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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:

Comprehensive ADP‐ribosylome analysis identifies tyrosine as an ADP‐ribose acceptor site
Deena M. Leslie Pedrioli, Mario Leutert, Vera Bilan, et al.
EMBO Reports (2018) Vol. 19, Iss. 8
Open Access | Times Cited: 92

Showing 1-25 of 92 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
(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
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
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
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
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
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
Interplay of Histone Marks with Serine ADP-Ribosylation
Edward Bartlett, Juán José Bonfiglio, Evgeniia Prokhorova, et al.
Cell Reports (2018) Vol. 24, Iss. 13, pp. 3488-3502.e5
Open Access | Times Cited: 91
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
The role of ADP-ribose metabolism in metabolic regulation, adipose tissue differentiation, and metabolism
Magdolna Szántó, Péter Bai
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 321-340
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
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 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
PARP1 roles in DNA repair and DNA replication: The basi(c)s of PARP inhibitor efficacy and resistance
Petar-Bogomil Kanev, Aleksandar Atemin, Stoyno Stoynov, et al.
Seminars in Oncology (2023) Vol. 51, Iss. 1-2, pp. 2-18
Open Access | Times Cited: 25
Covalent PARylation of DNA base excision repair proteins regulates DNA demethylation
Simon D Schwarz, Jianming Xu, Kapila Gunasekera, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 14
The chemistry of the vitamin B3 metabolome
Mikhail V. Makarov, Samuel A.J. Trammell, Marie E. Migaud
Biochemical Society Transactions (2018) Vol. 47, Iss. 1, pp. 131-147
Open Access | Times Cited: 79
ELTA: Enzymatic Labeling of Terminal ADP-Ribose
Yoshinari Ando, Elad Elkayam, Robert Lyle McPherson, et al.
Molecular Cell (2019) Vol. 73, Iss. 4, pp. 845-856.e5
Open Access | Times Cited: 65
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
Progress and outlook in studying the substrate specificities of PARPs and related enzymes
Marcin J. Suskiewicz, Luca Palazzo, R. J. M. Hughes, et al.
FEBS Journal (2020) Vol. 288, Iss. 7, pp. 2131-2142
Open Access | Times Cited: 52
Why structure and chain length matter: on the biological significance underlying the structural heterogeneity of poly(ADP-ribose)
Julia M. Reber, Aswin Mangerich
Nucleic Acids Research (2021) Vol. 49, Iss. 15, pp. 8432-8448
Open Access | Times Cited: 45
A rare human centenarian variant of SIRT6 enhances genome stability and interaction with Lamin A
Matthew Simon, Jiping Yang, Jonathan Gigas, et al.
The EMBO Journal (2022) Vol. 41, Iss. 21
Open Access | Times Cited: 37
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
PAR recognition by PARP1 regulates DNA‐dependent activities and independently stimulates catalytic activity of PARP1
Waghela Deeksha, Suman Abhishek, Eerappa Rajakumara
FEBS Journal (2023) Vol. 290, Iss. 21, pp. 5098-5113
Open Access | Times Cited: 18
ADP-ribosylation: from molecular mechanisms to human disease
Nícolas C. Hoch, Luis Mariano Polo
Genetics and Molecular Biology (2019) Vol. 43, Iss. 1 suppl 1
Open Access | Times Cited: 54
NADP+ is an endogenous PARP inhibitor in DNA damage response and tumor suppression
Chunjing Bian, Chao Zhang, Tao Luo, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 53
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