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Function analysis of sequences in human APOBEC3G involved in Vif-mediated degradation
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The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA
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The APOBEC-2 crystal structure and functional implications for the deaminase AID
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Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits
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Twin gradients in APOBEC3 edited HIV-1 DNA reflect the dynamics of lentiviral replication
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Monomeric APOBEC3G is catalytically active and has antiviral activity
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APOBEC3G DNA deaminase acts processively 3′ → 5′ on single-stranded DNA
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APOBEC3G is a single-stranded DNA cytidine deaminase and functions independently of HIV reverse transcriptase
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A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
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Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
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JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
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The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
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HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
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