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 26-50 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.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 6

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

Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains
A. Ariza, Qiang Liu, Nathan Cowieson, et al.
Journal of Biological Chemistry (2024), pp. 107770-107770
Open Access

Insights into mechanisms of ubiquitin ADP-ribosylation reversal
Zhengrui Zhang, Chittaranjan Das
Biochemical Society Transactions (2024)
Closed Access

A single inactivating amino acid change in the SARS-CoV-2 NSP3 Mac1 domain attenuates viral replication and pathogenesisin vivo
Taha Y. Taha, Rahul K. Suryawanshi, Irene P. Chen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1

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: 1

Uncovering Protein Ensembles: Automated Multiconformer Model Building for X-ray Crystallography and Cryo-EM
Stephanie A. Wankowicz, Ashraya Ravikumar, Shivani Sharma, et al.
(2023)
Open Access | Times Cited: 1

Realizing integration in structural biology: The 2022 ISBUC Annual Meeting
Birthe B. Kragelund, Claus J. Løland, Guillermo Montoya, et al.
Structure (2023) Vol. 31, Iss. 7, pp. 747-754
Closed Access

Crystal structure and biochemical activity of the macro domain from rubella virus p150
Guido A. Stoll, Liao Zhang, Yorgo Modis
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access

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