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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:

Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases
Chatrin Chatrin, Mads Gabrielsen, Lori Buetow, et al.
Science Advances (2020) Vol. 6, Iss. 38
Open Access | Times Cited: 77

Showing 1-25 of 77 citing articles:

ADP‐ribosyltransferases, an update on function and nomenclature
Bernhard Lüscher, Ivan Ahel, Matthias Altmeyer, et al.
FEBS Journal (2021) Vol. 289, Iss. 23, pp. 7399-7410
Open Access | Times Cited: 236
An expanded lexicon for the ubiquitin code
Ivan Đikić, Brenda A. Schulman
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 4, pp. 273-287
Open Access | Times Cited: 223
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: 16
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 | Times Cited: 3
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
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: 67
A new dawn beyond lysine ubiquitination
Daniel R. Squair, Satpal Virdee
Nature Chemical Biology (2022) Vol. 18, Iss. 8, pp. 802-811
Closed Access | Times Cited: 60
Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44
An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes
Haithem Barbour, Nadine Sen Nkwe, Benjamin Estavoyer, et al.
iScience (2023) Vol. 26, Iss. 5, pp. 106276-106276
Open Access | Times Cited: 25
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: 24
KH-like Domains in PARP9/DTX3L and PARP14 Coordinate Protein–Protein Interactions to Promote Cancer Cell Survival
H. Saleh, Triantafillos Liloglou, Daniel J. Rigden, et al.
Journal of Molecular Biology (2024) Vol. 436, Iss. 4, pp. 168434-168434
Open Access | Times Cited: 12
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: 9
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: 8
Sugar-mediated non-canonical ubiquitination impairs Nrf1/NFE2L1 activation
Yasuko Yoshida, Tsuyoshi Takahashi, Nozomi Ishii, et al.
Molecular Cell (2024) Vol. 84, Iss. 16, pp. 3115-3127.e11
Closed Access | Times Cited: 8
Reconstitution of the DTX3L–PARP9 complex reveals determinants for high-affinity heterodimerization and multimeric assembly
Yashwanth Ashok, Carlos Vela‐Rodríguez, Chunsong Yang, et al.
Biochemical Journal (2022) Vol. 479, Iss. 3, pp. 289-304
Open Access | Times Cited: 34
DTX3L induced NLRP3 ubiquitination inhibit R28 cell pyroptosis in OGD/R injury
Ziyu Zhou, Lei Shang, Qí Zhāng, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2023) Vol. 1870, Iss. 3, pp. 119433-119433
Open Access | Times Cited: 21
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: 20
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: 19
The mechanism of linear ubiquitination in regulating cell death and correlative diseases
Liyuan Gao, Wei Zhang, Xiao Hui Shi, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 10
Open Access | Times Cited: 19
NUDT16 regulates CtIP PARylation to dictate homologous recombination repair
Zhen Zhang, William E. Samsa, Zihua Gong
Nucleic Acids Research (2024) Vol. 52, Iss. 7, pp. 3761-3777
Open Access | Times Cited: 8
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: 7
Functions and Molecular Mechanisms of Deltex Family Ubiquitin E3 Ligases in Development and Disease
Lidong Wang, Xiaodan Sun, Jingni He, et al.
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 33
Beyond protein modification: the rise of non-canonical ADP-ribosylation
M. Schuller, Ivan Ahel
Biochemical Journal (2022) Vol. 479, Iss. 4, pp. 463-477
Open Access | Times Cited: 27
Medicinal Chemistry Perspective on Targeting Mono-ADP-Ribosylating PARPs with Small Molecules
Maria Giulia Nizi, Mirko M. Maksimainen, L. Lehtiö, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 11, pp. 7532-7560
Open Access | Times Cited: 25
[1,2,4]Triazolo[3,4-b]benzothiazole Scaffold as Versatile Nicotinamide Mimic Allowing Nanomolar Inhibition of Different PARP Enzymes
Sudarshan Murthy, Maria Giulia Nizi, Mirko M. Maksimainen, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 2, pp. 1301-1320
Open Access | Times Cited: 15
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