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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:

Intracellular Mono-ADP-Ribosylation in Signaling and Disease
Mareike Bütepage, Laura Eckei, Patricia Verheugd, et al.
Cells (2015) Vol. 4, Iss. 4, pp. 569-595
Open Access | Times Cited: 91

Showing 1-25 of 91 citing articles:

Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
Jian Lei, Yuri Kusov, Rolf Hilgenfeld
Antiviral Research (2017) Vol. 149, pp. 58-74
Open Access | Times Cited: 721
ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease
Bernhard Lüscher, Mareike Bütepage, Laura Eckei, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1092-1136
Closed Access | Times Cited: 222
Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
Rita Martello, Mario Leutert, Stephanie Jungmichel, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 212
Serine ADP-ribosylation reversal by the hydrolase ARH3
Pietro Fontana, Juán José Bonfiglio, Luca Palazzo, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 165
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: 139
The conserved macrodomains of the non-structural proteins of Chikungunya virus and other pathogenic positive strand RNA viruses function as mono-ADP-ribosylhydrolases
Laura Eckei, Sarah Krieg, Mareike Bütepage, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 134
ADP‐ribosylation: new facets of an ancient modification
Luca Palazzo, Andreja Mikoč, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 18, pp. 2932-2946
Open Access | Times Cited: 129
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: 115
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
Specificity of reversible ADP-ribosylation and regulation of cellular processes
Kerryanne Crawford, Juán José Bonfiglio, Andreja Mikoč, et al.
Critical Reviews in Biochemistry and Molecular Biology (2017) Vol. 53, Iss. 1, pp. 64-82
Closed Access | Times Cited: 91
MARTs and MARylation in the Cytosol: Biological Functions, Mechanisms of Action, and Therapeutic Potential
Sridevi Challa, MiKayla S Stokes, W. Lee Kraus
Cells (2021) Vol. 10, Iss. 2, pp. 313-313
Open Access | Times Cited: 56
Biallelic Mutations in ADPRHL2, Encoding ADP-Ribosylhydrolase 3, Lead to a Degenerative Pediatric Stress-Induced Epileptic Ataxia Syndrome
Shereen G. Ghosh, Kerstin Becker, He Huang, et al.
The American Journal of Human Genetics (2018) Vol. 103, Iss. 3, pp. 431-439
Open Access | Times Cited: 77
TiPARP forms nuclear condensates to degrade HIF-1α and suppress tumorigenesis
Lu Zhang, Ji Cao, Longying Dong, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 24, pp. 13447-13456
Open Access | Times Cited: 65
Protein Modifications as Manifestations of Hyperglycemic Glucotoxicity in Diabetes and Its Complications
Hong Zheng, Jinzi Wu, Zhen Jin, et al.
Biochemistry Insights (2016) Vol. 9, pp. BCI.S36141-BCI.S36141
Open Access | Times Cited: 63
Small-Molecule Chemical Probe Rescues Cells from Mono-ADP-Ribosyltransferase ARTD10/PARP10-Induced Apoptosis and Sensitizes Cancer Cells to DNA Damage
Harikanth Venkannagari, Patricia Verheugd, Jarkko Koivunen, et al.
Cell chemical biology (2016) Vol. 23, Iss. 10, pp. 1251-1260
Open Access | Times Cited: 63
Identification of evolutionary and kinetic drivers of NAD-dependent signaling
Mathias Bockwoldt, Dorothée Houry, Marc Niere, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 32, pp. 15957-15966
Open Access | Times Cited: 56
ADP-ribosylation systems in bacteria and viruses
Petra Mikolčević, Andrea Hloušek-Kasun, Ivan Ahel, et al.
Computational and Structural Biotechnology Journal (2021) Vol. 19, pp. 2366-2383
Open Access | Times Cited: 48
Thioparib inhibits homologous recombination repair, activates the type I IFN response, and overcomes olaparib resistance
Limin Wang, Pingyuan Wang, X. T. Chen, et al.
EMBO Molecular Medicine (2023) Vol. 15, Iss. 3
Open Access | Times Cited: 21
In vivo vizualisation of mono-ADP-ribosylation by dPARP16 upon amino-acid starvation
Angelica Aguilera-Gomez, Marinke M. van Oorschot, Tineke Veenendaal, et al.
eLife (2016) Vol. 5
Open Access | Times Cited: 55
Therapeutic applications of PARP inhibitors in ovarian cancer
Hongyu Xie, Wenjie Wang, Bairong Xia, et al.
Biomedicine & Pharmacotherapy (2020) Vol. 127, pp. 110204-110204
Open Access | Times Cited: 39
PARP7 and Mono-ADP-Ribosylation Negatively Regulate Estrogen Receptor α Signaling in Human Breast Cancer Cells
Marit Rasmussen, Susanna Tan, Venkata S. Somisetty, et al.
Cells (2021) Vol. 10, Iss. 3, pp. 623-623
Open Access | Times Cited: 34
Mono-ADP-ribosylation by PARP10 inhibits Chikungunya virus nsP2 proteolytic activity and viral replication
Sarah Krieg, Fabian Pott, Laura Potthoff, et al.
Cellular and Molecular Life Sciences (2023) Vol. 80, Iss. 3
Open Access | Times Cited: 14
Nicotinamide Adenine Dinucleotide and Signaling Transduction
Haidong Xu, Dingmei Zhang, Meiling Sun, et al.
(2025), pp. 239-268
Closed Access
Characterization of TCDD-inducible poly-ADP-ribose polymerase (TIPARP/ARTD14) catalytic activity
Alvin Gomez, Christian Bindesbøll, Somisetty V. Satheesh, et al.
Biochemical Journal (2018) Vol. 475, Iss. 23, pp. 3827-3846
Open Access | Times Cited: 46
Uncovering the Invisible: Mono-ADP-ribosylation Moved into the Spotlight
Ann-Katrin Hopp, Michael O. Hottiger
Cells (2021) Vol. 10, Iss. 3, pp. 680-680
Open Access | Times Cited: 27
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