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The Interaction between HIV-1 Gag and APOBEC3G

https://doi.org/10.1074/jbc.m402062200
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53/53 checkable references clean · checked 2026-07-25

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

The 53 checked references that resolve
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The Human Immunodeficiency Virus Type 1 Vif Protein Reduces Intracellular Expression and Inhibits Packaging of APOBEC3G (CEM15), a Cellular Inhibitor of Virus Infectivity
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HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
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Human immunodeficiency virus type 1 Vif protein binds to the Pr55Gag precursor
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Vif and the p55 <sup>Gag</sup> Polyprotein of Human Immunodeficiency Virus Type 1 Are Present in Colocalizing Membrane-Free Cytoplasmic Complexes
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Dimeric structure of a human apolipoprotein B mRNA editing protein and cloning and chromosomal localization of its gene.
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Escherichia coli cytidine deaminase provides a molecular model for ApoB RNA editing and a mechanism for RNA substrate recognition 1 1Edited by A. R. Fersht
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The Enzymatic Activity of CEM15/Apobec-3G Is Essential for the Regulation of the Infectivity of HIV-1 Virion but Not a Sole Determinant of Its Antiviral Activity
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The Role of Pr55 <sup> <i>gag</i> </sup> in the Annealing of tRNA <sub>3</sub> <sup>Lys</sup> to Human Immunodeficiency Virus Type 1 Genomic RNA
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