Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain.

By Chao Xu, Xiao Wang, Ke Liu, I. A. Roundtree, W. Tempel, Yanjun Li, Zhike Lu, Chuan He, J. Min. Nature Chemical Biology, 2014

657 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7593d8448878742e4d4c05c6ac334e0afbf87228

How researchers see this paper

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In Molecular Biology

1. Chuan He
2. Samie R. Jaffrey
3. Kate D. Meyer
4. I. A. Roundtree
5. Richard I. Gregory
6. Hailing Shi
7. P. He
8. S. Zaccara

Citations in the corpus

• METTL3 promotes translation in human cancer cells (2016, background): “Emerging models implicate the so-called reader proteins, the best characterized of which are the YTH domain-containing proteins, YTHDF1, -2, and -3 (YTH domain-containing family 1, -2, and -3), that selectively bind m(6)A-modified RNAs (Dominissini et al., 2012; Li et al., 2014; Theler et al., 2014;”
• YTHDC1 mediates nuclear export of N6-methyladenosine methylated mRNAs (2017, methodology): “YTHDC1 facilitates RNA binding to SRSF3 and NXF1 The YTH domain of YTHDC1 has been extensively biochemically characterized as a nuclear ‘reader’ protein, and binds mRNA with preference for m6A (Xu et al., 2014).”
• Rethinking m6A Readers, Writers, and Erasers (2017, methodology): “The structure of m6A mRNA complexed with a YTH domain was solved by several groups (Luo & Tong 2014, Theler et al. 2014, Xu et al. 2014).”