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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 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

Showing 1-25 of 315 citing articles:

NAD+ in Brain Aging and Neurodegenerative Disorders
Sofie Lautrup, David Sinclair, Mark P. Mattson, et al.
Cell Metabolism (2019) Vol. 30, Iss. 4, pp. 630-655
Open Access | Times Cited: 560
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
Poly(ADP-ribose) polymerase inhibition: past, present and future
Nicola J. Curtin, Csaba Szabó
Nature Reviews Drug Discovery (2020) Vol. 19, Iss. 10, pp. 711-736
Closed Access | Times Cited: 403
Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins
Elizaveta E. Alemasova, Olga I. Lavrik
Nucleic Acids Research (2019) Vol. 47, Iss. 8, pp. 3811-3827
Open Access | Times Cited: 387
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
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
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
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
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
DNA single-strand break repair and human genetic disease
Keith W. Caldecott
Trends in Cell Biology (2022) Vol. 32, Iss. 9, pp. 733-745
Closed Access | Times Cited: 109
Inhibitors of PARP: Number crunching and structure gazing
Johannes Rudolph, Karen Jung, Karolin Luger
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 11
Open Access | Times Cited: 85
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
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
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
The Enigmatic Function of PARP1: From PARylation Activity to PAR Readers
Tatiana Kamaletdinova, Zahra Fanaei‐Kahrani, Zhao‐Qi Wang
Cells (2019) Vol. 8, Iss. 12, pp. 1625-1625
Open Access | Times Cited: 133
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