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:
Molecular basis of threonine ADP-ribosylation of ubiquitin by bacterial ARTs
Jiaxing Tan, Yan Xu, Xiaofei Wang, et al.
Nature Chemical Biology (2023) Vol. 20, Iss. 4, pp. 463-472
Closed Access | Times Cited: 6
Jiaxing Tan, Yan Xu, Xiaofei Wang, et al.
Nature Chemical Biology (2023) Vol. 20, Iss. 4, pp. 463-472
Closed Access | Times Cited: 6
Showing 6 citing articles:
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
A new hybrid post-translational modification—have you lost your (MARUb)les?
Isaac de Araújo Matos, Nícolas C. Hoch
The EMBO Journal (2025)
Open Access
Isaac de Araújo Matos, Nícolas C. Hoch
The EMBO Journal (2025)
Open Access
Development of covalent probes to captureLegionella pneumophilaeffector enzymes
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Covalent Probes To Capture Legionella pneumophila Dup Effector Enzymes
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
Journal of the American Chemical Society (2024)
Open Access | Times Cited: 1
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
Journal of the American Chemical Society (2024)
Open Access | Times Cited: 1
General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase–Substrate Complexes
Hideaki Tsuge, Noriyuki Habuka, Toru Yoshida
Toxins (2024) Vol. 16, Iss. 7, pp. 313-313
Open Access
Hideaki Tsuge, Noriyuki Habuka, Toru Yoshida
Toxins (2024) Vol. 16, Iss. 7, pp. 313-313
Open Access
Crystal structure of bacterial ubiquitin ADP-ribosyltransferase CteC reveals a substrate-recruiting insertion
Zhengrui Zhang, Hannah M. Rondon-Cordero, Chittaranjan Das
Journal of Biological Chemistry (2023) Vol. 300, Iss. 2, pp. 105604-105604
Open Access | Times Cited: 1
Zhengrui Zhang, Hannah M. Rondon-Cordero, Chittaranjan Das
Journal of Biological Chemistry (2023) Vol. 300, Iss. 2, pp. 105604-105604
Open Access | Times Cited: 1
