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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:

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

Showing 1-25 of 163 citing articles:

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
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
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: 219
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: 189
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: 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: 159
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: 155
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: 75
PARP1 associates with R-loops to promote their resolution and genome stability
Natalie Laspata, Parminder Kaur, Sofiane Y. Mersaoui, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 5, pp. 2215-2237
Open Access | Times Cited: 50
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: 119
Mapping Physiological ADP-Ribosylation Using Activated Ion Electron Transfer Dissociation
Sara C. Buch-Larsen, Ivo A. Hendriks, Jean M. Lodge, et al.
Cell Reports (2020) Vol. 32, Iss. 12, pp. 108176-108176
Open Access | Times Cited: 104
The Role of PARPs in Inflammation—And Metabolic—Related Diseases: Molecular Mechanisms and Beyond
Yueshuang Ke, Chenxin Wang, Jiaqi Zhang, et al.
Cells (2019) Vol. 8, Iss. 9, pp. 1047-1047
Open Access | Times Cited: 100
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
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
Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation
Ann-Katrin Hopp, Patrick Grüter, Michael O. Hottiger
Cells (2019) Vol. 8, Iss. 8, pp. 890-890
Open Access | Times Cited: 90
An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation
Juán José Bonfiglio, Orsolya Leidecker, Helen Dauben, et al.
Cell (2020) Vol. 183, Iss. 4, pp. 1086-1102.e23
Open Access | Times Cited: 90
CARM1 regulates replication fork speed and stress response by stimulating PARP1
Marie‐Michelle Genois, Jean‐Philippe Gagné, Takaaki Yasuhara, et al.
Molecular Cell (2021) Vol. 81, Iss. 4, pp. 784-800.e8
Open Access | Times Cited: 83
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: 82
The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
Ivo A. Hendriks, Sara C. Buch-Larsen, Evgeniia Prokhorova, et al.
Nature Communications (2021) Vol. 12, Iss. 1
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: 80
Serine-linked PARP1 auto-modification controls PARP inhibitor response
Evgeniia Prokhorova, Florian Zobel, Rebecca Smith, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 77
PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling
Lotte van Beek, Éilís McClay, Saleha Patel, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 10, pp. 5112-5112
Open Access | Times Cited: 68
Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets
Kelsie M. Rodriguez, Sara C. Buch-Larsen, Ilsa T. Kirby, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 63
HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase
Johannes Rudolph, Genevieve Roberts, Uma M. Muthurajan, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 60
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