Cargando…
Characterization of SARS2 Nsp15 nuclease activity reveals it's mad about U
Nsp15 is a uridine specific endoribonuclease that coronaviruses employ to cleave viral RNA and evade host immune defense systems. Previous structures of Nsp15 from across Coronaviridae revealed that Nsp15 assembles into a homo-hexamer and has a conserved active site similar to RNase A. Beyond a pref...
Autores principales: | Frazier, Meredith N, Dillard, Lucas B, Krahn, Juno M, Perera, Lalith, Williams, Jason G, Wilson, Isha M, Stewart, Zachary D, Pillon, Monica C, Deterding, Leesa J, Borgnia, Mario J, Stanley, Robin E |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8385992/ https://www.ncbi.nlm.nih.gov/pubmed/34403466 http://dx.doi.org/10.1093/nar/gkab719 |
Ejemplares similares
-
Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics
por: Pillon, Monica C., et al.
Publicado: (2021) -
Cryo-EM Structures of the SARS-CoV-2 Endoribonuclease Nsp15
por: Pillon, Monica C., et al.
Publicado: (2020) -
Flipped Over U: Structural Basis for dsRNA Cleavage by the SARS-CoV-2 Endoribonuclease
por: Frazier, Meredith N., et al.
Publicado: (2022) -
Structural characterization of the virulence factor Sda1 nuclease from Streptococcus pyogenes
por: Moon, Andrea F., et al.
Publicado: (2016) -
Exploring cleavage activity of NSP15 using single molecule PIE-FRET
por: Gordon, Kenya, et al.
Publicado: (2023)