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Article

The in vitro Biochemical Characterization of an HIV-1 Restriction Factor APOBEC3F: Importance of Loop 7 on Both CD1 and CD2 for DNA Binding and Deamination

9 Apr 2016

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 27063502
DOI: 10.1016/j.jmb.2016.03.031

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The in vitro Biochemical Characterization of an HIV-1 Restriction Factor APOBEC3F: Importance of Loop 7 on Both CD1 and CD2 for DNA Binding and DeaminationPMID 27063502Read ↗

Structural determinants of HIV-1 Vif susceptibility and DNA binding in APOBEC3FSemantic proximity Read ↗

Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genomeSemantic proximity Read ↗

Role of the single deaminase domain APOBEC3A in virus restriction, retrotransposition, DNA damage and cancerSemantic proximity Read ↗

The Antiviral and Cancer Genomic DNA Deaminase APOBEC3H Is Regulated by a RNA-Mediated Dimerization MechanismSemantic proximity Read ↗

Multiple APOBEC3 Restriction Factors for HIV-1 and One Vif to Rule Them AllSemantic proximity Read ↗

Loop 1 of APOBEC3C regulates its antiviral activity against HIV-1Semantic proximity Read ↗

Mapping Region of Human Restriction Factor APOBEC3H Critical for Interaction with HIV-1 VifSemantic proximity Read ↗

Interactions of host APOBEC3 restriction factors with HIV-1 in vivo: implications for therapeuticsSemantic proximity Read ↗

NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificitySemantic proximity Read ↗

APOBEC3F Properties and Hypermutation Preferences Indicate Activity against HIV-1 In VivoSemantic proximity Read ↗

Structural determinants of human APOBEC3A enzymatic and nucleic acid binding properties.Semantic proximity Read ↗

Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificitySemantic proximity Read ↗

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