SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells - Wikidata - awgldk - TriplyDB

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

http://www.wikidata.org/entity/Q28270360

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Genome-wide survey and developmental expression mapping of zebrafish SET domain-containing genes The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair Biochemical characterization of the zinc-finger protein 217 transcriptional repressor complex: identification of a ZNF217 consensus recognition sequence Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains The SET-domain protein superfamily: protein lysine methyltransferases Regulation of the Telomerase Reverse Transcriptase Subunit through Epigenetic Mechanisms Targeting histone methyltransferases and demethylases in clinical trials for cancer therapy Dysregulation of protein methyltransferases in human cancer: An emerging target class for anticancer therapy SMYD proteins: key regulators in skeletal and cardiac muscle development and function Histone lysine-specific methyltransferases and demethylases in carcinogenesis: new targets for cancer therapy and prevention Histone methylations in heart development, congenital and adult heart diseases Role of epigenetic aberrations in the development and progression of human hepatocellular carcinoma Dietary intake alters gene expression in colon tissue: possible underlying mechanism for the influence of diet on disease.Smyd3 is required for the development of cardiac and skeletal muscle in zebrafish Crystal Structure of Cardiac-specific Histone Methyltransferase SmyD1 Reveals Unusual Active Site Architecture 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 Crystal Structures of Histone and p53 Methyltransferase SmyD2 Reveal a Conformational Flexibility of the Autoinhibitory C-Terminal Domain Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3 Structure of Human SMYD2 Protein Reveals the Basis of p53 Tumor Suppressor Methylation Integrating Epigenomics into the Understanding of Biomedical Insight RNAi screening with shRNAs against histone methylation-related genes reveals determinants of sorafenib sensitivity in hepatocellular carcinoma cells Effect of phenylhexyl isothiocyanate on aberrant histone H3 methylation in primary human acute leukemia Single-wall carbon nanohorns inhibited activation of microglia induced by lipopolysaccharide through blocking of Sirt3 Single-walled carbon nanohorn (SWNH) aggregates inhibited proliferation of human liver cell lines and promoted apoptosis, especially for hepatoma cell lines A Drosophila Smyd4 homologue is a muscle-specific transcriptional modulator involved in development The putative RNA helicase HELZ promotes cell proliferation, translation initiation and ribosomal protein S6 phosphorylation Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex Cardiac deletion of Smyd2 is dispensable for mouse heart development The methyltransferase SMYD3 mediates the recruitment of transcriptional cofactors at the myostatin and c-Met genes and regulates skeletal muscle atrophy C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in oncogenesis Evolutionary History of the Smyd Gene Family in Metazoans: A Framework to Identify the Orthologs of Human Smyd Genes in Drosophila and Other Animal Species Regulation of MLL1 H3K4 methyltransferase activity by its core components Epigenetic modifications and human disease Mutated KRAS results in overexpression of DUSP4, a MAP-kinase phosphatase, and SMYD3, a histone methyltransferase, in rectal carcinomas.Identification of Epigenetic Biomarkers of Lung Adenocarcinoma through Multi-Omics Data Analysis Elevated expression of protein regulator of cytokinesis 1, involved in the growth of breast cancer cells.Evolution of SET-domain protein families in the unicellular and multicellular Ascomycota fungi.Genome-wide profiling of histone h3 lysine 4 and lysine 27 trimethylation reveals an epigenetic signature in prostate carcinogenesis.

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SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

http://www.wikidata.org/entity/Q28270360

description

2004 nî lūn-bûn

@nan

2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի օգոստոսին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

@ast

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

@en

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

@nl

type

label

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

@ast

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

@en

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

@nl

prefLabel

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

@ast

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

@en

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

@nl

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Nature Cell Biology

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SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

@en

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Masashi Morita

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

Meihua Li

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

Ryuichiro Yagyu

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

Ryuji Hamamoto

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

Yoichi Furukawa

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

Yuko Iimura

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

Yusuke Nakamura

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

P2860

Translating the Histone Code

Regulation of chromatin structure by site-specific histone H3 methyltransferases

A novel nk-2-related transcription factor associated with human fetal liver and hepatocellular carcinoma

Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet.

The language of covalent histone modifications

The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation.

MLL2, the second human homolog of the Drosophila trithorax gene, maps to 19q13.1 and is amplified in solid tumor cell lines

Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3

Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails

MLL targets SET domain methyltransferase activity to Hox gene promoters

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P304

731-40

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scholarly article

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248762

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10.1038/NCB1151

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P433

8

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6

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P50

Fabio Pittella Silva

P577

2004-08-01T00:00:00Z

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

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8472569

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1022858088

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P698

15235609

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