Menin-MLL inhibitors reverse oncogenic activity of MLL fusion proteins in leukemia

MLL fusion genes often encode leukemogenic proteins that depend on interaction with menin, a component of the MLL SET1-like histone methyltransferase complex. MI-2 and MI-3 are the first small molecules that can block menin–MLL fusion protein interaction and their oncogenic effects in cells. Translo...

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Veröffentlicht in:	Nature chemical biology 2012-01, Vol.8 (3), p.277-284
Hauptverfasser:	Grembecka, Jolanta, He, Shihan, Shi, Aibin, Purohit, Trupta, Muntean, Andrew G, Sorenson, Roderick J, Showalter, Hollis D, Murai, Marcelo J, Belcher, Amalia M, Hartley, Thomas, Hess, Jay L, Cierpicki, Tomasz
Format:	Artikel
Sprache:	eng
Schlagworte:	631/92/556 631/92/613 631/92/96 692/699/67/1990/283 Animals Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology Antineoplastic Agents - therapeutic use Apoptosis Apoptosis - drug effects Biochemical Engineering Biochemistry Bioorganic Chemistry Cell Biology Cell Differentiation - drug effects Cell proliferation Cell Proliferation - drug effects Cells, Cultured Chemistry Chemistry and Materials Science Chemistry/Food Science Cofactors Differentiation Dose-Response Relationship, Drug Drug Screening Assays, Antitumor Fusion protein Gene expression HEK293 Cells Histone-Lysine N-Methyltransferase Humans Inhibitors Leukemia Leukemia - drug therapy Leukemia - genetics Leukemia - metabolism Leukemia - pathology Leukemogenesis MEN1 protein Mice MLL protein Molecular biology multiple endocrine neoplasia Mutation Myeloid-Lymphoid Leukemia Protein - antagonists & inhibitors Myeloid-Lymphoid Leukemia Protein - genetics Myeloid-Lymphoid Leukemia Protein - metabolism Oncology Prognosis Proteins Proto-Oncogene Proteins - antagonists & inhibitors Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins - metabolism Structure-Activity Relationship Transformation Translocation
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