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Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces.
First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3G.
Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity.
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G.
Inhibition of APOBEC3G activity impedes double-stranded DNA repair.
Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA.
Mechanism for APOBEC3G catalytic exclusion of RNA and non-substrate DNA.
Crystal Structure of a Soluble APOBEC3G Variant Suggests ssDNA to Bind in a Channel that Extends between the Two Domains.
HIV-1 VIF and human APOBEC3G interaction directly observed through molecular specific labeling using a new dual promotor vector.
APOBEC 3G Deaminase