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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:

NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains
Marie-France Langelier, Levani Zandarashvili, Pedro M. Aguiar, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 201

Showing 1-25 of 201 citing articles:

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
NAD+ metabolism, stemness, the immune response, and cancer
Lola E. Navas, Amancio Carnero
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 329
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
Structural basis for allosteric PARP-1 retention on DNA breaks
Levani Zandarashvili, Marie-France Langelier, Uday Kiran Velagapudi, et al.
Science (2020) Vol. 368, Iss. 6486
Open Access | Times Cited: 274
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
Multifaceted Role of PARP-1 in DNA Repair and Inflammation: Pathological and Therapeutic Implications in Cancer and Non-Cancer Diseases
Simonetta Pazzaglia, Claudio Pioli
Cells (2019) Vol. 9, Iss. 1, pp. 41-41
Open Access | Times Cited: 172
ATM, ATR and DNA-PKcs kinases—the lessons from the mouse models: inhibition ≠ deletion
Demis Menolfi, Shan Zha
Cell & Bioscience (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 165
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
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
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
Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications
Qian Zhong, Xina Xiao, Yijie Qiu, et al.
MedComm (2023) Vol. 4, Iss. 3
Open Access | Times Cited: 119
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: 75
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
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
PARP Inhibitors as a Therapeutic Agent for Homologous Recombination Deficiency in Breast Cancers
Man Yee Keung, Yanyuan Wu, Jaydutt V. Vadgama
Journal of Clinical Medicine (2019) Vol. 8, Iss. 4, pp. 435-435
Open Access | Times Cited: 136
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
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
Poly(ADP-ribose) polymerase enzymes and the maintenance of genome integrity
Travis Eisemann, John M. Pascal
Cellular and Molecular Life Sciences (2019) Vol. 77, Iss. 1, pp. 19-33
Open Access | Times Cited: 89
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
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
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
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) Glycohydrolase (PARG) vs. Poly(ADP-Ribose) Polymerase (PARP) – Function in Genome Maintenance and Relevance of Inhibitors for Anti-cancer Therapy
Daniel Harrision, Polly Gravells, Ruth Thompson, et al.
Frontiers in Molecular Biosciences (2020) Vol. 7
Open Access | Times Cited: 75
TASOR is a pseudo-PARP that directs HUSH complex assembly and epigenetic transposon control
Christopher H. Douse, Iva A. Tchasovnikarova, Richard T. Timms, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 74
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