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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:

Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
Jeannette Abplanalp, Mario Leutert, Emilie Frugier, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 116

Showing 1-25 of 116 citing articles:

Understanding and overcoming resistance to PARP inhibitors in cancer therapy
Mariana Paes Dias, Sarah C. Moser, Shridar Ganesan, et al.
Nature Reviews Clinical Oncology (2021) Vol. 18, Iss. 12, pp. 773-791
Closed Access | Times Cited: 359
The comings and goings of PARP-1 in response to DNA damage
John M. Pascal
DNA repair (2018) Vol. 71, pp. 177-182
Open Access | Times Cited: 299
Insights into the biogenesis, function, and regulation of ADP-ribosylation
Michael S. Cohen, Paul Chang
Nature Chemical Biology (2018) Vol. 14, Iss. 3, pp. 236-243
Open Access | Times Cited: 272
Cellular functions of the protein kinase ATM and their relevance to human disease
Ji‐Hoon Lee, Tanya T. Paull
Nature Reviews Molecular Cell Biology (2021) Vol. 22, Iss. 12, pp. 796-814
Closed Access | Times Cited: 186
Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation
Sara C. Buch-Larsen, Ivo A. Hendriks, David Lyon, et al.
Cell Reports (2018) Vol. 24, Iss. 9, pp. 2493-2505.e4
Open Access | Times Cited: 163
(ADP-ribosyl)hydrolases: structure, function, and biology
J.G.M. Rack, Luca Palazzo, Ivan Ahel
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 263-284
Open Access | Times Cited: 159
An Advanced Strategy for Comprehensive Profiling of ADP-ribosylation Sites Using Mass Spectrometry-based Proteomics*
Ivo A. Hendriks, Sara C. Buch-Larsen, Michael L. Nielsen
Molecular & Cellular Proteomics (2019) Vol. 18, Iss. 5, pp. 1010a-1026
Open Access | Times Cited: 155
Emerging roles of eraser enzymes in the dynamic control of protein ADP-ribosylation
Julia O’Sullivan, Maria Tedim Ferreira, Jean‐Philippe Gagné, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 141
Mapping Physiological ADP-Ribosylation Using Activated Ion Electron Transfer Dissociation
Sara C. Buch-Larsen, Ivo A. Hendriks, Jean M. Lodge, et al.
Cell Reports (2020) Vol. 32, Iss. 12, pp. 108176-108176
Open Access | Times Cited: 104
PARPs in lipid metabolism and related diseases
Magdolna Szántó, Rebecca Gupte, W. Lee Kraus, et al.
Progress in Lipid Research (2021) Vol. 84, pp. 101117-101117
Open Access | Times Cited: 102
ADP-ribosylation signalling and human disease
Luca Palazzo, Petra Mikolčević, Andreja Mikoč, et al.
Open Biology (2019) Vol. 9, Iss. 4
Open Access | Times Cited: 92
Interplay of Histone Marks with Serine ADP-Ribosylation
Edward Bartlett, Juán José Bonfiglio, Evgeniia Prokhorova, et al.
Cell Reports (2018) Vol. 24, Iss. 13, pp. 3488-3502.e5
Open Access | Times Cited: 91
Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation
Ann-Katrin Hopp, Patrick Grüter, Michael O. Hottiger
Cells (2019) Vol. 8, Iss. 8, pp. 890-890
Open Access | Times Cited: 90
An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation
Juán José Bonfiglio, Orsolya Leidecker, Helen Dauben, et al.
Cell (2020) Vol. 183, Iss. 4, pp. 1086-1102.e23
Open Access | Times Cited: 90
Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease
Evgeniia Prokhorova, Thomas Agnew, Anne R. Wondisford, et al.
Molecular Cell (2021) Vol. 81, Iss. 12, pp. 2640-2655.e8
Open Access | Times Cited: 82
The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
Ivo A. Hendriks, Sara C. Buch-Larsen, Evgeniia Prokhorova, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 81
Serine-linked PARP1 auto-modification controls PARP inhibitor response
Evgeniia Prokhorova, Florian Zobel, Rebecca Smith, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 77
ADP-ribosylation of RNA and DNA: fromin vitrocharacterization toin vivofunction
Lisa Weixler, Katja Schäringer, Jeffrey Momoh, et al.
Nucleic Acids Research (2021) Vol. 49, Iss. 7, pp. 3634-3650
Open Access | Times Cited: 68
PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling
Lotte van Beek, Éilís McClay, Saleha Patel, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 10, pp. 5112-5112
Open Access | Times Cited: 68
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: 38
A viral ADP-ribosyltransferase attaches RNA chains to host proteins
Maik Wolfram-Schauerte, Nadiia Pozhydaieva, Julia Grawenhoff, et al.
Nature (2023) Vol. 620, Iss. 7976, pp. 1054-1062
Open Access | Times Cited: 29
Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation
Kyuto Tashiro, Sven Wijngaarden, Jugal Mohapatra, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 25, pp. 14000-14009
Open Access | Times Cited: 25
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: 16
Mitotic chromatin marking governs the segregation of DNA damage
Juliette Ferrand, Juliette Dabin, Odile Chevallier, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
Maneuvers on PCNA Rings during DNA Replication and Repair
Dea Slade
Genes (2018) Vol. 9, Iss. 8, pp. 416-416
Open Access | Times Cited: 79
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