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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:

Macrodomain ADP-ribosylhydrolase and the pathogenesis of infectious diseases
Anthony K. L. Leung, Robert Lyle McPherson, Diane E. Griffin
PLoS Pathogens (2018) Vol. 14, Iss. 3, pp. e1006864-e1006864
Open Access | Times Cited: 54

Showing 1-25 of 54 citing articles:

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-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 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
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
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 SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent ADP-ribosylation induced by interferon signaling
Lilian C. Russo, Rebeka Tomasin, Isaac de Araújo Matos, et al.
Journal of Biological Chemistry (2021) Vol. 297, Iss. 3, pp. 101041-101041
Open Access | Times Cited: 97
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
Stress granule formation, disassembly, and composition are regulated by alphavirus ADP-ribosylhydrolase activity
Aravinth Kumar Jayabalan, Srivathsan Adivarahan, Aakash Koppula, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 6
Open Access | Times Cited: 73
Pro-Viral and Anti-Viral Roles of the RNA-Binding Protein G3BP1
Aravinth Kumar Jayabalan, Diane E. Griffin, Anthony K. L. Leung
Viruses (2023) Vol. 15, Iss. 2, pp. 449-449
Open Access | Times Cited: 24
Engineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins
Kathrin Nowak, Florian Rosenthal, T. Karlberg, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 67
Both ADP-Ribosyl-Binding and Hydrolase Activities of the Alphavirus nsP3 Macrodomain Affect Neurovirulence in Mice
Rachy Abraham, Robert Lyle McPherson, Morgan Dasovich, et al.
mBio (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 56
High-Throughput Activity Assay for Screening Inhibitors of the SARS-CoV-2 Mac1 Macrodomain
Morgan Dasovich, Junlin Zhuo, Jack A. Goodman, et al.
ACS Chemical Biology (2021) Vol. 17, Iss. 1, pp. 17-23
Open Access | Times Cited: 42
The Conserved Macrodomain Is a Potential Therapeutic Target for Coronaviruses and Alphaviruses
Anthony K. L. Leung, Diane E. Griffin, Jürgen Bosch, et al.
Pathogens (2022) Vol. 11, Iss. 1, pp. 94-94
Open Access | Times Cited: 32
Mutation of a highly conserved isoleucine residue in loop 2 of several 𝛽-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental to infection
Catherine M. Kerr, Jessica J. Pfannenstiel, Yousef M. Alhammad, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 6
ADPriboDB 2.0: an updated database of ADP-ribosylated proteins
Vinay Ayyappan, Ricky Wat, Calvin Barber, et al.
Nucleic Acids Research (2020) Vol. 49, Iss. D1, pp. D261-D265
Open Access | Times Cited: 42
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
ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological Perspectives
Giuseppe Manco, Giuseppina Lacerra, Elena Porzio, et al.
Biomolecules (2022) Vol. 12, Iss. 3, pp. 443-443
Open Access | Times Cited: 21
Analysis of Coronavirus Temperature-Sensitive Mutants Reveals an Interplay between the Macrodomain and Papain-Like Protease Impacting Replication and Pathogenesis
Xufang Deng, Robert C. Mettelman, Amornrat O’Brien, et al.
Journal of Virology (2019) Vol. 93, Iss. 12
Open Access | Times Cited: 34
A Bifunctional NAD+ for Profiling Poly-ADP-Ribosylation-Dependent Interacting Proteins
Albert T. Lam, Xiaonan Zhang, Valentine V. Courouble, et al.
ACS Chemical Biology (2021) Vol. 16, Iss. 2, pp. 389-396
Open Access | Times Cited: 24
Docking and Dynamics Studies: Identifying the Binding Ability of Quercetin Analogs to the ADP-Ribose Phosphatase of SARS CoV-2
Arfan Arfan
Jurnal Kartika Kimia (2023) Vol. 5, Iss. 2
Open Access | Times Cited: 10
Mutation of a highly conserved isoleucine residue in loop 2 of several β-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental for replication
Catherine M. Kerr, Jessica J. Pfannenstiel, Yousef M. Alhammad, et al.
Journal of Virology (2024) Vol. 98, Iss. 11
Closed Access | Times Cited: 3
The SARS-CoV-2 conserved macrodomain is a mono-ADP-ribosylhydrolase
Yousef M. Alhammad, M.M. Kashipathy, Anuradha Roy, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 25
High-Throughput Screening and Quantum Mechanics for Identifying Potent Inhibitors Against Mac1 Domain of SARS-CoV-2 Nsp3
Chandrabose Selvaraj, Dhurvas Chandrasekaran Dinesh, Umesh Panwar, et al.
IEEE/ACM Transactions on Computational Biology and Bioinformatics (2020) Vol. 18, Iss. 4, pp. 1262-1270
Open Access | Times Cited: 24
IFN-I-tolerant oncolytic Semliki Forest virus in combination with anti-PD1 enhances T cell response against mouse glioma
Miika Martikainen, Mohanraj Ramachandran, Roberta Lugano, et al.
Molecular Therapy — Oncolytics (2021) Vol. 21, pp. 37-46
Open Access | Times Cited: 21
Tankyrase-mediated ADP-ribosylation is a regulator of TNF-induced death
Lin Liu, Jarrod J. Sandow, Deena M. Leslie Pedrioli, et al.
Science Advances (2022) Vol. 8, Iss. 19
Open Access | Times Cited: 16
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