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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:

Quantitative site-specific ADP-ribosylation profiling of DNA-dependent PARPs
Jean‐Philippe Gagné, Chantal Éthier, Daniel Defoy, et al.
DNA repair (2015) Vol. 30, pp. 68-79
Closed Access | Times Cited: 62

Showing 1-25 of 62 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
PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain
Jennine M. Dawicki-McKenna, Marie-France Langelier, Jamie E. DeNizio, et al.
Molecular Cell (2015) Vol. 60, Iss. 5, pp. 755-768
Open Access | Times Cited: 301
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
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: 224
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 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
Poly(ADP-ribose) polymerase-1 antagonizes DNA resection at double-strand breaks
Marie‐Christine Caron, Ajit Kumar Sharma, Julia O’Sullivan, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 156
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
Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation
Gabriella Zarkovic, E. A. Belousova, Ibtissam Talhaoui, et al.
Nucleic Acids Research (2017) Vol. 46, Iss. 5, pp. 2417-2431
Open Access | Times Cited: 105
PARPs in lipid metabolism and related diseases
Magdolna Szántó, Rebecca Gupte, W. Lee Kraus, et al.
Progress in Lipid Research (2021) Vol. 84, pp. 101117-101117
Open Access | Times Cited: 102
The Viral Macrodomain Counters Host Antiviral ADP-Ribosylation
Yousef M. Alhammad, Anthony R. Fehr
Viruses (2020) Vol. 12, Iss. 4, pp. 384-384
Open Access | Times Cited: 99
PARP1 orchestrates epigenetic events setting up chromatin domains
Fabio Ciccarone, Michele Zampieri, Paola Caiafa
Seminars in Cell and Developmental Biology (2016) Vol. 63, pp. 123-134
Open Access | Times Cited: 96
Rapid Detection and Signaling of DNA Damage by PARP-1
Nootan Pandey, Ben E. Black
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 9, pp. 744-757
Open Access | Times Cited: 88
ADP-ribosylation of RNA and DNA: fromin vitrocharacterization toin vivofunction
Lisa Weixler, Katja Schäringer, Jeffrey Momoh, et al.
Nucleic Acids Research (2021) Vol. 49, Iss. 7, pp. 3634-3650
Open Access | Times Cited: 68
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
PARP1: Structural insights and pharmacological targets for inhibition
Jacob O. Spiegel, Bennett Van Houten, Jacob D. Durrant
DNA repair (2021) Vol. 103, pp. 103125-103125
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
HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications
Marie-France Langelier, Ramya Billur, Aleksandr Sverzhinsky, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 56
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
PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response
L. B. Aberle, Annika Krüger, Julia M. Reber, et al.
Nucleic Acids Research (2020) Vol. 48, Iss. 18, pp. 10015-10033
Open Access | Times Cited: 60
Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling
Pietro Fontana, Sara C. Buch-Larsen, Osamu Suyari, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 19
Specific and shared biological functions of PARP2 – is PARP2 really a lil’ brother of PARP1?
Magdolna Szántó, José Yélamos, Péter Bai
Expert Reviews in Molecular Medicine (2024) Vol. 26
Open Access | Times Cited: 8
The Nucleolus and PARP1 in Cancer Biology
Marina Engbrecht, Aswin Mangerich
Cancers (2020) Vol. 12, Iss. 7, pp. 1813-1813
Open Access | Times Cited: 48
Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity
Pamlea N. Brady, Anupam Goel, Margaret A. Johnson
Microbiology and Molecular Biology Reviews (2019) Vol. 83, Iss. 1
Open Access | Times Cited: 46
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