Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.
By Y. Dou, Thomas A. Milne, A. Tackett, Edwin R. Smith, A. Fukuda, J. Wysocka, C. D. Allis, Brian T. Chait, J. Hess, R. Roeder. Cell, 2005
713 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/308eb74d708e29de799918c57bc5ffd83ed635a8
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In Molecular Biology
Citations in the corpus
- Acetylation of the p53 DNA-binding domain regulates apoptosis induction. (2006, methodology): “Loss of acetylation due to hMOF or TIP60 depletion, prevents ATM from phosphorylating downstream effectors, such as p53 and CHK2 (Sun et al., 2005). hMOF and TIP60 physically interact with ATM and p53 (Dou et al., 2005; Tyteca et al., 2006).”
- Wnt signaling: is the party in the nucleus? (2006, background): “The mammalian SET1-related HMT proteins form complexes with Ash2, menin, HCF, WRD5, and RbBP5, and are thought to be frequent direct targets of transcriptional regulators (Yokoyama et al. 2004; Dou et al. 2005; Wysocka et al. 2005b).”
- The diverse functions of histone lysine methylation (2005, background): “The second identified methylated-K4-binding protein, WDR5, is a component of a mixed-lineage leukemia (MLL) complex that possesses H3-K4 meth-yltranferase activity 23,106 .”
- Histone acetyltransferase complexes: one size doesn't fit all (2007, background): “In humans, the MOF protein is associated with other complexes, including the MLL (mixed lineage leukaemia) complex, which confers a more global function for MO”