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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:

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

Showing 1-25 of 219 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: 724
NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential
Na Xie, Lu Zhang, Wei Gao, et al.
Signal Transduction and Targeted Therapy (2020) Vol. 5, Iss. 1
Open Access | Times Cited: 653
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
PARP Inhibitors: Clinical Relevance, Mechanisms of Action and Tumor Resistance
Maddison Rose, Joshua T. Burgess, Kenneth J. O’Byrne, et al.
Frontiers in Cell and Developmental Biology (2020) Vol. 8
Open Access | Times Cited: 515
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
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
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
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
HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation
Marcin J. Suskiewicz, Florian Zobel, T.E.H. Ogden, et al.
Nature (2020) Vol. 579, Iss. 7800, pp. 598-602
Open Access | Times Cited: 217
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
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
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
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
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: 153
HPF1-dependent histone ADP-ribosylation triggers chromatin relaxation to promote the recruitment of repair factors at sites of DNA damage
Rebecca Smith, Siham Zentout, Magdalena B. Rother, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 5, pp. 678-691
Open Access | Times Cited: 45
Poly(ADP-ribosyl)ation enhances nucleosome dynamics and organizes DNA damage repair components within biomolecular condensates
Michael L. Nosella, Tae Hun Kim, Shuya Kate Huang, et al.
Molecular Cell (2024) Vol. 84, Iss. 3, pp. 429-446.e17
Closed Access | Times Cited: 21
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
PARP2 mediates branched poly ADP-ribosylation in response to DNA damage
Qian Chen, Muzaffer Ahmad Kassab, Françoise Dantzer, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 147
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): 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
Bridging of DNA breaks activates PARP2–HPF1 to modify chromatin
Silvija Bilokapić, Marcin J. Suskiewicz, Ivan Ahel, et al.
Nature (2020) Vol. 585, Iss. 7826, pp. 609-613
Open Access | Times Cited: 118
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