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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:

Viral Macro Domains Reverse Protein ADP-Ribosylation
Changqing Li, Yannick Debing, Gytis Jankevicius, et al.
Journal of Virology (2016) Vol. 90, Iss. 19, pp. 8478-8486
Open Access | Times Cited: 158

Showing 1-25 of 158 citing articles:

Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
Jian Lei, Yuri Kusov, Rolf Hilgenfeld
Antiviral Research (2017) Vol. 149, pp. 58-74
Open Access | Times Cited: 724
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
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
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
Coronaviruses: An Updated Overview of Their Replication and Pathogenesis
Yuhang Wang, Matthew Grunewald, Stanley Perlman
Methods in molecular biology (2020), pp. 1-29
Open Access | Times Cited: 187
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
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 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
Alphavirus polymerase and RNA replication
Maija K. Pietilä, Kirsi Hellström, Tero Ahola
Virus Research (2017) Vol. 234, pp. 44-57
Closed Access | Times Cited: 131
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
PARPs and ADP-ribosylation in RNA biology: from RNA expression and processing to protein translation and proteostasis
Dae-Seok Kim, Sridevi Challa, Aarin Jones, et al.
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 302-320
Open Access | Times Cited: 122
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
ADP-ribosyl–binding and hydrolase activities of the alphavirus nsP3 macrodomain are critical for initiation of virus replication
Rachy Abraham, Debra Hauer, Robert Lyle McPherson, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 44
Open Access | Times Cited: 119
Viral Macrodomains: Unique Mediators of Viral Replication and Pathogenesis
Anthony R. Fehr, Gytis Jankevicius, Ivan Ahel, et al.
Trends in Microbiology (2017) Vol. 26, Iss. 7, pp. 598-610
Open Access | Times Cited: 114
Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3
David N. Frick, Rajdeep S. Virdi, Nemanja Vuksanovic, et al.
Biochemistry (2020) Vol. 59, Iss. 28, pp. 2608-2615
Open Access | Times Cited: 113
The Viral Macrodomain Counters Host Antiviral ADP-Ribosylation
Yousef M. Alhammad, Anthony R. Fehr
Viruses (2020) Vol. 12, Iss. 4, pp. 384-384
Open Access | Times Cited: 99
Role of Host-Mediated Post-Translational Modifications (PTMs) in RNA Virus Pathogenesis
Ramesh Kumar, Divya Mehta, Nimisha Mishra, et al.
International Journal of Molecular Sciences (2020) Vol. 22, Iss. 1, pp. 323-323
Open Access | Times Cited: 96
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
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