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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:

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

Showing 1-25 of 387 citing articles:

The Role of Post-Translational Modifications in the Phase Transitions of Intrinsically Disordered Proteins
Izzy Owen, Frank Shewmaker
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 21, pp. 5501-5501
Open Access | Times Cited: 190
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
TIR-catalyzed ADP-ribosylation reactions produce signaling molecules for plant immunity
Aolin Jia, Shijia Huang, Wen Song, et al.
Science (2022) Vol. 377, Iss. 6605
Open Access | Times Cited: 154
Targeting PARP proteins in acute leukemia: DNA damage response inhibition and therapeutic strategies
Antonella Padella, Andrea Ghelli Luserna di Rorà, Giovanni Marconi, et al.
Journal of Hematology & Oncology (2022) Vol. 15, Iss. 1
Open Access | Times Cited: 71
PARP1-DNA co-condensation drives DNA repair site assembly to prevent disjunction of broken DNA ends
Nagaraja Chappidi, Thomas Quail, Simon Doll, et al.
Cell (2024) Vol. 187, Iss. 4, pp. 945-961.e18
Open Access | Times Cited: 50
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
AutoGrow4: an open-source genetic algorithm for de novo drug design and lead optimization
Jacob O. Spiegel, Jacob D. Durrant
Journal of Cheminformatics (2020) Vol. 12, Iss. 1
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
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
DNA Damage Response and Immune Defense
Claudia Nastasi, Laura Mannarino, Maurizio D’Incalci
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 20, pp. 7504-7504
Open Access | Times Cited: 98
The Ubiquitin Ligase TRIP12 Limits PARP1 Trapping and Constrains PARP Inhibitor Efficiency
Marco Gatti, Ralph Imhof, Qingyao Huang, et al.
Cell Reports (2020) Vol. 32, Iss. 5, pp. 107985-107985
Open Access | Times Cited: 94
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
Regulation of liquid–liquid phase separation with focus on post-translational modifications
Yun-Yi Luo, Jun Wu, Yanmei Li
Chemical Communications (2021) Vol. 57, Iss. 98, pp. 13275-13287
Closed Access | Times Cited: 85
Real-time monitoring of PARP1-dependent PARylation by ATR-FTIR spectroscopy
Annika Krüger, Alexander Bürkle, Karin Hauser, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 79
Poly(ADP-Ribose)Polymerase (PARP) Inhibitors and Radiation Therapy
Stephen A. Jannetti, Brian M. Zeglis, Michael R. Zalutsky, et al.
Frontiers in Pharmacology (2020) Vol. 11
Open Access | Times Cited: 76
Autonomous molecule generation using reinforcement learning and docking to develop potential novel inhibitors
Woosung Jeon, Dongsup Kim
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 72
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
SREBP1c-PARP1 axis tunes anti-senescence activity of adipocytes and ameliorates metabolic imbalance in obesity
Gung Lee, Ye Young Kim, Hagoon Jang, et al.
Cell Metabolism (2022) Vol. 34, Iss. 5, pp. 702-718.e5
Open Access | Times Cited: 64
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
Micropeptide PACMP inhibition elicits synthetic lethal effects by decreasing CtIP and poly(ADP-ribosyl)ation
Chuanchao Zhang, Bo Zhou, Feng Gu, et al.
Molecular Cell (2022) Vol. 82, Iss. 7, pp. 1297-1312.e8
Open Access | Times Cited: 62
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
Deubiquitinating enzymes and the proteasome regulate preferential sets of ubiquitin substrates
Fredrik Trulsson, Vyacheslav Akimov, Mihaela Robu, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 52
Structure, biochemical function, and signaling mechanism of plant NLRs
Jizong Wang, Wen Song, Jijie Chai
Molecular Plant (2022) Vol. 16, Iss. 1, pp. 75-95
Open Access | Times Cited: 51
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