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- W2968854070 endingPage "1730" @default.
- W2968854070 startingPage "1718" @default.
- W2968854070 abstract "5-Methylcytosine (5mC), the major modified DNA base in mammalian cells, can be oxidized enzymatically to 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC), and 5-carboxylcytosine (5caC) by the Ten-Eleven-Translocation (TET) family of proteins. Whereas 5fC and 5caC are recognized and removed by base excision repair proteins, the 5hmC base accumulates to substantial levels in certain cell types such as brain-derived neurons and is viewed as a relatively stable DNA base. As such, the existence of reader proteins that recognize 5hmC would be a logical assumption, and various searches have been undertaken to identify proteins that specifically bind to 5hmC and the other oxidized 5mC bases. However, the existence of definitive 5hmC readers has remained unclear and proteins interacting specifically with 5fC or 5caC are also very few. On the other hand, 5hmC is incapable of interacting with a number of proteins that recognize 5mC at CpG sequences, suggesting that 5hmC is an anti-reader modification that may serve to displace 5mC readers from DNA. In this review article, we discuss candidate proteins that may interact with oxidized 5mC bases." @default.
- W2968854070 created "2019-08-22" @default.
- W2968854070 creator A5024171279 @default.
- W2968854070 creator A5042620320 @default.
- W2968854070 creator A5048312997 @default.
- W2968854070 date "2020-03-01" @default.
- W2968854070 modified "2023-09-27" @default.
- W2968854070 title "Protein Interactions at Oxidized 5-Methylcytosine Bases" @default.
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