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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:

Profiling DUBs and Ubl-specific proteases with activity-based probes
Paul P. Geurink, Gerbrand J. van der Heden van Noort, Monique P. C. Mulder, et al.
Methods in enzymology on CD-ROM/Methods in enzymology (2019), pp. 357-387
Open Access | Times Cited: 15

Showing 15 citing articles:

Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity
Dong Hyuk Shin, Rukmini Mukherjee, Diana Grewe, et al.
Nature (2020) Vol. 587, Iss. 7835, pp. 657-662
Open Access | Times Cited: 1082
Mechanism and inhibition of the papain‐like protease, PLpro, of SARS‐CoV‐2
Theresa Klemm, Gregor Ebert, Dale J. Calleja, et al.
The EMBO Journal (2020) Vol. 39, Iss. 18
Open Access | Times Cited: 436
CYLD in health and disease
José Luis Marín‐Rubio, Ishier Raote, Joseph Inns, et al.
Disease Models & Mechanisms (2023) Vol. 16, Iss. 6
Open Access | Times Cited: 22
Profiling expression strategies for a type III polyketide synthase in a lysate-based, cell-free system
Tien T. Sword, Jaime Lorenzo N. Dinglasan, Ghaeath S. K. Abbas, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 4
Chemical approaches to explore ubiquitin-like proteins
Reem Mousa, Doron Shkolnik, Yam Alalouf, et al.
RSC Chemical Biology (2025)
Open Access
Inhibition of papain-like protease PLpro blocks SARS-CoV-2 spread and promotes anti-viral immunity
Dong Hyuk Shin, Rukmini Mukherjee, Diana Grewe, et al.
Research Square (Research Square) (2020)
Open Access | Times Cited: 24
Deciphering non-canonical ubiquitin signaling: biology and methodology
Nila van Overbeek, Tim Aguirre, Gerbrand J. van der Heden van Noort, et al.
Frontiers in Molecular Biosciences (2024) Vol. 10
Open Access | Times Cited: 2
Mechanism and inhibition of SARS-CoV-2 PLpro
Theresa Klemm, Gregor Ebert, Dale J. Calleja, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 15
Detecting Active Deconjugating Enzymes with Genetically Encoded Activity-Based Ubiquitin and Ubiquitin-like Protein Probes
Xin Shu, Qingqing Liao, Shang‐Tong Li, et al.
Analytical Chemistry (2023)
Closed Access | Times Cited: 4
Acyl azide modification of the ubiquitin C-terminus enables DUB capture
Hua Xiao, Yanyan Guo, Yu Wang, et al.
Chemical Communications (2022) Vol. 59, Iss. 10, pp. 1333-1336
Closed Access | Times Cited: 5
USP24 is an ISG15 cross-reactive deubiquitinase that mediates IFN-I production by de-ISGylating the RNA helicase MOV10
Rishov Mukhopadhyay, Simeon D. Draganov, Jimmy J.L.L. Akkermans, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
[Expression of ubiquitin-specific protease 7 in lung tissue of preterm rats after hyperoxia exposure].
Xiaoyue Huang, Quan Yu-feng, Longli Yan, et al.
Zhongguo dangdai erke zazhi (2020) Vol. 22, Iss. 12, pp. 1331-1337
Closed Access | Times Cited: 1
Strategies for Monitoring “Ubiquitin C-Terminal Hydrolase 1” (Yuh1) Activity
Shahaf Saad, Eden Berda, Yuval Klein, et al.
Methods in molecular biology (2022), pp. 107-122
Closed Access | Times Cited: 1
The Ubiquitin-like Proteins of Saccharomyces cerevisiae
Swarnab Sengupta, Elah Pick
Biomolecules (2023) Vol. 13, Iss. 5, pp. 734-734
Open Access
Profiling Expression Strategies for a Type III Polyketide Synthase in a Lysate-Based, Cell-free System
Tien T. Sword, Jaime Lorenzo N. Dinglasan, Ghaeath S. K. Abbas, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
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