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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:

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

Showing 1-25 of 56 citing articles:

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
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
Poly(ADP-ribose) drives condensation of FUS via a transient interaction
Kevin Rhine, Morgan Dasovich, Joseph Yoniles, et al.
Molecular Cell (2022) Vol. 82, Iss. 5, pp. 969-985.e11
Open Access | Times Cited: 61
SARS-CoV-2 Mac1 is required for IFN antagonism and efficient virus replication in cell culture and in mice
Yousef M. Alhammad, Srivatsan Parthasarathy, Roshan Ghimire, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 35
Open Access | Times Cited: 39
PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools
Morgan Dasovich, Anthony K. L. Leung
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1552-1572
Open Access | Times Cited: 34
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
Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors
Chris A. Brosey, Jerry H. Houl, Panagiotis Katsonis, et al.
Progress in Biophysics and Molecular Biology (2021) Vol. 163, pp. 171-186
Open Access | Times Cited: 54
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
Discovery of compounds that inhibit SARS-CoV-2 Mac1-ADP-ribose binding by high-throughput screening
Anu Roy, Yousef M. Alhammad, Peter R. McDonald, et al.
Antiviral Research (2022) Vol. 203, pp. 105344-105344
Open Access | Times Cited: 30
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
Unique Mutations in the Murine Hepatitis Virus Macrodomain Differentially Attenuate Virus Replication, Indicating Multiple Roles for the Macrodomain in Coronavirus Replication
Lynden S. Voth, Joseph J. O’Connor, Catherine M. Kerr, et al.
Journal of Virology (2021) Vol. 95, Iss. 15
Open Access | Times Cited: 37
Regulation of Biomolecular Condensates by Poly(ADP-ribose)
Kevin Rhine, Hana M. Odeh, James Shorter, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 9065-9093
Closed Access | Times Cited: 16
Switch-like compaction of poly(ADP-ribose) upon cation binding
Mohsen Badiee, Adam Kenet, Laura R. Ganser, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 19
Open Access | Times Cited: 13
Design, synthesis and evaluation of inhibitors of the SARS-CoV-2 nsp3 macrodomain
Lavinia M. Sherrill, Elva E. Joya, AnnMarie Walker, et al.
Bioorganic & Medicinal Chemistry (2022) Vol. 67, pp. 116788-116788
Open Access | Times Cited: 20
The life cycle of the alphaviruses: From an antiviral perspective
Andrew M. Skidmore, Steven B. Bradfute
Antiviral Research (2022) Vol. 209, pp. 105476-105476
Open Access | Times Cited: 19
IFN-γ signaling is required for the efficient replication of murine hepatitis virus (MHV) strain JHM in the brains of infected mice.
Catherine M. Kerr, Macie A. Proctor-Roser, Srivatsan Parthasarathy, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Zinc-finger PARP proteins ADP-ribosylate alphaviral proteins and are required for interferon-γ–mediated antiviral immunity
Andrew P. Ryan, Sofia E. Delgado-Rodriguez, Matthew D. Daugherty
Science Advances (2025) Vol. 11, Iss. 5
Open Access
NAD+-consuming enzymes in immune defense against viral infection
Jialin Shang, Michael R. Smith, Ananya Anmangandla, et al.
Biochemical Journal (2021) Vol. 478, Iss. 23, pp. 4071-4092
Open Access | Times Cited: 27
Intracellular mono-ADP-ribosyltransferases at the host–virus interphase
Bernhard Lüscher, Maud Verheirstraeten, Sarah Krieg, et al.
Cellular and Molecular Life Sciences (2022) Vol. 79, Iss. 6
Open Access | Times Cited: 18
Crystal structures and functional analysis of the ZnF5-WWE1-WWE2 region of PARP13/ZAP define a distinctive mode of engaging poly(ADP-ribose)
Jijin R. A. Kuttiyatveetil, Heddy Soufari, Morgan Dasovich, et al.
Cell Reports (2022) Vol. 41, Iss. 4, pp. 111529-111529
Open Access | Times Cited: 17
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
Recombinant infectious bronchitis virus containing mutations in non-structural proteins 10, 14, 15, and 16 and within the macrodomain provides complete protection against homologous challenge
Sarah Keep, Katalin Földes, Giulia Dowgier, et al.
Journal of Virology (2025)
Open Access
1H, 13C and 15N chemical shift assignments of Rubella virus macro domain in the free and in the ADPr bound state
Danai Moschidi, Nikolaos K. Fourkiotis, Christos Sideras-Bisdekis, et al.
Biomolecular NMR Assignments (2025)
Open Access
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