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Mutation of highly conserved residues in loop 2 of the coronavirus macrodomain demonstrates that enhanced ADP-ribose binding is detrimental to infection.
Kerr CM, Pfannenstiel JJ, Alhammad YM, Roy A, O'Connor JJ, Ghimire R, Khattabi R, Shrestha R, McDonald PR, Gao P, Johnson DK, More S, Channappanavar R, Fehr AR. Kerr CM, et al. Among authors: mcdonald pr. bioRxiv [Preprint]. 2024 Jan 4:2024.01.03.574082. doi: 10.1101/2024.01.03.574082. bioRxiv. 2024. PMID: 38260573 Free PMC article. Preprint.
The SARS-CoV-2 conserved macrodomain is a mono-ADP-ribosylhydrolase.
Alhammad YMO, Kashipathy MM, Roy A, Gagné JP, McDonald P, Gao P, Nonfoux L, Battaile KP, Johnson DK, Holmstrom ED, Poirier GG, Lovell S, Fehr AR. Alhammad YMO, et al. bioRxiv [Preprint]. 2020 Oct 28:2020.05.11.089375. doi: 10.1101/2020.05.11.089375. bioRxiv. 2020. PMID: 32511412 Free PMC article. Updated. Preprint.
The SARS-CoV-2 Conserved Macrodomain Is a Mono-ADP-Ribosylhydrolase.
Alhammad YMO, Kashipathy MM, Roy A, Gagné JP, McDonald P, Gao P, Nonfoux L, Battaile KP, Johnson DK, Holmstrom ED, Poirier GG, Lovell S, Fehr AR. Alhammad YMO, et al. J Virol. 2021 Jan 13;95(3):e01969-20. doi: 10.1128/JVI.01969-20. Print 2021 Jan 13. J Virol. 2021. PMID: 33158944 Free PMC article.
102 results