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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:

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: 61

Showing 1-25 of 61 citing articles:

ADP-ribosylation from molecular mechanisms to therapeutic implications
Marcin J. Suskiewicz, Evgeniia Prokhorova, J.G.M. Rack, et al.
Cell (2023) Vol. 186, Iss. 21, pp. 4475-4495
Open Access | Times Cited: 64
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
Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling
Edoardo José Longarini, Helen Dauben, Carolina Locatelli, et al.
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1743-1760.e11
Open Access | Times Cited: 37
PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities
N Mimica Dukic, Øyvind Strømland, Jonas D. Elsborg, et al.
Science Advances (2023) Vol. 9, Iss. 37
Open Access | Times Cited: 36
PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools
Morgan Dasovich, Anthony K. L. Leung
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1552-1572
Open Access | Times Cited: 32
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
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: 12
UBE2A and UBE2B are recruited by an atypical E3 ligase module in UBR4
Lucy Barnsby-Greer, Peter D. Mabbitt, Marc-André Déry, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 2, pp. 351-363
Open Access | Times Cited: 11
PARP14 is regulated by the PARP9/DTX3L complex and promotes interferon γ-induced ADP-ribosylation
Victória Chaves Ribeiro, Lilian C. Russo, Nícolas C. Hoch
The EMBO Journal (2024) Vol. 43, Iss. 14, pp. 2908-2928
Open Access | Times Cited: 8
The logic of protein post‐translational modifications (PTMs): Chemistry, mechanisms and evolution of protein regulation through covalent attachments
Marcin J. Suskiewicz
BioEssays (2024) Vol. 46, Iss. 3
Open Access | Times Cited: 7
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: 7
ADP-ribose contributions to genome stability and PARP enzyme trapping on sites of DNA damage; paradigm shifts for a coming-of-age modification
Élise Rouleau-Turcotte, John M. Pascal
Journal of Biological Chemistry (2023) Vol. 299, Iss. 12, pp. 105397-105397
Open Access | Times Cited: 20
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: 17
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
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
Nudix Hydrolase 13 Impairs the Initiation of Colorectal Cancer by Inhibiting PKM1 ADP‐Ribosylation
Jinlong Lin, Yixin Yin, Jinghua Cao, et al.
Advanced Science (2025)
Open 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
SARS-CoV-2 and UPS with potentials for therapeutic interventions
Jannatul Ferdoush, Rizwaan Abdul Kadir, Selin Simay Kaplanoglu, et al.
Gene (2024) Vol. 912, pp. 148377-148377
Closed Access | Times Cited: 3
DTX3L E3 ligase targets p53 for degradation at poly ADP-ribose polymerase-associated DNA damage sites
Qingsheng Yan, Jingyi Ding, Sumbul Jawed Khan, et al.
iScience (2023) Vol. 26, Iss. 4, pp. 106444-106444
Open Access | Times Cited: 9
Activities and binding partners of E3 ubiquitin ligase DTX3L and its roles in cancer
Carlos Vela‐Rodríguez, L. Lehtiö
Biochemical Society Transactions (2022) Vol. 50, Iss. 6, pp. 1683-1692
Closed Access | Times Cited: 15
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
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