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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:

(ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition
J.G.M. Rack, A. Ariza, Bryon Drown, et al.
Cell chemical biology (2018) Vol. 25, Iss. 12, pp. 1533-1546.e12
Open Access | Times Cited: 63

Showing 1-25 of 63 citing articles:

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
(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
Ligand recognition and gating mechanism through three ligand-binding sites of human TRPM2 channel
Yihe Huang, Rebecca Roth, Wei Lü, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 97
Cellular stress leads to the formation of membraneless stress assemblies in eukaryotic cells
Wessel van Leeuwen, Cathérine Rabouille
Traffic (2019) Vol. 20, Iss. 9, pp. 623-638
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
An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation
Juán José Bonfiglio, Orsolya Leidecker, Helen Dauben, et al.
Cell (2020) Vol. 183, Iss. 4, pp. 1086-1102.e23
Open Access | Times Cited: 90
Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease
Evgeniia Prokhorova, Thomas Agnew, Anne R. Wondisford, et al.
Molecular Cell (2021) Vol. 81, Iss. 12, pp. 2640-2655.e8
Open Access | Times Cited: 82
Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential
J.G.M. Rack, Valentina Zorzini, Zihan Zhu, et al.
Open Biology (2020) Vol. 10, Iss. 11
Open Access | Times Cited: 77
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
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
PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation
Archimede Torretta, Constantinos Chatzicharalampous, Carmen Ebenwaldner, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 9, pp. 105096-105096
Open Access | Times Cited: 24
DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids
Kang Zhu, Marcin J. Suskiewicz, Chatrin Chatrin, et al.
Nucleic Acids Research (2023) Vol. 52, Iss. 2, pp. 801-815
Open Access | Times Cited: 24
The ambivalent role of water at the origins of life
Andrey do Nascimento Vieira, Karl Kleinermanns, William Martin, et al.
FEBS Letters (2020) Vol. 594, Iss. 17, pp. 2717-2733
Open Access | Times Cited: 55
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
ADP-ribosylation systems in bacteria and viruses
Petra Mikolčević, Andrea Hloušek-Kasun, Ivan Ahel, et al.
Computational and Structural Biotechnology Journal (2021) Vol. 19, pp. 2366-2383
Open Access | Times Cited: 48
Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal
J.G.M. Rack, Qiang Liu, Valentina Zorzini, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 48
ADP-ribosylation of RNA in mammalian cells is mediated by TRPT1 and multiple PARPs
Lisa Weixler, Karla L. H. Feijs, Roko Žaja
Nucleic Acids Research (2022) Vol. 50, Iss. 16, pp. 9426-9441
Open Access | Times Cited: 37
Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain
Zhengrui Zhang, Jiaqi Fu, J.G.M. Rack, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
A molecular toolbox for ADP-ribosyl binding proteins
Sven T. Sowa, Albert Galera‐Prat, Sarah Wazir, et al.
Cell Reports Methods (2021) Vol. 1, Iss. 8, pp. 100121-100121
Open Access | Times Cited: 33
Beyond protein modification: the rise of non-canonical ADP-ribosylation
M. Schuller, Ivan Ahel
Biochemical Journal (2022) Vol. 479, Iss. 4, pp. 463-477
Open Access | Times Cited: 27
Mechanisms of promiscuity among drug metabolizing enzymes and drug transporters
William M. Atkins
FEBS Journal (2019) Vol. 287, Iss. 7, pp. 1306-1322
Open Access | Times Cited: 36
Discovery of reversing enzymes for RNA ADP-ribosylation reveals a possible defence module against toxic attack
Yang Lu, M. Schuller, Nathan P. Bullen, et al.
Nucleic Acids Research (2025) Vol. 53, Iss. 4
Open Access
Kinetic Mechanism of the Emergent Anticancer Target, Human ADP-ribosyltransferase 1
D. Groom, Amanda Lopacinski, S. Garforth, et al.
Biochemistry (2025)
Closed Access
Overview of the mammalian ADP-ribosyl-transferases clostridia toxin-like (ARTCs) family
Maria Di Girolamo, Gaia Fabrizio
Biochemical Pharmacology (2019) Vol. 167, pp. 86-96
Closed Access | Times Cited: 32
The function and regulation of ADP-ribosylation in the DNA damage response
Lena Duma, Ivan Ahel
Biochemical Society Transactions (2023) Vol. 51, Iss. 3, pp. 995-1008
Open Access | Times Cited: 8
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