Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4.

By M. Vermeulen, Klaas W. Mulder, Sergei Denissov, W. Pijnappel, Frederik M. A. van Schaik, Radhika A. Varier, Marijke P. A. Baltissen, H. Stunnenberg, Matthias Mann, H. Timmers. Cell, 2007

923 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/b22aead0779d639199c718b649a4c112e9adbf2d

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In Molecular Biology

1. D. Reinberg
2. A. Bird
3. C. D. Allis
4. J. Whetstine
5. K. Helin
6. Yi Zhang
7. A. Deaton
8. Alexander J. Ruthenburg

Citations in the corpus

• A double take on bivalent promoters. (2013, background): “The PHD finger of the TAF3 subunit of TFIID recognizes H3K4me3 (Vermeulen et al. 2007), whereas the TAF1 subunit binds to acetylated lysines on histones H3 and H4 via its bromodomains (Jacobson et al. 2000).”
• Covalent histone modifications: miswritten, misinterpreted, and miserased in human cancers (2010, background): “For example, the targeting of TFIID to H3K4me3 at promoters has been suggested to help anchor and/or recruit TFIID and associated machinery for active transcriptional initiatio”
• Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. (2008, background): “However, another study has shown that the basal transcription factor TFIID binds to the H3K4me3 mark via the PHD finger of TAF3, indicating that the interaction between TFIID and H3K4me3 may be important for PIC assembly and subsequent activation of genes in mammalian cells (Vermeulen et al. 2007).”