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Schiffer, CeliaPerson Why?
First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3G.Academic Article Why?
Substrate sequence selectivity of APOBEC3A implicates intra-DNA interactions.Academic Article Why?
Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity.Academic Article Why?
RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.Academic Article Why?
Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexes.Academic Article Why?
Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA.Academic Article Why?
Structural analysis of the active site and DNA binding of human cytidine deaminase APOBEC3B.Academic Article Why?
Crystal structure of a soluble APOBEC3G variant suggests ssDNA to bind in a channel that extends between the two domains.Academic Article Why?
The ssDNA Mutator APOBEC3A Is Regulated by Cooperative Dimerization.Academic Article Why?
Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces.Academic Article Why?
Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity.Academic Article Why?
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G.Academic Article Why?
Inhibition of APOBEC3G activity impedes double-stranded DNA repair.Academic Article Why?
Mechanism for APOBEC3G catalytic exclusion of RNA and non-substrate DNA.Academic Article Why?
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