ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation.

By Tatsuya Nakamura, Toshiki Mori, Shinichiro Tada, W. Krajewski, Tanya Rozovskaia, R. Wassell, G. Dubois, A. Mazo, Carlo Maria Croce, E. Canaani. Molecules and Cells, 2002

780 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d879bcb0da303f97cc4d9db7b54ba8749a6eade6

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Citations in the corpus

Covalent histone modifications: miswritten, misinterpreted, and miserased in human cancers (2010, background): “, and was later shown to encode a major H3K4-specific HMT enzym”
Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. (2005, background): “…methyltransferase activity (Beisel et al., 2002; Cao et al., 2002; Czermin et al., 2002; Kuzmichev et al., 2002; Milne et al., 2002; Muller et al., 2002; Nakamura et al., 2002), the PRC1 complex has been recently demonstrated to possess H2A-K119 ubiquitin E3 ligase activity (Wang et al., 2004a).”
Histone methylation by PRC2 is inhibited by active chromatin marks. (2011, background): “Among the trxG proteins that keep PcG target genes active are the HMTases Trx and Ash1, which methylate H3K4 and H3K36, respectively (Milne et al., 2002; Nakamura et al., 2002; Tanaka et al., 2007).”
Pharmacologic disruption of Polycomb-repressive complex 2-mediated gene repression selectively induces apoptosis in cancer cells. (2007, background): “PRCs contain intrinsic histone methyltransferase (HMTase) activity and maintain gene repression through methylation of core histones (Beisel et al. 2002; Cao et al. 2002; Milne et al. 2002; Muller et al. 2002; Nakamura et al. 2002).”
Potent inhibition of DOT1L as treatment of MLL-fusion leukemia. (2013, background): “The MLL gene encodes a large multidomain protein (MLL) that regulates transcription of developmental genes including the HOX genes.1 The amino terminal portion of the protein contains regions that target MLL to DNA directly, whereas the carboxyl terminal portion of the protein contains a Su(Var)3-9,”
Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. (2003, background): “MLL/ALL is a componentsition between initiation and elongation, and Set1 inof an H3-K4 methylase that is recruited to active Hoxteracts with the form of Pol II whose CTD is phosphorypromoters (Milne et al., 2002; Nakamura et al., 2002).lated at serine 5 but not serine 2.”
The menin tumor suppressor protein is an essential oncogenic cofactor for MLL-associated leukemogenesis. (2005, background): “MLL possesses inherent histone methyltransferase (HMT) activity, which is specific for lysine 4 of histone H3 (H3K4) (Milne et al., 2002; Nakamura et al., 2002), a mark that is generally associated with transcriptionally active states of chromatin (Noma et al., 2001; Strahl et al., 1999), thus…”
The SWI/SNF complex — chromatin and cancer (2004, background): “MLL is also present with SWI/SNF as well as the NuRD and SIN3A covalent chromatin-remodelling complexes in a supercomplex that remodels, acetylates, deacetylates and methylates histones to regulate transcriptio”
Leukemia Proto-Oncoprotein MLL Forms a SET1-Like Histone Methyltransferase Complex with Menin To Regulate Hox Gene Expression (2004, background): “(44), we were unable to coprecipitate either the corepressor Sin3A or chromatin remodeling protein BRM with MLL or MLL.”
Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact (2012, positive): “KDM1A contains a flavin adenine dinucleotide (FAD)-dependent amine oxidase domain that demethylates H3K4me2 and H3K4me1 and modulates gene expression (Figures 1B and 1C) (Shi et al., 2004).”
Elongation by RNA polymerase II: the short and long of it. (2004, background): “Only recently was it determined that MLL, and its related proteins, function as histone methyltransferases (Milne et al. 2002; Nakamura et al. 2002).”