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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:

Distribution of protein poly(ADP-ribosyl)ation systems across all domains of life
Dragutin Perina, Andreja Mikoč, Josip Ahel, et al.
DNA repair (2014) Vol. 23, pp. 4-16
Open Access | Times Cited: 169

Showing 1-25 of 169 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: 380
HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity
Ian Gibbs‐Seymour, Pietro Fontana, J.G.M. Rack, et al.
Molecular Cell (2016) Vol. 62, Iss. 3, pp. 432-442
Open Access | Times Cited: 270
Functions of PARylation in DNA Damage Repair Pathways
Huiting Wei, Xiaochun Yu
Genomics Proteomics & Bioinformatics (2016) Vol. 14, Iss. 3, pp. 131-139
Open Access | Times Cited: 262
Structures and Mechanisms of Enzymes Employed in the Synthesis and Degradation of PARP-Dependent Protein ADP-Ribosylation
Eva Barkauskaite, Gytis Jankevicius, Ivan Ahel
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 935-946
Open Access | Times Cited: 242
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: 223
PARP-1 involvement in neurodegeneration: A focus on Alzheimer’s and Parkinson’s diseases
Sara Martire, Luciana Mosca, Maria D’Erme
Mechanisms of Ageing and Development (2015) Vol. 146-148, pp. 53-64
Closed Access | Times Cited: 215
Macrodomains: Structure, Function, Evolution, and Catalytic Activities
J.G.M. Rack, Dragutin Perina, Ivan Ahel
Annual Review of Biochemistry (2016) Vol. 85, Iss. 1, pp. 431-454
Open Access | Times Cited: 203
(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: 156
Biological Properties of Vitamins of the B-Complex, Part 1: Vitamins B1, B2, B3, and B5
Marcel Hrubša, Tomáš Siatka, Iveta Nejmanová, et al.
Nutrients (2022) Vol. 14, Iss. 3, pp. 484-484
Open Access | Times Cited: 137
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: 68
PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation
Pulak Kar, Chatrin Chatrin, N Mimica Dukic, et al.
The EMBO Journal (2024) Vol. 43, Iss. 14, pp. 2929-2953
Open Access | Times Cited: 16
The Toxin-Antitoxin System DarTG Catalyzes Reversible ADP-Ribosylation of DNA
Gytis Jankevicius, A. Ariza, Marijan Ahel, et al.
Molecular Cell (2016) Vol. 64, Iss. 6, pp. 1109-1116
Open Access | Times Cited: 165
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
Reversible mono‐ADP‐ribosylation of DNA breaks
Deeksha Munnur, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 23, pp. 4002-4016
Open Access | Times Cited: 142
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: 139
Reversible ADP-ribosylation of RNA
Deeksha Munnur, Edward Bartlett, Petra Mikolčević, et al.
Nucleic Acids Research (2019) Vol. 47, Iss. 11, pp. 5658-5669
Open Access | Times Cited: 134
ADP‐ribosylation: new facets of an ancient modification
Luca Palazzo, Andreja Mikoč, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 18, pp. 2932-2946
Open Access | Times Cited: 129
Processing of protein ADP-ribosylation by Nudix hydrolases
Luca Palazzo, Benjamin Thomas, Ann‐Sofie Jemth, et al.
Biochemical Journal (2015) Vol. 468, Iss. 2, pp. 293-301
Open Access | Times Cited: 124
PARP Inhibitors as Therapeutics: Beyond Modulation of PARylation
Ahrum Min, Seock Ah Im
Cancers (2020) Vol. 12, Iss. 2, pp. 394-394
Open Access | Times Cited: 109
The PARP family: insights into functional aspects of poly (ADP‐ribose) polymerase‐1 in cell growth and survival
Tina Jubin, Ashlesha Kadam, Munira Jariwala, et al.
Cell Proliferation (2016) Vol. 49, Iss. 4, pp. 421-437
Open Access | Times Cited: 103
Niacin
James B. Kirkland, Mirella L. Meyer‐Ficca
Advances in food and nutrition research (2018), pp. 83-149
Closed Access | Times Cited: 95
The Similarities between Human Mitochondria and Bacteria in the Context of Structure, Genome, and Base Excision Repair System
Karolina Boguszewska, Michał Szewczuk, Julia Kaźmierczak-Barańska, et al.
Molecules (2020) Vol. 25, Iss. 12, pp. 2857-2857
Open Access | Times Cited: 93
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
Specificity of reversible ADP-ribosylation and regulation of cellular processes
Kerryanne Crawford, Juán José Bonfiglio, Andreja Mikoč, et al.
Critical Reviews in Biochemistry and Molecular Biology (2017) Vol. 53, Iss. 1, pp. 64-82
Closed Access | Times Cited: 91
ADP-ribosylation of DNA and RNA
Joséphine Groslambert, Evgeniia Prokhorova, Ivan Ahel
DNA repair (2021) Vol. 105, pp. 103144-103144
Open Access | Times Cited: 79
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