Structural origins for the product specificity of SET domain protein methyltransferases - Wikidata - thesis-toulmin - TriplyDB

Structural origins for the product specificity of SET domain protein methyltransferases

Structural origins for the product specificity of SET domain protein methyltransferases

http://www.wikidata.org/entity/Q27653167

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The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism The functional diversity of protein lysine methylation Carbon-oxygen hydrogen bonding in biological structure and function Protein methylation at the surface and buried deep: thinking outside the histone box Structural Biology of Human H3K9 Methyltransferases SET7/9 Catalytic Mutants Reveal the Role of Active Site Water Molecules in Lysine Multiple Methylation Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3 A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases Structure of the Catalytic Domain of EZH2 Reveals Conformational Plasticity in Cofactor and Substrate Binding Sites and Explains Oncogenic Mutations Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin.Catalytic and functional roles of conserved amino acids in the SET domain of the S. cerevisiae lysine methyltransferase Set1 Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae.Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27)Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives Comparative analyses of SUV420H1 isoforms and SUV420H2 reveal differences in their cellular localization and effects on myogenic differentiation.Bioinformatic Identification of Novel Methyltransferases Inner workings and regulatory inputs that control Polycomb repressive complex 2 QM/MM MD and free energy simulations of G9a-like protein (GLP) and its mutants: understanding the factors that determine the product specificity Dynamics of histone lysine methylation: structures of methyl writers and erasers Direct evidence for methyl group coordination by carbon-oxygen hydrogen bonds in the lysine methyltransferase SET7/9 Arabidopsis trithorax-related3/SET domain GROUP2 is required for the winter-annual habit of Arabidopsis thaliana.Kinetic isotope effects reveal early transition state of protein lysine methyltransferase SET8.Functional roles in S-adenosyl-L-methionine binding and catalysis for active site residues of the thiostrepton resistance methyltransferase Structure of Naegleria Tet-like dioxygenase (NgTet1) in complexes with a reaction intermediate 5-hydroxymethylcytosine DNA.Transition state for the NSD2-catalyzed methylation of histone H3 lysine 36 Division of labor between the chromodomains of HP1 and Suv39 methylase enables coordination of heterochromatin spread.Establishing a hematopoietic genetic network through locus-specific integration of chromatin regulators.Regulation of H3K4 trimethylation via Cps40 (Spp1) of COMPASS is monoubiquitination independent: implication for a Phe/Tyr switch by the catalytic domain of Set1.Degrees make all the difference: the multifunctionality of histone H4 lysine 20 methylation Set2-dependent K36 methylation is regulated by novel intratail interactions within H3 Every methyl counts--epigenetic calculus.Structure and function of histone H3 lysine 9 methyltransferases and demethylases.Targets in epigenetics: inhibiting the methyl writers of the histone code Structural Chemistry of Human SET Domain Protein Methyltransferases.Protein and nucleic acid methylating enzymes: mechanisms and regulation QM/MM MD and free energy simulation study of methyl transfer processes catalyzed by PKMTs and PRMTs.Structural Insights into Substrate Recognition and Catalysis in Outer Membrane Protein B (OmpB) by Protein-lysine Methyltransferases from Rickettsia.Evolving Catalytic Properties of the MLL Family SET Domain.Enhancing Paradynamics for QM/MM Sampling of Enzymatic Reactions.

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Structural origins for the product specificity of SET domain protein methyltransferases

http://www.wikidata.org/entity/Q27653167

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2008 nî lūn-bûn

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2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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Structural origins for the product specificity of SET domain protein methyltransferases

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Structural origins for the product specificity of SET domain protein methyltransferases

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Structural origins for the product specificity of SET domain protein methyltransferases

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Structural origins for the product specificity of SET domain protein methyltransferases

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Structural origins for the product specificity of SET domain protein methyltransferases

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Structural origins for the product specificity of SET domain protein methyltransferases

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Structural origins for the product specificity of SET domain protein methyltransferases

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Structural origins for the product specificity of SET domain protein methyltransferases

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P2093

Jean-François Couture

http://www.w3.org/2001/XMLSchema#string

Joseph S Brunzelle

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Lynnette M A Dirk

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Raymond C Trievel

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Robert L Houtz

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P2860

Structure and catalytic mechanism of the human histone methyltransferase SET7/9

Structural basis for the methylation site specificity of SET7/9

Specificity and mechanism of the histone methyltransferase Pr-Set7.

Regulation of p53 activity through lysine methylation

Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases

Structural basis for the product specificity of histone lysine methyltransferases

The SET-domain protein superfamily: protein lysine methyltransferases

Improved methods for building protein models in electron density maps and the location of errors in these models

Processing of X-ray diffraction data collected in oscillation mode

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20659-64

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10.1073/PNAS.0806712105

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