Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT - Wikidata - wikimedia - TriplyDB

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

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Specificity and mechanism of the histone methyltransferase Pr-Set7.Lysine methylation of the NF-κB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-κB signaling On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex Identification of a novel gene, CIA6, required for normal pyrenoid formation in Chlamydomonas reinhardtii In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases The SET-domain protein superfamily: protein lysine methyltransferases The functional diversity of protein lysine methylation Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase Multiple-Site Trimethylation of Ribosomal Protein L11 by the PrmA Methyltransferase Structural origins for the product specificity of SET domain protein methyltransferases SET7/9 Catalytic Mutants Reveal the Role of Active Site Water Molecules in Lysine Multiple Methylation Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3 Histone lysine methyltransferases as anti-cancer targets for drug discovery Theoretical insights into catalytic mechanism of protein arginine methyltransferase 1 Histone methyltransferase SETD3 regulates muscle differentiation Mixed lineage leukemia: a structure-function perspective of the MLL1 protein.Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20.Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases.Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase.Genome-wide identification, phylogenetic and co-expression analysis of OsSET gene family in rice Direct evidence for methyl group coordination by carbon-oxygen hydrogen bonds in the lysine methyltransferase SET7/9 Biochemical reconstitution and phylogenetic comparison of human SET1 family core complexes involved in histone methylation Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specificity.Structural and sequence motifs of protein (histone) methylation enzymes.Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase.Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases Rubisco catalytic properties of wild and domesticated relatives provide scope for improving wheat photosynthesis.Structural dynamics of protein lysine methylation and demethylation.The role of a newly identified SET domain-containing protein, SETD3, in oncogenesis.Plant SET domain-containing proteins: structure, function and regulation Ab initio quantum mechanical/molecular mechanical molecular dynamics simulation of enzyme catalysis: the case of histone lysine methyltransferase SET7/9.Rubisco in complex with Rubisco large subunit methyltransferase How do SET-domain protein lysine methyltransferases achieve the methylation state specificity? Revisited by Ab initio QM/MM molecular dynamics simulations.Chemical mechanisms of histone lysine and arginine modifications Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase SET7/9 mediated methylation of non-histone proteins in mammalian cells.SET domain-containing Protein 4 (SETD4) is a Newly Identified Cytosolic and Nuclear Lysine Methyltransferase involved in Breast Cancer Cell Proliferation.Structure and function of histone H3 lysine 9 methyltransferases and demethylases.

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Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

http://www.wikidata.org/entity/Q27641462

description

2003 nî lūn-bûn

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2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի հուլիսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

@ast

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

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Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

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type

label

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

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Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

@en

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

@nl

prefLabel

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

@ast

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

@en

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

@nl

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Nature structural biology

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Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

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P2093

E Megan Flynn

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James H Hurley

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Raymond C Trievel

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Robert L Houtz

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scholarly article

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4596348

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10.1038/NSB946

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7

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2003-07-01T00:00:00Z

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12819771

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