Structure of the Catalytic Domain of EZH2 Reveals Conformational Plasticity in Cofactor and Substrate Binding Sites and Explains Oncogenic Mutations
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Targeting histone methyltransferases and demethylases in clinical trials for cancer therapyLong Noncoding RNAs as Novel Biomarkers Have a Promising Future in Cancer DiagnosticsHOTAIR: an oncogenic long non-coding RNA in different cancersGain-of-function mutation of chromatin regulators as a tumorigenic mechanism and an opportunity for therapeutic interventionPolycomb repressive complex 2 structure with inhibitor reveals a mechanism of activation and drug resistance.Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2Targeting activating mutations of EZH2 leads to potent cell growth inhibition in human melanoma by derepression of tumor suppressor genesHistone lysine methyltransferases as anti-cancer targets for drug discoveryMolecular architecture of polycomb repressive complexesHistone deacetylase inhibition modulates histone acetylation at gene promoter regions and affects genome-wide gene transcription in Schistosoma mansoniIdentification of (R)-N-((4-Methoxy-6-methyl-2-oxo-1,2-dihydropyridin-3-yl)methyl)-2-methyl-1-(1-(1-(2,2,2-trifluoroethyl)piperidin-4-yl)ethyl)-1H-indole-3-carboxamide (CPI-1205), a Potent and Selective Inhibitor of Histone Methyltransferase EZH2, SComprehensive mutational profiling of core binding factor acute myeloid leukemia.Selective inhibition of EZH2 and EZH1 enzymatic activity by a small molecule suppresses MLL-rearranged leukemiaStructural insights into binding of small molecule inhibitors to Enhancer of Zeste Homolog 2.The Human Mixed Lineage Leukemia 5 (MLL5), a Sequentially and Structurally Divergent SET Domain-Containing Protein with No Intrinsic Catalytic Activity.Discovery and Molecular Basis of a Diverse Set of Polycomb Repressive Complex 2 Inhibitors Recognition by EED.Targeting EZH2 and PRC2 dependence as novel anticancer therapy.Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2.Structural analysis of an active fungal PRC2.EZH2: an emerging role in melanoma biology and strategies for targeted therapy.Acquisition of a single EZH2 D1 domain mutation confers acquired resistance to EZH2-targeted inhibitors.Polycomb repressive complex 2 in an autoinhibited state.Role of the Polycomb Repressive Complex 2 (PRC2) in Transcriptional Regulation and Cancer.Maintaining cell identity: PRC2-mediated regulation of transcription and cancer.Comment on "Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2".Role of the long non-coding RNA HOTAIR in hepatocellular carcinoma.Evolving Catalytic Properties of the MLL Family SET Domain.Structure-Activity Relationship Studies for Enhancer of Zeste Homologue 2 (EZH2) and Enhancer of Zeste Homologue 1 (EZH1) Inhibitors.MUC1-C activates EZH2 expression and function in human cancer cells.Mrg15 stimulates Ash1 H3K36 methyltransferase activity and facilitates Ash1 Trithorax group protein function in Drosophila.Structure, mechanism, and regulation of polycomb repressive complex 2.Apollo-NADP(+): a spectrally tunable family of genetically encoded sensors for NADP(+).STRUCTURAL BIOLOGY. Chromatin complex, crystal clear.Combined HAT/EZH2 modulation leads to cancer-selective cell death.An Evolutionarily Conserved Structural Platform for PRC2 Inhibition by a Class of Ezh2 Inhibitors.Roles of H3K36-specific histone methyltransferases in transcription: antagonizing silencing and safeguarding transcription fidelity
P2860
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P2860
Structure of the Catalytic Domain of EZH2 Reveals Conformational Plasticity in Cofactor and Substrate Binding Sites and Explains Oncogenic Mutations
description
2013 nî lūn-bûn
@nan
2013 թուականին հրատարակուած գիտական յօդուած
@hyw
2013 թվականին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Structure of the Catalytic Dom ...... d Explains Oncogenic Mutations
@ast
Structure of the Catalytic Dom ...... d Explains Oncogenic Mutations
@en
Structure of the Catalytic Dom ...... d Explains Oncogenic Mutations
@nl
type
label
Structure of the Catalytic Dom ...... d Explains Oncogenic Mutations
@ast
Structure of the Catalytic Dom ...... d Explains Oncogenic Mutations
@en
Structure of the Catalytic Dom ...... d Explains Oncogenic Mutations
@nl
prefLabel
Structure of the Catalytic Dom ...... d Explains Oncogenic Mutations
@ast
Structure of the Catalytic Dom ...... d Explains Oncogenic Mutations
@en
Structure of the Catalytic Dom ...... d Explains Oncogenic Mutations
@nl
P2093
P2860
P50
P3181
P1433
P1476
Structure of the Catalytic Dom ...... d Explains Oncogenic Mutations
@en
P2093
Aiping Dong
Alma Seitova
Fengling Li
Shili Duan
P2860
P304
P3181
P356
10.1371/JOURNAL.PONE.0083737
P407
P577
2013-01-01T00:00:00Z