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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:

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

Showing 19 citing articles:

SARS-CoV-2 and innate immunity: the good, the bad, and the “goldilocks”
Benjamín L. Sievers, Mark T. K. Cheng, Kata Csiba, et al.
Cellular and Molecular Immunology (2023) Vol. 21, Iss. 2, pp. 171-183
Open Access | Times Cited: 51
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
PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation
Archimede Torretta, Constantinos Chatzicharalampous, Carmen Ebenwaldner, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 9, pp. 105096-105096
Open Access | Times Cited: 24
PARP14 is regulated by the PARP9/DTX3L complex and promotes interferon γ-induced ADP-ribosylation
Victória Chaves Ribeiro, Lilian C. Russo, Nícolas C. Hoch
The EMBO Journal (2024) Vol. 43, Iss. 14, pp. 2908-2928
Open Access | Times Cited: 9
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
Discovery and Development Strategies for SARS-CoV-2 NSP3 Macrodomain Inhibitors
M. Schuller, Tryfon Zarganes‐Tzitzikas, James M. Bennett, et al.
Pathogens (2023) Vol. 12, Iss. 2, pp. 324-324
Open Access | Times Cited: 14
Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets
Filip Mihalič, Caroline Benz, Eszter Kassa, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 13
A new hybrid post-translational modification—have you lost your (MARUb)les?
Isaac de Araújo Matos, Nícolas C. Hoch
The EMBO Journal (2025)
Open Access
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
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
PARPs and ADP-Ribosylation in Chronic Inflammation: A Focus on Macrophages
Diego Vinicius Santinelli Pestana, Elena Aïkawa, Sasha A. Singh, et al.
Pathogens (2023) Vol. 12, Iss. 7, pp. 964-964
Open Access | Times Cited: 8
Identification of Poly(ADP-ribose) Polymerase 9 (PARP9) as a Potent Suppressor for Mycobacterium tuberculosis Infection
Zhenyu Zhu, Shufeng Weng, Fen Zheng, et al.
Phenomics (2023) Vol. 4, Iss. 2, pp. 158-170
Closed Access | Times Cited: 5
COVID-19: Are We Facing Secondary Pellagra Which Cannot Simply Be Cured by Vitamin B3?
Renata Novak Kujundžić
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 8, pp. 4309-4309
Open Access | Times Cited: 8
PARP14 is a writer, reader and eraser of mono-ADP-ribosylation
Archimede Torretta, Constantinos Chatzicharalampous, Carmen Ebenwaldner, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
Macro1 domain residue F156: A hallmark of SARS-CoV-2 de-MARylation specificity
Oney Ortega Granda, Karine Alvarez, Maria J. Mate-Perez, et al.
Virology (2023) Vol. 587, pp. 109845-109845
Open Access | Times Cited: 2
Targeting SARS-CoV-2 Macrodomain-1 to Restore the Innate Immune Response Using In Silico Screening of Medicinal Compounds and Free Energy Calculation Approaches
Anwar Mohammad, Eman Alshawaf, Hossein Arefanian, et al.
Viruses (2023) Vol. 15, Iss. 9, pp. 1907-1907
Open Access | Times Cited: 2
Computational Investigations of Traditional Chinese Medicinal Compounds against the Omicron Variant of SARS-CoV-2 to Rescue the Host Immune System
Ziad Tareq Naman, Salim Kadhim, Zahraa J. K. Al-Isawi, et al.
Pharmaceuticals (2022) Vol. 15, Iss. 6, pp. 741-741
Open Access | Times Cited: 3
The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and X-ray diffraction at room temperature
G.J. Correy, Daniel W. Kneller, G.N. Phillips, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 2
Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets
Filip Mihalič, Caroline Benz, Eszter Kassa, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
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