The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation. - Test2 - elhamkhani - TriplyDB

The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.

The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.

http://www.wikidata.org/entity/Q35650662

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Interplay between Transcription Factors and the Epigenome: Insight from the Role of RUNX1 in Leukemia Myeloid malignancies: mutations, models and management Protein lysine acetylation by p300/CBP A stable transcription factor complex nucleated by oligomeric AML1–ETO controls leukaemogenesis The Role of Histone Acetyltransferases in Normal and Malignant Hematopoiesis Generation of a Selective Small Molecule Inhibitor of the CBP/p300 Bromodomain for Leukemia Therapy Diverse small molecule inhibitors of human apurinic/apyrimidinic endonuclease APE1 identified from a screen of a large public collection Salicylate, diflunisal and their metabolites inhibit CBP/p300 and exhibit anticancer activity Histone acetyltransferase inhibitors block neuroblastoma cell growth in vivo PRMT4 blocks myeloid differentiation by assembling a methyl-RUNX1-dependent repressor complex.Cancer genetics and epigenetics: two sides of the same coin?A histone acetyltransferase p300 inhibitor C646 induces cell cycle arrest and apoptosis selectively in AML1-ETO-positive AML cells Differentiation therapy for the treatment of t(8;21) acute myeloid leukemia using histone deacetylase inhibitors Small-molecule inhibitors of acetyltransferase p300 identified by high-throughput screening are potent anticancer agents.Cooperation between RUNX1-ETO9a and novel transcriptional partner KLF6 in upregulation of Alox5 in acute myeloid leukemia.Genome-wide co-occupancy of AML1-ETO and N-CoR defines the t(8;21) AML signature in leukemic cells.RUNX1 mutations in clonal myeloid disorders: from conventional cytogenetics to next generation sequencing, a story 40 years in the making BET Bromodomain Inhibition Suppresses the Function of Hematopoietic Transcription Factors in Acute Myeloid Leukemia.Identification of a dynamic core transcriptional network in t(8;21) AML that regulates differentiation block and self-renewal.Regulation of AKT signaling by Id1 controls t(8;21) leukemia initiation and progression.PRMT1 interacts with AML1-ETO to promote its transcriptional activation and progenitor cell proliferative potential Depletion of RUNX1/ETO in t(8;21) AML cells leads to genome-wide changes in chromatin structure and transcription factor binding.Combined gene expression and DNA occupancy profiling identifies potential therapeutic targets of t(8;21) AML.JMJD1C is required for the survival of acute myeloid leukemia by functioning as a coactivator for key transcription factors.ERG and FLI1 binding sites demarcate targets for aberrant epigenetic regulation by AML1-ETO in acute myeloid leukemia Live-cell studies of p300/CBP histone acetyltransferase activity and inhibition The epigenetic regulators CBP and p300 facilitate leukemogenesis and represent therapeutic targets in acute myeloid leukemia.An Inv(16)(p13.3q24.3)-encoded CBFA2T3-GLIS2 fusion protein defines an aggressive subtype of pediatric acute megakaryoblastic leukemia.Characterizing the Covalent Targets of a Small Molecule Inhibitor of the Lysine Acetyltransferase P300.Differential role of Id1 in MLL-AF9-driven leukemia based on cell of origin.Supraphysiologic levels of the AML1-ETO isoform AE9a are essential for transformation.Loss of RUNX1/AML1 arginine-methylation impairs peripheral T cell homeostasis GPS-PAIL: prediction of lysine acetyltransferase-specific modification sites from protein sequences.New insights into transcriptional and leukemogenic mechanisms of AML1-ETO and E2A fusion proteins.Heritable Gene Regulation in the CD4:CD8 T Cell Lineage Choice.AML1-ETO driven acute leukemia: insights into pathogenesis and potential therapeutic approaches.Ghrelin O-acyltransferase assays and inhibition.SIAH proteins: critical roles in leukemogenesis.Histone-modifying enzymes: their role in the pathogenesis of acute leukemia and their therapeutic potential.Cancers with wrong HATs: the impact of acetylation.

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P2860

The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.

http://www.wikidata.org/entity/Q35650662

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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2011年论文

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2011年论文

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name

The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.

@ast

The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.

@en

type

label

The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.

@ast

The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.

@en

prefLabel

The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.

@ast

The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.

@en

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SCIENCE.1201662

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The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.

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Alexander Gural

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

Ari Melnick

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

Fan Liu

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

Francesca Voza

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

Gang Huang

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

Haiming Xu

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

Hao Xu

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

Lan Wang

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

Megan A Hatlen

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

Philip A Cole

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

P2860

The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity

Structure of the AML1-ETO eTAFH domain-HEB peptide complex and its contribution to AML1-ETO activity.

Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain

Lysine acetylation targets protein complexes and co-regulates major cellular functions

Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity.

t(8;21)(q22;q22) Fusion proteins preferentially bind to duplicated AML1/RUNX1 DNA-binding sequences to differentially regulate gene expression.

Virtual ligand screening of the p300/CBP histone acetyltransferase: identification of a selective small molecule inhibitor

Interaction and functional cooperation of the leukemia-associated factors AML1 and p300 in myeloid cell differentiation.

Histone deacetylases: a common molecular target for differentiation treatment of acute myeloid leukemias?

E protein silencing by the leukemogenic AML1-ETO fusion protein.

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