Cargando…
NMPylation and de-NMPylation of SARS-CoV-2 nsp9 by the NiRAN domain
The catalytic subunit of SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) contains two active sites that catalyze nucleotidyl-monophosphate transfer (NMPylation). Mechanistic studies and drug discovery have focused on RNA synthesis by the highly conserved RdRp. The second active site, which resides in...
Autores principales: | Wang, Bing, Svetlov, Dmitri, Artsimovitch, Irina |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8385902/ https://www.ncbi.nlm.nih.gov/pubmed/34352100 http://dx.doi.org/10.1093/nar/gkab677 |
Ejemplares similares
-
Conserved Characteristics of NMPylation Activities of Alpha- and Betacoronavirus NiRAN Domains
por: Slanina, Heiko, et al.
Publicado: (2023) -
Coronavirus replication–transcription complex: Vital and selective NMPylation of a conserved site in nsp9 by the NiRAN-RdRp subunit
por: Slanina, Heiko, et al.
Publicado: (2021) -
Allosteric control of the RNA polymerase by the elongation factor RfaH
por: Svetlov, Vladimir, et al.
Publicado: (2007) -
The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA polymerase capable of both de novo initiation and primer extension
por: te Velthuis, Aartjan J.W., et al.
Publicado: (2012) -
Structural and functional insights into the enzymatic plasticity of the SARS-CoV-2 NiRAN Domain
por: Small, Gabriel I., et al.
Publicado: (2023)