Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G
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DOI: 10.1038/s41467-017-00501-y
Abstract: APOBEC3G (A3G) is a human enzyme that inhibits human immunodeficiency virus type 1 (HIV-1) infectivity, in the absence of the viral infectivity factor Vif, through deoxycytidine deamination and a deamination-independent mechanism. A3G converts from a… read more here.
Keywords: apobec3g; dna; dimerization regulates; a3g ... See more keywords
Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA
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DOI: 10.1038/s41467-018-04872-8
Abstract: The human APOBEC3G protein is a cytidine deaminase that generates cytidine to deoxy-uridine mutations in single-stranded DNA (ssDNA), and capable of restricting replication of HIV-1 by generating mutations in viral genome. The mechanism by which… read more here.
Keywords: crystal structure; catalytic domain; apobec3g; ssdna ... See more keywords
APOBEC3G is increasingly expressed on the human uterine cervical intraepithelial neoplasia along with disease progression
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DOI: 10.1111/aji.12703
Abstract: APOBEC3G (A3G) is a cytidine deaminase that exhibits antiviral activity by introducing C‐to‐T hypermutation in viral DNA. We recently observed the distinct presence of C‐to‐T hypermutation of human papillomavirus DNA in uterine cervical intraepithelial neoplasia… read more here.
Keywords: apobec3g; intraepithelial neoplasia; uterine cervical; progression ... See more keywords
The cytidine deaminase APOBEC3G contributes to cancer mutagenesis and clonal evolution in bladder cancer.
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DOI: 10.1158/0008-5472.can-22-2912
Abstract: Mutagenic processes leave distinct signatures in cancer genomes. The mutational signatures attributed to APOBEC3 cytidine deaminases are pervasive in human cancers. However, data linking individual APOBEC3 proteins to cancer mutagenesis in vivo are limited. Here,… read more here.
Keywords: cytidine; cancer mutagenesis; apobec3g; bladder cancer ... See more keywords