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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:

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: 204

Showing 1-25 of 204 citing articles:

PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Rebecca Gupte, Ziying Liu, W. Lee Kraus
Genes & Development (2017) Vol. 31, Iss. 2, pp. 101-126
Open Access | Times Cited: 618
Poly(ADP-ribose) polymerase inhibition: past, present and future
Nicola J. Curtin, Csaba Szabó
Nature Reviews Drug Discovery (2020) Vol. 19, Iss. 10, pp. 711-736
Closed Access | Times Cited: 403
Serine ADP-Ribosylation Depends on HPF1
Juán José Bonfiglio, Pietro Fontana, Qi Zhang, et al.
Molecular Cell (2017) Vol. 65, Iss. 5, pp. 932-940.e6
Open Access | Times Cited: 315
ADP‐ribosyltransferases, an update on function and nomenclature
Bernhard Lüscher, Ivan Ahel, Matthias Altmeyer, et al.
FEBS Journal (2021) Vol. 289, Iss. 23, pp. 7399-7410
Open Access | Times Cited: 238
The Conserved Coronavirus Macrodomain Promotes Virulence and Suppresses the Innate Immune Response during Severe Acute Respiratory Syndrome Coronavirus Infection
Anthony R. Fehr, Rudragouda Channappanavar, Gytis Jankevicius, et al.
mBio (2016) Vol. 7, Iss. 6
Open Access | Times Cited: 229
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: 224
Targeted and Persistent 8-Oxoguanine Base Damage at Telomeres Promotes Telomere Loss and Crisis
Elise Fouquerel, Ryan P. Barnes, Shikhar Uttam, et al.
Molecular Cell (2019) Vol. 75, Iss. 1, pp. 117-130.e6
Open Access | Times Cited: 219
Signaling Pathways in Cancer: Therapeutic Targets, Combinatorial Treatments, and New Developments
Hon Yan Kelvin Yip, Antonella Papa
Cells (2021) Vol. 10, Iss. 3, pp. 659-659
Open Access | Times Cited: 205
The coronavirus macrodomain is required to prevent PARP-mediated inhibition of virus replication and enhancement of IFN expression
Matthew Grunewald, Yating Chen, Chad V. Kuny, et al.
PLoS Pathogens (2019) Vol. 15, Iss. 5, pp. e1007756-e1007756
Open Access | Times Cited: 190
The impact of PARPs and ADP-ribosylation on inflammation and host–pathogen interactions
Anthony R. Fehr, Sasha A. Singh, Catherine M. Kerr, et al.
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 341-359
Open Access | Times Cited: 188
ADP-ribosylhydrolase activity of Chikungunya virus macrodomain is critical for virus replication and virulence
Robert Lyle McPherson, Rachy Abraham, Easwaran Sreekumar, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 7, pp. 1666-1671
Open Access | Times Cited: 176
New World and Old World Alphaviruses Have Evolved to Exploit Different Components of Stress Granules, FXR and G3BP Proteins, for Assembly of Viral Replication Complexes
Dal‐Young Kim, Joséphine M. Reynaud, Rasalouskaya Aliaksandra, et al.
PLoS Pathogens (2016) Vol. 12, Iss. 8, pp. e1005810-e1005810
Open Access | Times Cited: 170
Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking
M. Schuller, G.J. Correy, Stefan Gahbauer, et al.
Science Advances (2021) Vol. 7, Iss. 16
Open Access | Times Cited: 162
(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
The DarTG toxin-antitoxin system provides phage defence by ADP-ribosylating viral DNA
Michele LeRoux, Sriram Srikant, Gabriella I. C. Teodoro, et al.
Nature Microbiology (2022) Vol. 7, Iss. 7, pp. 1028-1040
Open Access | Times Cited: 131
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
The conserved macrodomains of the non-structural proteins of Chikungunya virus and other pathogenic positive strand RNA viruses function as mono-ADP-ribosylhydrolases
Laura Eckei, Sarah Krieg, Mareike Bütepage, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 134
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
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
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
Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes
K. Michalska, Youngchang Kim, R. Jedrzejczak, et al.
IUCrJ (2020) Vol. 7, Iss. 5, pp. 814-824
Open Access | Times Cited: 123
The SARS-CoV-2 Conserved Macrodomain Is a Mono-ADP-Ribosylhydrolase
Yousef M. Alhammad, M.M. Kashipathy, Anuradha Roy, et al.
Journal of Virology (2020) Vol. 95, Iss. 3
Open Access | Times Cited: 121
The Enigmatic Alphavirus Non-Structural Protein 3 (nsP3) Revealing Its Secrets at Last
Benjamin Götte, Lifeng Liu, Gerald M. McInerney
Viruses (2018) Vol. 10, Iss. 3, pp. 105-105
Open Access | Times Cited: 120
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