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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:

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

Showing 1-25 of 129 citing articles:

Serine is the major residue for ADP-ribosylation upon DNA damage
Luca Palazzo, Orsolya Leidecker, Evgeniia Prokhorova, et al.
eLife (2018) Vol. 7
Open Access | Times Cited: 207
The coronavirus macrodomain is required to prevent PARP-mediated inhibition of virus replication and enhancement of IFN expression
Matthew Grunewald, Yating Chen, Chad V. Kuny, et al.
PLoS Pathogens (2019) Vol. 15, Iss. 5, pp. e1007756-e1007756
Open Access | Times Cited: 190
PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification
Marie-France Langelier, Travis Eisemann, Amanda A. Riccio, et al.
Current Opinion in Structural Biology (2018) Vol. 53, pp. 187-198
Open Access | Times Cited: 162
(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
The expanding universe of PARP1-mediated molecular and therapeutic mechanisms
Dan Huang, W. Lee Kraus
Molecular Cell (2022) Vol. 82, Iss. 12, pp. 2315-2334
Open Access | Times Cited: 158
Round, round we go – strategies for enzymatic cofactor regeneration
Silja Mordhorst, Jennifer N. Andexer
Natural Product Reports (2020) Vol. 37, Iss. 10, pp. 1316-1333
Closed Access | Times Cited: 156
Biological Properties of Vitamins of the B-Complex, Part 1: Vitamins B1, B2, B3, and B5
Marcel Hrubša, Tomáš Siatka, Iveta Nejmanová, et al.
Nutrients (2022) Vol. 14, Iss. 3, pp. 484-484
Open Access | Times Cited: 141
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
Reversible mono‐ADP‐ribosylation of DNA breaks
Deeksha Munnur, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 23, pp. 4002-4016
Open Access | Times Cited: 142
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
Reversible ADP-ribosylation of RNA
Deeksha Munnur, Edward Bartlett, Petra Mikolčević, et al.
Nucleic Acids Research (2019) Vol. 47, Iss. 11, pp. 5658-5669
Open Access | Times Cited: 134
Poly(ADP-ribose): A Dynamic Trigger for Biomolecular Condensate Formation
Anthony K. L. Leung
Trends in Cell Biology (2020) Vol. 30, Iss. 5, pp. 370-383
Open Access | Times Cited: 129
Viral Macrodomains: Unique Mediators of Viral Replication and Pathogenesis
Anthony R. Fehr, Gytis Jankevicius, Ivan Ahel, et al.
Trends in Microbiology (2017) Vol. 26, Iss. 7, pp. 598-610
Open Access | Times Cited: 114
Nuclear PARPs and genome integrity
Kameron Azarm, Susan Smith
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 285-301
Open Access | Times Cited: 98
Niacin
James B. Kirkland, Mirella L. Meyer‐Ficca
Advances in food and nutrition research (2018), pp. 83-149
Closed Access | Times Cited: 95
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
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
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: 81
ADP-ribosylation of DNA and RNA
Joséphine Groslambert, Evgeniia Prokhorova, Ivan Ahel
DNA repair (2021) Vol. 105, pp. 103144-103144
Open Access | Times Cited: 79
Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential
J.G.M. Rack, Valentina Zorzini, Zihan Zhu, et al.
Open Biology (2020) Vol. 10, Iss. 11
Open Access | Times Cited: 77
Stress granule formation, disassembly, and composition are regulated by alphavirus ADP-ribosylhydrolase activity
Aravinth Kumar Jayabalan, Srivathsan Adivarahan, Aakash Koppula, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 6
Open Access | Times Cited: 73
HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones
Fa-Hui Sun, Peng Zhao, Nan Zhang, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 66
Legionella pneumophila modulates host energy metabolism by ADP-ribosylation of ADP/ATP translocases
Jiaqi Fu, Mowei Zhou, Marina Gritsenko, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 44
Clinical PARP inhibitors allosterically induce PARP2 retention on DNA
Marie-France Langelier, Xiaohui Lin, Shan Zha, et al.
Science Advances (2023) Vol. 9, Iss. 12
Open Access | Times Cited: 32
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