The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases - Wikidata - awgldk - TriplyDB

The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases

The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases

http://www.wikidata.org/entity/Q27676833

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Structural analysis of the KANSL1/WDR5/KANSL2 complex reveals that WDR5 is required for efficient assembly and chromatin targeting of the NSL complex Hijacked in cancer: the KMT2 (MLL) family of methyltransferases On WD40 proteins: propelling our knowledge of transcriptional control?Intrinsic protein disorder in histone lysine methylation.Structural Basis for WDR5 Interaction (Win) Motif Recognition in Human SET1 Family Histone Methyltransferases Molecular basis for DPY-30 association to COMPASS-like and NURF complexes Structural basis for activity regulation of MLL family methyltransferases Targeted Disruption of the Interaction Between WD-40 Repeat Protein 5 (WDR5) and Mixed Lineage Leukemia (MLL)/SET1 Family Proteins Specifically Inhibits MLL1 and SETd1A Methyltransferase Complexes A non-active-site SET domain surface crucial for the interaction of MLL1 and the RbBP5/Ash2L heterodimer within MLL family core complexes Genetic organization of interphase chromosome bands and interbands in Drosophila melanogaster WRAD: enabler of the SET1-family of H3K4 methyltransferases.The role of WDR5 in silencing human fetal globin gene expression.Sperm and spermatids contain different proteins and bind distinct egg factors.Promoter RNA links transcriptional regulation of inflammatory pathway genes.A phosphorylation switch on RbBP5 regulates histone H3 Lys4 methylation.WD repeat-containing protein 5 (WDR5) localizes to the midbody and regulates abscission.Epigenetics: Disrupting histone lysine methylation.The Human Mixed Lineage Leukemia 5 (MLL5), a Sequentially and Structurally Divergent SET Domain-Containing Protein with No Intrinsic Catalytic Activity.SET for life: biochemical activities and biological functions of SET domain-containing proteins The many facets of MLL1 regulation.Small molecule epigenetic inhibitors targeted to histone lysine methyltransferases and demethylases.Mind the methyl: methyllysine binding proteins in epigenetic regulation.Synthesis, Optimization, and Evaluation of Novel Small Molecules as Antagonists of WDR5-MLL Interaction.CHARGE and Kabuki Syndromes: Gene-Specific DNA Methylation Signatures Identify Epigenetic Mechanisms Linking These Clinically Overlapping Conditions.Inhibitors of Protein Methyltransferases and Demethylases.Targeting human SET1/MLL family of proteins.A SET-domain-independent role of WRAD complex in cell-cycle regulatory function of mixed lineage leukemia.Evolving Catalytic Properties of the MLL Family SET Domain.Development and Use of Assay Conditions Suited to Screening for and Profiling of SET-Domain-Targeted Inhibitors of the MLL/SET1 Family of Lysine Methyltransferases.Structural basis of arginine asymmetrical dimethylation by PRMT6.Small-molecule inhibition of MLL activity by disruption of its interaction with WDR5 Assembling a COMPASS.Upon Infection the Cellular WD Repeat-containing Protein 5 (WDR5) Localizes to Cytoplasmic Inclusion Bodies and Enhances Measles Virus Replication.Regulation of neuronal survival by DNA methyltransferases.Bivalent Epigenetic Control of Oncofetal Gene Expression in Cancer.FBXW7 regulates DISC1 stability via the ubiquitin-proteosome system.Moonlighting with WDR5: A Cellular Multitasker.CHARGE and Kabuki syndromes: a phenotypic and molecular link.Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin.

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The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases

http://www.wikidata.org/entity/Q27676833

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2012 nî lūn-bûn

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2012 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2012 թվականի մայիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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The plasticity of WDR5 peptide ...... of histone methyltransferases

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The plasticity of WDR5 peptide ...... of histone methyltransferases

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The plasticity of WDR5 peptide ...... of histone methyltransferases

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The plasticity of WDR5 peptide ...... of histone methyltransferases

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The plasticity of WDR5 peptide ...... of histone methyltransferases

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The plasticity of WDR5 peptide ...... of histone methyltransferases

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Hwabin Lee

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Jean-Francois Couture

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Joseph S Brunzelle

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Pamela Zhang

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P2860

Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex

The BRCT-domain containing protein PTIP links PAX2 to a histone H3, lysine 4 methyltransferase complex

Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression

Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex

Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes

Structural basis for molecular recognition and presentation of histone H3 by WDR5

PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex

Coactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferases

Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus

Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5

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339667

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10.1093/NAR/GKR1235

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9

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40

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221767950

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22266653

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histone methyltransferase activity

Lysine methyltransferase 2C

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3351189

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