NMR assignments of the macro domain from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
Author:
Funder
National Taiwan University
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
http://link.springer.com/content/pdf/10.1007/s12104-020-09996-x.pdf
Reference14 articles.
1. Alhammad YMO, Fehr AR (2020) The viral macrodomain counters host antiviral ADP-ribosylation. Viruses 12:384. https://doi.org/10.3390/v12040384
2. Cho CC, Lin MH, Chuang CY, Hsu CH (2016) Macro domain from middle east respiratory syndrome coronavirus (MERS-CoV) is an efficient ADP-ribose binding module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES. J Biol Chem 291:4894–4902. https://doi.org/10.1074/jbc.M115.700542
3. Egloff MP et al (2006) Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains. J Virol 80:8493–8502. https://doi.org/10.1128/JVI.00713-06
4. Eriksson KK, Cervantes-Barragan L, Ludewig B, Thiel V (2008) Mouse hepatitis virus liver pathology is dependent on ADP-ribose-1″-phosphatase, a viral function conserved in the alpha-like supergroup. J Virol 82:12325–12334. https://doi.org/10.1128/JVI.02082-08
5. Fehr AR, Singh SA, Kerr CM, Mukai S, Higashi H, Aikawa M (2020) The impact of PARPs and ADP-ribosylation on inflammation and host-pathogen interactions. Genes Dev 34:341–359. https://doi.org/10.1101/gad.334425.119
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