N6-Methyladenosine in Nuclear RNA is a Major Substrate of the Obesity-Associated FTO
By G. Jia, G. Zheng, Chengqi Yi, Tomas Lindahl, D. Anastasiou, Yiming Yu, William J. Israelsen, M. Boxer, S. Dimov, Abhishek K. Jha and 19 more. Nature Chemical Biology, 2011
2,963 citations recorded by the source corpus.
Subfields: Cancer Research, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/3298f4c09fc00263faa61029d56c94f0e3411475
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Citations in the corpus
- METTL14 Inhibits Hematopoietic Stem/Progenitor Differentiation and Promotes Leukemogenesis via mRNA m6A Modification (2017, positive): “The m(6)A level was calculated as the ratio of m(6)A to A (Jia et al., 2011).”
- The m6A reader YTHDF1 promotes ovarian cancer progression via augmenting EIF3C translation (2020, positive): “The interaction between ‘writers’ and ‘erasers’ determines the dynamic and reversible feature of m6A modification (7,8).”
- METTL14 suppresses the metastatic potential of hepatocellular carcinoma by modulating N6‐methyladenosine‐dependent primary MicroRNA processing (2017, neutral): “As expected, we observed a clear and significant decrease of METTL14 and FTO in HCC tissues (Supporting Fig.”
- A majority of m6A residues are in the last exons, allowing the potential for 3′ UTR regulation (2015, neutral): “Furthermore, mutations in one of the human demethylase genes is associated with a phenotype (overweight) (Jia et al. 2011; Zheng et al. 2013).”
- N 6-methyladenosine alters RNA structure to regulate binding of a low-complexity protein (2017, neutral): “N6-methyladenosine (m6A) is the most abundant internal modification of messenger RNAs (mRNAs) and has known functions in RNA splicing, export, translation and decay (1). m6A is a reversible and dynamic modification that is introduced at a subset of RRACH motifs (R = A/G, H = A/C/U) through the activ”
- Meclofenamic acid selectively inhibits FTO demethylation of m6A over ALKBH5 (2014, positive): “The m6A residues in HeLa cells exist in an FTO activity-dependent manner as seen for other cell lines, such as 293FT and BE(2)-C (3,42).”
- YTH Domain: A Family of N6-methyladenosine (m6A) Readers (2018, neutral): “Similar to other epigenetic modifications, m6A is dynamic and reversible, established mainly by the METTL3–METTL14 methyltransferase complex [20,21] and removed by demethylases including the fat mass and obesity-associated protein (FTO) [22] and AlkB homolog 5 RNA demethylase (ALKBH5) [23].”
- A protocol for RNA methylation differential analysis with MeRIP-Seq data and exomePeak R/Bioconductor package. (2014, positive): “44%) after FTO knockout is consistent with the fact that FTO is a known m6A demethylase [35].”
- Zc3h13 regulates nuclear RNA m6A methylation and mouse embryonic stem cell self-renewal (2018, positive): “Indeed, the m6A methyltransferases Mettl3, Mettl14 and demethylases FTO and ALKBH5 have all been found to co-localize with markers of nuclear speckles (Jia et al., 2011; Zheng et al., 2013).”
- Targeting FTO suppresses cancer stem cell maintenance and immune evasion (2020, positive): “Fat mass and obesity-associated protein (FTO) was identified as the first RNA demethylase that can remove m6A from RNA through an α-Ketoglutarate (α-KG) and Fe(II)-dependent mechanism (Jia et al., 2011), suggesting that m6A is a type of reversible and dynamic RNA modification (Jia et al.”
- m6A RNA methylation: from mechanisms to therapeutic potential (2021, positive): “An important facet of m 6 A methylation as a regulatory system is its reversibility. m 6 A on mRNA can be removed by FTO and ALKBH5, m 6 A demethylases, posing an additional dimension of regulation for the m 6 A epitranscriptome (Jia et al , 2011; Zheng et al , 2013).”
- m6A RNA Methylation Regulates the Self-Renewal and Tumorigenesis of Glioblastoma Stem Cells (2017, positive): “, 1975), the physiological significance of m6A modification in mRNA has only been appreciated in recent years because of breakthrough findings of two mammalian RNA demethylases, the fat mass- and obesity-associated protein (FTO) and alkylation repair homolog protein 5 (ALKBH5), which demonstrated th”