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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:

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.
Science Advances (2022) Vol. 8, Iss. 21
Open Access | Times Cited: 36

Showing 1-25 of 36 citing articles:

Iterative computational design and crystallographic screening identifies potent inhibitors targeting the Nsp3 macrodomain of SARS-CoV-2
Stefan Gahbauer, G.J. Correy, M. Schuller, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 2
Open Access | Times Cited: 87
ADP-ribosylation from molecular mechanisms to therapeutic implications
Marcin J. Suskiewicz, Evgeniia Prokhorova, J.G.M. Rack, et al.
Cell (2023) Vol. 186, Iss. 21, pp. 4475-4495
Open Access | Times Cited: 64
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: 37
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: 22
A single inactivating amino acid change in the SARS-CoV-2 NSP3 Mac1 domain attenuates viral replication in vivo
Taha Y. Taha, Rahul K. Suryawanshi, Irene P. Chen, et al.
PLoS Pathogens (2023) Vol. 19, Iss. 8, pp. e1011614-e1011614
Open Access | Times Cited: 17
Exploring pyrazolines as potential inhibitors of NSP3-macrodomain of SARS-CoV-2: synthesis and in silico analysis
R. R. Joshi, Harsh Gaikwad, Bhavana Soge, et al.
Scientific Reports (2025) Vol. 15, Iss. 1
Open Access
The Mac1 ADP-ribosylhydrolase is a Therapeutic Target for SARS-CoV-2
Rahul K. Suryawanshi, Priyadarshini Jaishankar, G.J. Correy, et al.
(2025)
Open Access
The Mac1 ADP-ribosylhydrolase is a Therapeutic Target for SARS-CoV-2
Rahul K. Suryawanshi, Priyadarshini Jaishankar, G.J. Correy, et al.
(2025)
Open Access
Derivatives of MOPS: promising scaffolds for SARS coronaviruses Macro domain‐targeted inhibition
Oney Ortega Granda, Karine Alvarez, Benjamin Morin, et al.
FEBS Journal (2025)
Open Access
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: 13
Automated multiconformer model building for X-ray crystallography and cryo-EM
Stephanie A. Wankowicz, Ashraya Ravikumar, Shivani Sharma, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 12
The Mac1 ADP-ribosylhydrolase is a Therapeutic Target for SARS-CoV-2
Rahul K. Suryawanshi, Priyadarshini Jaishankar, G.J. Correy, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Extensive exploration of structure activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment merging and active learning
G.J. Correy, Moira Rachman, Takaya Togo, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Uncovering Protein Ensembles: Automated Multiconformer Model Building for X-ray Crystallography and Cryo-EM
Stephanie A. Wankowicz, Ashraya Ravikumar, Shivani Sharma, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 11
SARS-CoV-2 Mac1 is required for IFN antagonism and efficient virus replication in mice
Yousef M. Alhammad, Srivatsan Parthasarathy, Roshan Ghimire, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 9
Neutron diffraction from a microgravity-grown crystal reveals the active site hydrogens of the internal aldimine form of tryptophan synthase
Victoria N. Drago, Juliette M. Devos, Matthew P. Blakeley, et al.
Cell Reports Physical Science (2024) Vol. 5, Iss. 2, pp. 101827-101827
Open Access | Times Cited: 2
Automated multiconformer model building for X-ray crystallography and cryo-EM
Stephanie A. Wankowicz, Ashraya Ravikumar, Shivani Sharma, et al.
eLife (2024) Vol. 12
Open Access | Times Cited: 2
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: 7
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
A Fluorescence Polarization Assay for Macrodomains Facilitates the Identification of Potent Inhibitors of the SARS-CoV-2 Macrodomain
Ananya Anmangandla, Sadhan Jana, Kewen Peng, et al.
ACS Chemical Biology (2023) Vol. 18, Iss. 5, pp. 1200-1207
Open Access | Times Cited: 6
Structure-Based High-Throughput Virtual Screening and Molecular Dynamics Simulation for the Discovery of Novel SARS-CoV-2 NSP3 Mac1 Domain Inhibitors
Behnaz Yazdani, Hajar Sirous, Simone Brogi, et al.
Viruses (2023) Vol. 15, Iss. 12, pp. 2291-2291
Open Access | Times Cited: 6
Resolving conformational changes that mediate a two-step catalytic mechanism in a model enzyme
Jack B. Greisman, Kevin M. Dalton, Dennis E. Brookner, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 5
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: 1
GS-441524-Diphosphate-Ribose Derivatives as Nanomolar Binders and Fluorescence Polarization Tracers for SARS-CoV-2 and Other Viral Macrodomains
Kewen Peng, Shamar D. Wallace, Saket R. Bagde, et al.
ACS Chemical Biology (2024) Vol. 19, Iss. 5, pp. 1093-1105
Open Access | Times Cited: 1
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: 8
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