Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G
Sign Up to like & getrecommendations! Published in 2017 at "Nature Communications"
DOI: 10.1038/s41467-017-00501-y
Abstract: APOBEC3G (A3G) is a human enzyme that inhibits human immunodeficiency virus type 1 (HIV-1) infectivity, in the absence of the viral infectivity factor Vif, through deoxycytidine deamination and a deamination-independent mechanism. A3G converts from a… read more here.
Keywords: apobec3g; dna; dimerization regulates; a3g ... See more keywords
HIV-1 Vif Gained Breadth in APOBEC3G Specificity after Cross-Species Transmission of Its Precursors
Sign Up to like & getrecommendations! Published in 2021 at "Journal of Virology"
DOI: 10.1128/jvi.02071-21
Abstract: APOBEC3G (A3G) is an antiviral protein that potently restricts retroviruses like HIV. In turn, the HIV-1 protein Vif has evolved to antagonize A3G through degradation. ABSTRACT APOBEC3G (A3G) is a host-encoded cytidine deaminase that potently… read more here.
Keywords: cross species; a3g; species transmission; vif ... See more keywords
Structural Determinants of the APOBEC3G N-Terminal Domain for HIV-1 RNA Association
Sign Up to like & getrecommendations! Published in 2019 at "Frontiers in Cellular and Infection Microbiology"
DOI: 10.3389/fcimb.2019.00129
Abstract: APOBEC3G (A3G) is a cellular protein that inhibits HIV-1 infection through virion incorporation. The interaction of the A3G N-terminal domain (NTD) with RNA is essential for A3G incorporation in the HIV-1 virion. The interaction between… read more here.
Keywords: terminal domain; hiv; rna; a3g ... See more keywords