Cargando…
Characterization of the Interaction of Full-Length HIV-1 Vif Protein with its Key Regulator CBFβ and CRL5 E3 Ubiquitin Ligase Components
Human immunodeficiency virus-1 (HIV-1) viral infectivity factor (Vif) is essential for viral replication because of its ability to eliminate the host's antiviral response to HIV-1 that is mediated by the APOBEC3 family of cellular cytidine deaminases. Vif targets these proteins, including APOBE...
Autores principales: | Zhou, Xiaohong, Evans, Sean L., Han, Xue, Liu, Yayan, Yu, Xiao-Fang |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3316577/ https://www.ncbi.nlm.nih.gov/pubmed/22479405 http://dx.doi.org/10.1371/journal.pone.0033495 |
Ejemplares similares
-
Requirement of HIV-1 Vif C-terminus for Vif-CBF-β interaction and assembly of CUL5-containing E3 ligase
por: Wang, Hong, et al.
Publicado: (2014) -
CRL Ubiquitin Ligases and DNA Damage Response
por: Li, Ju-Mei, et al.
Publicado: (2012) -
Interactions between HIV-1 Vif and human ElonginB-ElonginC are important for CBF-β binding to Vif
por: Wang, Xiaodan, et al.
Publicado: (2013) -
Identification of a tripartite interaction between the N-terminus of HIV-1 Vif and CBFβ that is critical for Vif function
por: Desimmie, Belete A., et al.
Publicado: (2017) -
Pathogenic Role of the CRL4 Ubiquitin Ligase in Human Disease
por: Lee, Jennifer, et al.
Publicado: (2012)