cited: 3
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on protein substrates
Kang Zhu, Marcin J. Suskiewicz, Andrea Hloušek-Kasun, et al.
Science Advances (2022) Vol. 8, Iss. 40
Open Access | Times Cited: 67
A new dawn beyond lysine ubiquitination
Daniel R. Squair, Satpal Virdee
Nature Chemical Biology (2022) Vol. 18, Iss. 8, pp. 802-811
Closed Access | Times Cited: 60
Mechanism-based traps enable protease and hydrolase substrate discovery
Shan Tang, Adam T. Beattie, Lucie Kafková, et al.
Nature (2022) Vol. 602, Iss. 7898, pp. 701-707
Open Access | Times Cited: 48
Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Edoardo José Longarini, Ivan Matić
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 15
Bacterial esterases reverse lipopolysaccharide ubiquitylation to block host immunity
Magdalena Szczesna, Yizhou Huang, Rachel E. Lacoursiere, et al.
Cell Host & Microbe (2024) Vol. 32, Iss. 6, pp. 913-924.e7
Open Access | Times Cited: 13
The emerging roles of non-canonical ubiquitination in proteostasis and beyond
Yoshino Akizuki, Stephanie Kaypee, Fumiaki Ohtake, et al.
The Journal of Cell Biology (2024) Vol. 223, Iss. 5
Open Access | Times Cited: 10
Discovery and characterization of noncanonical E2-conjugating enzymes
S.A. Abdul Rehman, Chiara Cazzaniga, Elena Di Nisio, et al.
Science Advances (2024) Vol. 10, Iss. 13
Open Access | Times Cited: 10
VCP/p97-associated proteins are binders and debranching enzymes of K48–K63-branched ubiquitin chains
Sven M. Lange, Matthew R. McFarland, Frédéric Lamoliatte, et al.
Nature Structural & Molecular Biology (2024)
Open Access | Times Cited: 10
E2–Ub-R74G strategy reveals E2-specific ubiquitin conjugation profiles in live cells
Siqi Shen, Hang Yin
Nature Chemical Biology (2025)
Closed Access | Times Cited: 1
A family of bacterial Josephin-like deubiquitinases with an irreversible cleavage mode
Thomas Hermanns, Susanne Kolek, Matthias Uthoff, et al.
Molecular Cell (2025)
Open Access | Times Cited: 1
The linear ubiquitin chain assembly complex (LUBAC) generates heterotypic ubiquitin chains
Alan Rodriguez Carvajal, Irina Grishkovskaya, Carlos Gómez-Díaz, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 48
Ubiquitination of non-protein substrates
Jun-Ichi Sakamaki, Noboru Mizushima
Trends in Cell Biology (2023) Vol. 33, Iss. 11, pp. 991-1003
Open Access | Times Cited: 20
Chemical methods for protein site-specific ubiquitination
Weijun Gui, Gregory A. Davidson, Zhihao Zhuang
RSC Chemical Biology (2021) Vol. 2, Iss. 2, pp. 450-467
Open Access | Times Cited: 34
Targeting PTEN Regulation by Post Translational Modifications
Ana González-Garcı́a, António Garrido, Ana C. Carrera
Cancers (2022) Vol. 14, Iss. 22, pp. 5613-5613
Open Access | Times Cited: 23
Comprehensive approach to study branched ubiquitin chains reveals roles for K48-K63 branches in VCP/p97-related processes
Sven M. Lange, Matthew R. McFarland, Frédéric Lamoliatte, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 16
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
PSMD14 stabilizes estrogen signaling and facilitates breast cancer progression via deubiquitinating ERα
Penghe Yang, Yang Xiao, Dehai Wang, et al.
Oncogene (2023) Vol. 43, Iss. 4, pp. 248-264
Open Access | Times Cited: 12
Specificity profiling of deubiquitylases against endogenously generated ubiquitin-protein conjugates
Valentina Rossio, João A. Paulo, Xinyue Liu, et al.
Cell chemical biology (2024) Vol. 31, Iss. 7, pp. 1349-1362.e5
Closed Access | Times Cited: 4
The RBR E3 ubiquitin ligase HOIL-1 can ubiquitinate diverse non-protein substrates in vitro
Xiangyi S. Wang, Jenny Jiou, Anthony Cerra, et al.
Life Science Alliance (2025) Vol. 8, Iss. 6, pp. e202503243-e202503243
Open Access
Insights into non-proteinaceous ubiquitination
Emily L Dearlove, Danny T. Huang
Biochemical Society Transactions (2025) Vol. 53, Iss. 02
Open Access
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