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 26-50 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.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 25

Crystal structure and biochemical activity of the macrodomain from rubella virus p150
Guido A. Stoll, Nikos Nikolopoulos, Haoming Zhai, et al.
Journal of Virology (2024) Vol. 98, Iss. 2
Open Access | Times Cited: 3

Host ADP-ribosylation and the SARS-CoV-2 macrodomain
Nícolas C. Hoch
Biochemical Society Transactions (2021) Vol. 49, Iss. 4, pp. 1711-1721
Open Access | Times Cited: 19

Vitamin D modulates the expression of Toll-like receptors and pro-inflammatory cytokines without affecting Chikungunya virus replication, in monocytes and macrophages
Juan Felipe Valdés‐López, Paula A. Velilla, Silvio Urcuqui‐Inchima
Acta Tropica (2022) Vol. 232, pp. 106497-106497
Open Access | Times Cited: 14

Discovery of potent SARS-CoV-2 nsp3 macrodomain inhibitors uncovers lack of translation to cellular antiviral response
Alpha A. Lee, Isabelle Amick, Jasmin C. Aschenbrenner, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2

The search for inhibitors of macrodomains for targeting the readers and erasers of mono-ADP-ribosylation
Wei Fu, Huiqiao Yao, Mareike Bütepage, et al.
Drug Discovery Today (2021) Vol. 26, Iss. 11, pp. 2547-2558
Closed Access | Times Cited: 15

ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4
Robert G. Hammond, Norbert Schormann, Robert Lyle McPherson, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 2
Open Access | Times Cited: 11

Host Factor Nucleophosmin 1 (NPM1/B23) Exerts Antiviral Effects against Chikungunya Virus by Its Interaction with Viral Nonstructural Protein 3
Parvanendhu Pradeep, Sivakumar Krishnankutty Chandrika, Easwaran Sreekumar
Microbiology Spectrum (2023) Vol. 11, Iss. 4
Open Access | Times Cited: 4

Sindbis Macrodomain Poly-ADP-Ribose Hydrolase Activity Is Important for Viral RNA Synthesis
Eduardo G. Aguilar, Gabrielle Paniccia, Carolina Adura, et al.
Journal of Virology (2022) Vol. 96, Iss. 7
Open Access | Times Cited: 7

Alphavirus Virulence Determinants
Margarita V. Rangel, Kenneth A. Stapleford
Pathogens (2021) Vol. 10, Iss. 8, pp. 981-981
Open Access | Times Cited: 9

TMEΜ45B Interacts with Sindbis Virus Nsp1 and Nsp4 and Inhibits Viral Replication
Feixiang Yan, Wei Yang, Xinlu Wang, et al.
Journal of Virology (2022) Vol. 96, Iss. 17
Open Access | Times Cited: 5

G3BP/Rin-Binding Motifs Inserted into Flexible Regions of nsP2 Support RNA Replication of Chikungunya Virus
Sainan Wang, Andres Merits
Journal of Virology (2022) Vol. 96, Iss. 21
Open Access | Times Cited: 5

Semliki Forest Virus Chimeras with Functional Replicase Modules from Related Alphaviruses Survive by Adaptive Mutations in Functionally Important Hot Spots
Mona Teppor, Eva Žusinaite, Liis Karo-Astover, et al.
Journal of Virology (2021) Vol. 95, Iss. 20
Open Access | Times Cited: 7

In silico -based screening of natural products as potential inhibitors of SARS-CoV-2 macrodomain 1
Song Xie, Shoujing Cao, Juhong Wu, et al.
Journal of Biomolecular Structure and Dynamics (2023) Vol. 42, Iss. 10, pp. 5229-5237
Closed Access | Times Cited: 2

Cell-Type-Dependent Role for nsP3 Macrodomain ADP-Ribose Binding and Hydrolase Activity during Chikungunya Virus Infection
Taewoo Kim, Rachy Abraham, Lisa Pieterse, et al.
Viruses (2022) Vol. 14, Iss. 12, pp. 2744-2744
Open Access | Times Cited: 4

Variable Macro X Domain of SARS-CoV-2 Retains the Ability to Bind ADP-ribose
David N. Frick, Rajdeep S. Virdi, Nemanja Vuksanovic, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 5

Molecular Basis for ADP-ribose Binding to the Macro-X Domain of SARS-CoV-2 Nsp3
David N. Frick, Rajdeep S. Virdi, Nemanja Vuksanovic, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 5

High-throughput Activity Assay for Screening Inhibitors of the SARS-CoV-2 Mac1 Macrodomain
Morgan Dasovich, Junlin Zhuo, Jack A. Goodman, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 5

U-CAN-seq: A Universal Competition Assay by Nanopore Sequencing
Jennifer Diaz, John D. Sears, Che-Kang Chang, et al.
Viruses (2024) Vol. 16, Iss. 4, pp. 636-636
Open Access

Identification of mosquito proteins that differentially interact with alphavirus nonstructural protein 3, a determinant of vector specificity
Nathaniel M. Byers, Paul Burns, Olga Stuchlik, et al.
PLoS neglected tropical diseases (2023) Vol. 17, Iss. 1, pp. e0011028-e0011028
Open Access | Times Cited: 1

Switch-like Compaction of Poly(ADP-ribose) Upon Cation Binding
Mohsen Badiee, Adam Kenet, Laura R. Ganser, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1

Emerging Concepts on the Role of ADP-Ribosylation
Palmiro Poltronieri
Challenges (2020) Vol. 11, Iss. 1, pp. 3-3
Open Access | Times Cited: 2

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