Web3 feb. 2024 · Lin, T. B. et al. Inhibiting MLL1-WDR5 interaction ameliorates neuropathic allodynia by attenuating histone H3 lysine 4 trimethylation-dependent spinal mGluR5 transcription. Pain 161, 1995–2009 ... Web5 nov. 2024 · MLL1-WDR5 interaction Phenyltriazole scaffold inhibitor Antitumor MLL1 HMT activity 1. Introduction Mixed-lineage leukemia 1 (MLL1) belongs to the SET1 family of methyltransferases, and it catalyzes the mono-, di-, and trimethylation of histone 3 lysine 4 (H3K4) as well as facilitates transcriptional initiation [[1], [2], [3], [4]].
MM-102-TFA-(HMTase-Inhibitor-IX-(TFA))-Histone …
Web15 aug. 2012 · Mixed lineage leukemia 1 (MLL1) is a histone H3 lysine 4 (H3K4) methyltransferase, and targeting the MLL1 enzymatic activity has been proposed as a novel therapeutic strategy for the treatment of acute leukemia harboring MLL1 fusion proteins. The MLL1/WDR5 protein-protein interaction is essential for MLL1 enzymatic activity ... Web21 jun. 2024 · WDR5, a histone H3 lysine 4 (H3K4) presenter, together with H3K4 methyltransferases MLL1-MLL4 and other protein subunits, DPY30, ASH2L, and RBBP5, forms protein complexes and plays a vital role in histone methylation, chromatin remodelling, transcriptional activation of target genes, and normal and disease biology [ 9, 10, 11 ]. bolind a/s
Discovery of a potent MLL1 and WDR5 protein-protein …
Web21 nov. 2008 · Like histone H3 bound to WDR5, the N terminus of the MLL1 Win peptide forms a 3 10-helix that fits snuggly into the outer opening of the central cavity, like a cork in a bottle (Fig. 1).Conserved MLL1 residues GSARAE all participate in the formation of the 3 10-helix, which is stabilized by intramolecular i → i+3 main-chain hydrogen bonds … Web17 mei 2016 · Blocking MLL1–WDR5 interaction by small molecule inhibitor MM-401 disrupts MLL1 chromatin association at a significant subset of genes that are important … Web1 feb. 2024 · We prepared a recombinant version of the MLL1 core complex (composed of MLL1, WDR5, RbBP5, ASH2L, and DPY30 subunits) and compared its enzymatic activities on both unmodified histone H3(1–15) and H3(1–15)Q5ser peptides using matrix-assisted laser desorption ionization–time of flight (MALDI-TOF) mass spectrometry. glycan therapeutics llc