Induction of APOBEC3G Ubiquitination and Degradation by an HIV-1 Vif-Cul5-SCF Complex

By Xianghui Yu, Yunkai Yu, Bindong Liu, K. Luo, Wei Kong, P. Mao, Xiaofeng Yu. Science, 2003

1,246 citations recorded by the source corpus.

Subfields: Immunology, Infectious Diseases, Virology

View Paper: https://www.semanticscholar.org/paper/855579a6733aa2487cb7231abf0ca5a965fd997f

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In Immunology

1. Reuben S. Harris

Citations in the corpus

• Retroviral restriction by APOBEC proteins (2004, background): “has now opened the door to molecular studies showing that HIV-1 Vif functions by triggering the polyubiquitylation and proteasomal degradation of human APOBEC3G before virion incorporatio”
• Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome (2004, background): “Vif binding to APOBEC3G induces its ubiquitination and degradation by a proteasomal pathwa”
• HIV-1 accessory proteins--ensuring viral survival in a hostile environment. (2008, background): “In the majority of wild-type viral infections, Vif effectively antagonizes the antiviral effects of A3G through the recruitment of a cullin-RING ubiquitin ligase and the induction of polyubiquitylation (of A3G and Vif itself) and degradation (Table 1; Figure 2) (Mehle et al., 2004; Yu et al., 2003).”