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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:

Processing of protein ADP-ribosylation by Nudix hydrolases
Luca Palazzo, Benjamin Thomas, Ann‐Sofie Jemth, et al.
Biochemical Journal (2015) Vol. 468, Iss. 2, pp. 293-301
Open Access | Times Cited: 125

Showing 1-25 of 125 citing articles:

PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Rebecca Gupte, Ziying Liu, W. Lee Kraus
Genes & Development (2017) Vol. 31, Iss. 2, pp. 101-126
Open Access | Times Cited: 618
Serine ADP-Ribosylation Depends on HPF1
Juán José Bonfiglio, Pietro Fontana, Qi Zhang, et al.
Molecular Cell (2017) Vol. 65, Iss. 5, pp. 932-940.e6
Open Access | Times Cited: 315
Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination
Sagar Bhogaraju, Sissy Kalayil, Yaobin Liu, et al.
Cell (2016) Vol. 167, Iss. 6, pp. 1636-1649.e13
Open Access | Times Cited: 281
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
Structures and Mechanisms of Enzymes Employed in the Synthesis and Degradation of PARP-Dependent Protein ADP-Ribosylation
Eva Barkauskaite, Gytis Jankevicius, Ivan Ahel
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 935-946
Open Access | Times Cited: 242
Readers of poly(ADP-ribose): designed to be fit for purpose
Federico Teloni, Matthias Altmeyer
Nucleic Acids Research (2015) Vol. 44, Iss. 3, pp. 993-1006
Open Access | Times Cited: 226
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: 223
Serine is a new target residue for endogenous ADP-ribosylation on histones
Orsolya Leidecker, Juán José Bonfiglio, Thomas Colby, et al.
Nature Chemical Biology (2016) Vol. 12, Iss. 12, pp. 998-1000
Open Access | Times Cited: 219
Macrodomains: Structure, Function, Evolution, and Catalytic Activities
J.G.M. Rack, Dragutin Perina, Ivan Ahel
Annual Review of Biochemistry (2016) Vol. 85, Iss. 1, pp. 431-454
Open Access | Times Cited: 204
The role of poly ADP-ribosylation in the first wave of DNA damage response
Chao Liu, Aditi Vyas, Muzaffer Ahmad Kassab, et al.
Nucleic Acids Research (2017) Vol. 45, Iss. 14, pp. 8129-8141
Open Access | Times Cited: 198
The Promise of Proteomics for the Study of ADP-Ribosylation
Casey M. Daniels, Shao-En Ong, Anthony K. L. Leung
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 911-924
Open Access | Times Cited: 193
A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication
Kristin M. Kotewicz, Vinay Ramabhadran, Nicole M. Sjoblom, et al.
Cell Host & Microbe (2016) Vol. 21, Iss. 2, pp. 169-181
Open Access | Times Cited: 187
ADP-ribosylhydrolase activity of Chikungunya virus macrodomain is critical for virus replication and virulence
Robert Lyle McPherson, Rachy Abraham, Easwaran Sreekumar, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 7, pp. 1666-1671
Open Access | Times Cited: 176
(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
Shigella evades pyroptosis by arginine ADP-riboxanation of caspase-11
Zilin Li, Wang Liu, Jiaqi Fu, et al.
Nature (2021) Vol. 599, Iss. 7884, pp. 290-295
Open Access | Times Cited: 153
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: 72
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
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
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
Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragmentsin vitro
Ibtissam Talhaoui, Н. А. Лебедева, Gabriella Zarkovic, et al.
Nucleic Acids Research (2016), pp. gkw675-gkw675
Open Access | Times Cited: 116
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
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