Pr55(Gag)
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gag
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Single-virion fluorescence microscopy analysis demonstrates that the efficiency of A3G-YFP and A3F-YFP incorporation into HIV-1 Gag-CeFP virions is higher than that of A3C-YFP incorporation into HIV-1 Gag-CeFP virions |
PubMed
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gag
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Interaction of APOBEC3C with HIV-1 Gag is required for its incorporation into Vif(-) virions and the interaction between APOBEC3C and Gag is MA domain-dependent and 7SL RNA-dependent |
PubMed
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Vif
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vif
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HIV-1 Vif degrades APOBEC3C and APOBEC3F and is dependent on Vif F1, F2, and F3 box mutations involving residues D14, R15, M16, W79, D172, and W174 |
PubMed
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vif
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HIV-1 Vif degrades APOBEC3F and APOBEC3C |
PubMed
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vif
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HIV-1 Vif internal amino acid salt bridge (E171-K167-D101) mediates human APOBEC3C and APOBEC3F degradation |
PubMed
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vif
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APOBEC3C restricts HIV-1 replication by causing G to A mutations in viral DNA replication intermediates; HIV-1 Vif binds to and destabilizes APOBEC3C |
PubMed
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vif
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APOBEC3C levels in virus particles are increased when the virus particles are produced from N.41 treated 293T cells in the presence of Vif expression |
PubMed
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vif
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Immunoblotting and crystal structure analyses reveal ten amino acids L72, F75, C76, I79, L80, S81, Y86, E106, F107, and H111 between the alpha 2 and alpha 3 helices of APOBEC3C are involved in forming the Vif-interaction interface |
PubMed
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vif
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CBF-beta-mediated increase of HIV-1 Vif steady-state levels results in decreased cellular levels of all Vif-sensitive APOBEC proteins (A3C, A3D, A3F, A3G, and A3H haplotype II) |
PubMed
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vif
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A potent small molecular compound VEC-5 protects APOBEC3G, APOBEC3F, and APOBEC3C from HIV-1 Vif-induced degradation and enhances A3G incorporation into HIV-1 virions by inhibiting the interaction between Vif and elongin C |
PubMed
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vif
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Stress causes A3A, A3B, A3C, and A3F to co-localize efficiently with Vif(IIIB) and mRNA-PABP1 complexes in stress granules |
PubMed
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vif
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Vif(IIIB) induces A3A, A3B, and A3C emigration from the nucleus to the cytosol and thereby causes net increases in their cytosolic concentrations and anti-HIV-1 activities |
PubMed
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vif
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Small molecule RN-18 specifically inhibits HIV-1 Vif-mediated downregulation of APOBEC3C/F/G proteins by decreasing Vif protein levels when Vif interacts with these proteins |
PubMed
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vif
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A novel conserved 69YXXL72 motif in HIV-1 Vif regulates A3C expression in cells |
PubMed
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vif
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The LV portion of the Vif SLV/Ix4Yx9Y motif is required for optimal suppression of A3C or A3DE |
PubMed
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vif
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HIV-1 Vif K22E and RH41/42AA mutants are able to suppress the anti-viral activity of A3C, but are ineffective in suppressing the anti-viral activity of A3G. K22, R41, and H42 residues are important for Vif-mediated degradation of A3G, but not A3C |
PubMed
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vif
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Amino acid E289 in the EFLARH sequence of A3C is critical for HIV-1 Vif-mediated degradation |
PubMed
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Vpr
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vpr
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HIV-1 Vpr upregulates the gene expression of APOBEC3C in human monocyte-derived macrophages |
PubMed
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matrix
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gag
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Interaction of APOBEC3C with HIV-1 Gag is required for its incorporation into Vif(-) virions and the interaction between APOBEC3C and Gag is MA domain-dependent and 7SL RNA-dependent |
PubMed
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