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:

DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids
Kang Zhu, Marcin J. Suskiewicz, Chatrin Chatrin, et al.
Nucleic Acids Research (2023) Vol. 52, Iss. 2, pp. 801-815
Open Access | Times Cited: 21

Showing 21 citing articles:

PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation
Pulak Kar, Chatrin Chatrin, N Mimica Dukic, et al.
The EMBO Journal (2024) Vol. 43, Iss. 14, pp. 2929-2953
Open Access | Times Cited: 15

Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 1

Just how big is the ubiquitin system?
Bernhard C. Lechtenberg, David Komander
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 2, pp. 210-213
Closed Access | Times Cited: 6

DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids
Emily L Dearlove, Chatrin Chatrin, Lori Buetow, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 6

DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids
Emily L Dearlove, Chatrin Chatrin, Lori Buetow, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 5

RING dimerisation drives higher‐order organisation of SINA/SIAH E3 ubiquitin ligases
F Coste, Aanchal Mishra, Catherine Chapuis, et al.
FEBS Journal (2025)
Closed Access

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

Deltex family E3 ligases specifically ubiquitinate the terminal ADP-ribose of poly(ADP-ribosyl)ation
Matt Kelly, Chase Dietz, Samuel Kasson, et al.
Biochemical and Biophysical Research Communications (2024) Vol. 720, pp. 150101-150101
Open Access | Times Cited: 2

Capturing Legionella pneumophila effector enzymes using a ubiquitin derived photo-activatable probe
Max S. Kloet, Gerbrand J. van der Heden van Noort
Frontiers in Molecular Biosciences (2024) Vol. 11
Open Access | Times Cited: 2

Ubiquitylation of nucleic acids by DELTEX ubiquitin E3 ligase DTX3L
Kang Zhu, Chatrin Chatrin, Marcin J. Suskiewicz, et al.
EMBO Reports (2024) Vol. 25, Iss. 10, pp. 4172-4189
Open Access | Times Cited: 2

Mono-ADP-ribosylation, a MARylationmultifaced modification of protein, DNA and RNA: characterizations, functions and mechanisms
Hao Wu, Anqi Lu, Jiuzhi Yuan, et al.
Cell Death Discovery (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 1

DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids
Emily L Dearlove, Chatrin Chatrin, Lori Buetow, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

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

An E3 ubiquitin ligase localization screen uncovers DTX2 as a novel ADP-ribosylation-dependent regulator of DNA double-strand break repair
Billel Djerir, Isabelle Marois, Jean-Christophe Dubois, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 8, pp. 107545-107545
Open Access

DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids
Emily L Dearlove, Chatrin Chatrin, Lori Buetow, et al.
(2024)
Open Access

Insights into mechanisms of ubiquitin ADP-ribosylation reversal
Zhengrui Zhang, Chittaranjan Das
Biochemical Society Transactions (2024)
Closed Access

Understanding ubiquitination in neurodevelopment by integrating insights across space and time
Mateusz C. Ambrozkiewicz, Sonja Lorenz
Nature Structural & Molecular Biology (2024)
Closed Access

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