Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Ubiquitin‐targeted bacterial effectors: rule breakers of the ubiquitin system
Cameron G. Roberts, Tyler G. Franklin, Jonathan N. Pruneda
The EMBO Journal (2023) Vol. 42, Iss. 18
Open Access | Times Cited: 15

Showing 15 citing articles:

Targeting the Ubiquitin–Proteasome System and Recent Advances in Cancer Therapy
Daniela Spano, Giuliana Catara
Cells (2023) Vol. 13, Iss. 1, pp. 29-29
Open Access | Times Cited: 21
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: 9
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
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
Mechanisms and Therapeutic Strategies for NLRP3 Degradation via Post-Translational Modifications in Ubiquitin-proteasome and Autophagy Lysosomal Pathway
Kaiyue Su, Minghai Tang, Jie Wu, et al.
European Journal of Medicinal Chemistry (2025) Vol. 289, pp. 117476-117476
Closed Access
In the moonlight: non-catalytic functions of ubiquitin and ubiquitin-like proteases
Marta Campos Alonso, Klaus‐Peter Knobeloch
Frontiers in Molecular Biosciences (2024) Vol. 11
Open Access | Times Cited: 4
Specificities and redundancies in the NEL family of bacterial E3 ubiquitin ligases of Salmonella enterica serovar Typhimurium
Andrea Bullones-Bolaños, Paula Martín-Muñoz, Claudia Vallejo-Grijalba, et al.
Frontiers in Immunology (2024) Vol. 15
Open Access | Times Cited: 3
Ubiquitylation: Sword and shield in the bacterial arsenal
Jonathan N. Pruneda, Felix Randow
Molecular Cell (2024) Vol. 84, Iss. 18, pp. 3378-3380
Closed Access | Times Cited: 1
Genetic Code Expansion Approaches to Decipher the Ubiquitin Code
Vera Wanka, Maximilian Fottner, Marko Cigler, et al.
Chemical Reviews (2024) Vol. 124, Iss. 20, pp. 11544-11584
Open Access | Times Cited: 1
Discovery of ester-linked ubiquitylation of PARP10 mono-ADP-ribosylation in cells: a dual post-translational modification on Glu/Asp side chains
Daniel S. Bejan, Rachel E. Lacoursiere, Jonathan N. Pruneda, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
A family of bacterial Josephin-like deubiquitinases with an unusual cleavage mode
Thomas Hermanns, Susanne Kolek, Matthias Uthoff, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
A functional screen for ubiquitin regulation identifies an E3 ligase secreted by Pseudomonas aeruginosa
Cameron G. Roberts, Supender Kaur, Aaron J. Ogden, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Structural diversity of the CE-clan proteases in bacteria to disarm host ubiquitin defenses
Lucía Sánchez-Alba, Helena Borràs-Gas, Ge Huang, et al.
Trends in Biochemical Sciences (2024)
Open Access
Insights into ubiquitinome dynamics in the host‒pathogen interplay during Francisella novicida infection
Luyu Yang, Yanfeng Li, Qingqing Xie, et al.
Cell Communication and Signaling (2024) Vol. 22, Iss. 1
Open Access
An Emerging Way for Bacteria to Engage with Host Cells via Protein ADP-riboxanation
Wei Xian, Zhiheng Tang, Qinxin Zhang, et al.
Toxins (2024) Vol. 16, Iss. 11, pp. 467-467
Open Access
Bacterial ligases reveal fundamental principles of polyubiquitin specificity
Tyler G. Franklin, Peter S. Brzović, Jonathan N. Pruneda
Molecular Cell (2023) Vol. 83, Iss. 24, pp. 4538-4554.e4
Open Access | Times Cited: 1
Page 1

Scroll to top