Cargando…
Analysis of proteolytic processing sites in potyvirus polyproteins revealed differential amino acid preferences of NIa-Pro protease in each of seven cleavage sites
Potyviruses encode a large polyprotein that undergoes proteolytic processing, producing 10 mature proteins: P1, HC-Pro, P3, 6K1, CI, 6K2, VPg, NIa-Pro, NIb-RdRp, and CP. While P1/HC-Pro and HC-Pro/P3 junctions are cleaved by P1 and HC-Pro, respectively, the remaining seven are processed by NIa-Pro....
Autores principales: | Goh, Chul Jun, Hahn, Yoonsoo |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7833154/ https://www.ncbi.nlm.nih.gov/pubmed/33493199 http://dx.doi.org/10.1371/journal.pone.0245853 |
Ejemplares similares
-
Proteolytic Processing of Plant Proteins by Potyvirus NIa Proteases
por: Xiao, Huogen, et al.
Publicado: (2022) -
Identification of Cleavage Sites Proteolytically Processed by NS2B-NS3 Protease in Polyprotein of Japanese Encephalitis Virus
por: Wahaab, Abdul, et al.
Publicado: (2021) -
Identification of the protease cleavage sites in a reconstituted Gag polyprotein of an HERV-K(HML-2) element
por: George, Maja, et al.
Publicado: (2011) -
Analysis of the Proteolytic Processing of ABCA3: Identification of Cleavage Site and Involved Proteases
por: Hofmann, Nicole, et al.
Publicado: (2016) -
Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex
por: Li, Shanshan, et al.
Publicado: (2021)