An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22.
By A. Jarmuz, A. Chester, J. Bayliss, Jane Gisbourne, I. Dunham, James Scott, N. Navaratnam. Genomics, 2002
733 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/138c6af7c6f5b20d6e71548471979b76ec43e3f0
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Citations in the corpus
- DNA deamination mediates innate immunity to retroviral infection. (2003, background): “Michael S. Neuberger,1 and Michael H. Malim2 CEM15/APOBEC3G is a member of the APOBEC family of proteins of which the RNA editing protein APO-1Medical Research Council Laboratory of Molecular Biology BEC1 is the founder (Teng et al., 1993; Jarmuz et al., 2002).”
- Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts (2003, background): “APOBEC3G is closely related to APOBEC1, the central component of an RNA-editing complex that deaminates a cytosine residue in apoB messenger RN”
- Adenosine deaminases acting on RNA (ADARs): RNA-editing enzymes (2004, unknown): “degree of gene-family expansion in the chordate lineage similar to that found in many other gene families, notably including the cytosine deaminases acting on RNA (CDARs) [14].”
- HIV-1 accessory proteins--ensuring viral survival in a hostile environment. (2008, background): “Given that many of the APOBEC3 proteins are expressed in the testes and/or ovaries (e.g., Jarmuz et al., 2002), this appears, perhaps not unexpectedly, to be of particular importance for the protection of germline.”
- Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. (2003, background): “In addition, APOBEC3G, like the related produced as JR.FL or VSV-G pseudotypes by cotransfection of 293TAID, is likely to be regulated by cellular activation signals using Lipofectamine 2000 (Invitrogen) and were quantitated by p24 and these could increase expression to limiting levels. or p27 ELISA”
- Retroviral restriction by APOBEC proteins (2004, background): “APOBEC3G belongs to a larger family of bona fide and putative cytosine-deaminase protein”
- The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA (2003, methodology): “In the bottom panel, the rows are: (7) wild-type viruses, without CEM15; (8) wild-type viruses, with CEM15. b, Comparison of G to A mutation frequency in newly synthesized DNA (301 nucleotides in U3-R-U5 region, n ¼ 8).”