Cargando…
The HSV-1 ubiquitin ligase ICP0: Modifying the cellular proteome to promote infection
Herpes simplex virus 1 (HSV-1) hijacks ubiquitination machinery to modify the cellular proteome to create an environment permissive for virus replication. HSV-1 encodes its own RING-finger E3 ubiquitin (Ub) ligase, Infected Cell Protein 0 (ICP0), that directly interfaces with component proteins of t...
Autores principales: | Rodríguez, Milagros Collados, Dybas, Joseph M., Hughes, Joseph, Weitzman, Matthew D., Boutell, Chris |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Science
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7303953/ https://www.ncbi.nlm.nih.gov/pubmed/32416261 http://dx.doi.org/10.1016/j.virusres.2020.198015 |
Ejemplares similares
-
A quantitative assay to monitor HSV-1 ICP0 ubiquitin ligase activity in vitro
por: Boutell, Chris, et al.
Publicado: (2015) -
The Intrinsic Antiviral Defense to Incoming HSV-1 Genomes Includes Specific DNA Repair Proteins and Is Counteracted by the Viral Protein ICP0
por: Lilley, Caroline E., et al.
Publicado: (2011) -
HSV-1 ICP0: An E3 Ubiquitin Ligase That Counteracts Host Intrinsic and Innate Immunity
por: Lanfranca, Mirna Perusina, et al.
Publicado: (2014) -
A Novel Recognition by the E3 Ubiquitin Ligase of HSV-1 ICP0 Enhances the Degradation of PML Isoform I to Prevent ND10 Reformation in Late Infection
por: Jan Fada, Behdokht, et al.
Publicado: (2023) -
A 77 Amino Acid Region in the N-Terminal Half of the HSV-1 E3 Ubiquitin Ligase ICP0 Contributes to Counteracting an Established Type 1 Interferon Response
por: Perusina Lanfranca, Mirna, et al.
Publicado: (2022)