Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase
By R. Bransteitter, P. Pham, M. Scharff, Myron F. Goodman. Proceedings of the National Academy of Sciences of the United States of America, 2003
699 citations recorded by the source corpus.
Subfields: Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/d7c013b270cbb9944923e95d6c8d94ad770c5339
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Citations in the corpus
- DNA deamination mediates innate immunity to retroviral infection. (2003, background): “…substrate (Figure 1), an action of an innate antiviral mechanism (Sova and Volactivity that has recently also been observed with other sky, 1993; von Schwedler et al., 1993; Simon and Malim, APOBEC family members, AID (Bransteitter et al., 2003; 1996; Madani and Kabat, 1998; Simon et al., 1998a).”
- Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation (2003, background): “Purified AID catalyses the deamination of C to U on single-stranded (ss)DN”
- Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain (2011, neutral): “However, 5mCs appear to be less favorable substrates than unmethylated cytosines for AID in vitro (Bransteitter et al., 2003; Larijani et al., 2005), suggesting that AID might not directly deaminate 5mCs during the process of active DNA demethylation.”
- Class-switch recombination: interplay of transcription, DNA deamination and DNA repair (2004, background): “Second, in vitro studies showed that purified AID is a ssDNA deaminase that converts deoxycytidine residues to deoxyuridine on target DN”
- Reversing DNA Methylation: Mechanisms, Genomics, and Biological Functions (2014, positive): “However, AID/APOBEC only efficiently acts on single-strand but not double-strand DNA (Bransteitter et al., 2003), and exhibit substantially lower activity on 5mC (10- to 20-fold) relative to cytosine, their canonical substrate (Nabel et al., 2012).”
- Induction of activation‐induced cytidine deaminase gene expression by IL‐4 and CD40 ligation is dependent on STAT6 and NFκB (2004, background): “However, recent data has shown that AID catalyzes deamination of dC residues on singlestranded DNA in vitro, but not on double-stranded DNA, RNA‐ DNA hybrids or RNA (17, 18 ).”