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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 26-50 of 54 citing articles:

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
An Update on the Current State of SARS-CoV-2 Mac1 Inhibitors
Joseph J. O’Connor, Dana Ferraris, Anthony R. Fehr
Pathogens (2023) Vol. 12, Iss. 10, pp. 1221-1221
Open Access | Times Cited: 7
Targeting ADP-ribosylation as an antimicrobial strategy
Giuliana Catara, Annunziata Corteggio, Carmen Valente, et al.
Biochemical Pharmacology (2019) Vol. 167, pp. 13-26
Open Access | Times Cited: 21
The DarT/DarG Toxin–Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies
Giuliana Catara, Rocco Caggiano, Luca Palazzo
Pathogens (2023) Vol. 12, Iss. 2, pp. 240-240
Open Access | Times Cited: 6
Binding Adaptation of GS-441524 Diversifies Macro Domains and Downregulates SARS-CoV-2 de-MARylation Capacity
Aikaterini C. Tsika, Angelo Gallo, Nikolaos K. Fourkiotis, et al.
Journal of Molecular Biology (2022) Vol. 434, Iss. 16, pp. 167720-167720
Open Access | Times Cited: 9
Mutations in Hypervariable Domain of Venezuelan Equine Encephalitis Virus nsP3 Protein Differentially Affect Viral Replication
Chetan D. Meshram, Aaron T. Phillips, Tetyana Lukash, et al.
Journal of Virology (2019) Vol. 94, Iss. 3
Open 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
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
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
Poly‐ADP‐ribosylation dynamics, signaling, and analysis
Rasha Q. Al‐Rahahleh, Robert W. Sobol
Environmental and Molecular Mutagenesis (2024)
Closed Access | Times Cited: 1
Snapshots of ADP-ribose bound to Getah virus macro domain reveal an intriguing choreography
Ana Sofia Ferreira Ramos, G. Sulzenbacher, Bruno Canard, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 10
The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent ADP-ribosylation induced by interferon signalling
Lillian Cristina Russo, Rebeka Tomasin, Isaac de Araújo Matos, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 9
A molecular toolbox for ADP-ribosyl binding proteins
Sven T. Sowa, Albert Galera‐Prat, Sarah Wazir, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 6
Metabolic Activation of PARP as a SARS-CoV-2 Therapeutic Target—Is It a Bait for the Virus or the Best Deal We Could Ever Make with the Virus? Is AMBICA the Potential Cure?
Prasanth Puthanveetil
Biomolecules (2023) Vol. 13, Iss. 2, pp. 374-374
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
An uncharacterized FMAG_01619 protein from Fusobacterium mortiferum ATCC 9817 demonstrates that some bacterial macrodomains can also act as poly-ADP-ribosylhydrolases
Antonio Ginés García-Saura, Rubén Zapata‐Pérez, José Francisco Hidalgo, et al.
Scientific Reports (2019) Vol. 9, Iss. 1
Open Access | Times Cited: 5
Alphavirus nsP3 ADP-ribosylhydrolase Activity Disrupts Stress Granule Formation
Aravinth Kumar Jayabalan, Diane E. Griffin, Anthony K. L. Leung
bioRxiv (Cold Spring Harbor Laboratory) (2019)
Open Access | Times Cited: 5
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
ADP-ribosylhydrolases: from DNA damage repair to COVID-19
Lily Yu, Xiuhua Liu, Xiaochun Yu
Journal of Zhejiang University SCIENCE B (2021) Vol. 22, Iss. 1, pp. 21-30
Open Access | Times Cited: 4
Elucidating the tunability of binding behavior for the MERS-CoV macro domain with NAD metabolites
Meng-Hsuan Lin, Chao‐Cheng Cho, Yi‐Chih Chiu, et al.
Communications Biology (2021) Vol. 4, Iss. 1
Open Access | Times Cited: 4
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
Global remodeling of ADP-ribosylation by PARP1 suppresses influenza A virus infection
Zhenyu Zhang, Isabel Uribe, Kaitlin A. Davis, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Identification of a series of pyrrolo-pyrimidine based SARS-CoV-2 Mac1 inhibitors that repress coronavirus replication
Jessica J. Pfannenstiel, Men Thi Hoai Duong, Daniel Cluff, et al.
(2024)
Open Access

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