Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase
about
A novel disrupter of telomere silencing 1-like (DOT1L) interaction is required for signal transducer and activator of transcription 1 (STAT1)-activated gene expressionSinefungin derivatives as inhibitors and structure probes of protein lysine methyltransferase SETD2Linking H3K79 trimethylation to Wnt signaling through a novel Dot1-containing complex (DotCom)The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylationOn the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complexDOT1L/KMT4 recruitment and H3K79 methylation are ubiquitously coupled with gene transcription in mammalian cellsNatural history of S-adenosylmethionine-binding proteinsTargeting histone methylation for cancer therapy: enzymes, inhibitors, biological activity and perspectivesTargeting histone methyltransferases and demethylases in clinical trials for cancer therapyStructural biology and chemistry of protein arginine methyltransferasesSynthesis of lysine methyltransferase inhibitorsStructural and functional coordination of DNA and histone methylationChemical probes of histone lysine methyltransferasesRegulation of αENaC transcriptionStructure and function of dioxygenases in histone demethylation and DNA/RNA demethylationEpigenetics and the control of the collecting duct epithelial sodium channelChemogenetic analysis of human protein methyltransferasesSelective Inhibitors of Histone Methyltransferase DOT1L: Design, Synthesis, and Crystallographic StudiesConformational adaptation drives potent, selective and durable inhibition of the human protein methyltransferase DOT1LCrystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatinRole of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9.The Rtf1 component of the Paf1 transcriptional elongation complex is required for ubiquitination of histone H2B.Histone lysine methyltransferases as anti-cancer targets for drug discoveryA charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new trans-histone pathwayStructure and regulation of the mDot1 gene, a mouse histone H3 methyltransferaseMany paths to methyltransfer: a chronicle of convergenceDiscovery of Novel Dot1L Inhibitors through a Structure-Based Fragmentation ApproachModulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectivesRegulation of the DNA damage response and gene expression by the Dot1L histone methyltransferase and the 53Bp1 tumour suppressorIL-22(+)CD4(+) T cells promote colorectal cancer stemness via STAT3 transcription factor activation and induction of the methyltransferase DOT1LRate of elongation by RNA polymerase II is associated with specific gene features and epigenetic modifications.Histones and their modifications in ovarian cancer - drivers of disease and therapeutic targets.A medicinal chemistry perspective for targeting histone H3 lysine-79 methyltransferase DOT1L.Dot1a contains three nuclear localization signals and regulates the epithelial Na+ channel (ENaC) at multiple levels.Dot1a-AF9 complex mediates histone H3 Lys-79 hypermethylation and repression of ENaCalpha in an aldosterone-sensitive manner.The tale beyond the tail: histone core domain modifications and the regulation of chromatin structureA novel non-SET domain multi-subunit methyltransferase required for sequential nucleosomal histone H3 methylation by the mixed lineage leukemia protein-1 (MLL1) core complexAqp5 is a new transcriptional target of Dot1a and a regulator of Aqp2.Dynamics of histone lysine methylation: structures of methyl writers and erasers
P2860
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P2860
Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Structure of the catalytic dom ...... omal histone methyltransferase
@ast
Structure of the catalytic dom ...... omal histone methyltransferase
@en
Structure of the catalytic dom ...... omal histone methyltransferase
@nl
type
label
Structure of the catalytic dom ...... omal histone methyltransferase
@ast
Structure of the catalytic dom ...... omal histone methyltransferase
@en
Structure of the catalytic dom ...... omal histone methyltransferase
@nl
prefLabel
Structure of the catalytic dom ...... omal histone methyltransferase
@ast
Structure of the catalytic dom ...... omal histone methyltransferase
@en
Structure of the catalytic dom ...... omal histone methyltransferase
@nl
P2093
P3181
P1433
P1476
Structure of the catalytic dom ...... omal histone methyltransferase
@en
P2093
Jinrong Min
Rui-Ming Xu
Zhizhong Li
P304
P3181
P356
10.1016/S0092-8674(03)00114-4
P407
P50
P577
2003-03-01T00:00:00Z