The CW domain, a new histone recognition module in chromatin proteins
about
Structure-function analysis reveals a novel mechanism for regulation of histone demethylase LSD2/AOF1/KDM1bPRC1 is taking the lead in PcG repressionHistone methylation: a dynamic mark in health, disease and inheritanceQuantitative proteomic analysis of histone modificationsPhylogenetic analysis and classification of the Brassica rapa SET-domain protein family.A novel HSI2 mutation in Arabidopsis affects the PHD-like domain and leads to derepression of seed-specific gene expression.A chromatin modifying enzyme, SDG8, is involved in morphological, gene expression, and epigenetic responses to mechanical stimulation.Regulation of the seed to seedling developmental phase transition by the LAFL and VAL transcription factor networks.Regulation of arabidopsis flowering by the histone mark readers MRG1/2 via interaction with CONSTANS to modulate FT expression.HSI2/VAL1 PHD-like domain promotes H3K27 trimethylation to repress the expression of seed maturation genes and complex transgenes in Arabidopsis seedlings.Family-wide Characterization of Histone Binding Abilities of Human CW Domain-containing ProteinsThe MORC family: new epigenetic regulators of transcription and DNA damage response.Mouse MORC3 is a GHKL ATPase that localizes to H3K4me3 marked chromatin.Propagation of histone marks and epigenetic memory during normal and interrupted DNA replication.Epigenetics meets mathematics: towards a quantitative understanding of chromatin biology.H3K36 methylation is critical for brassinosteroid-regulated plant growth and development in rice.Structural insight into inhibitors of flavin adenine dinucleotide-dependent lysine demethylases.MORC3, a Component of PML Nuclear Bodies, Has a Role in Restricting Herpes Simplex Virus 1 and Human Cytomegalovirus.Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions.MORC proteins and epigenetic regulation.The histone methyltransferase SDG8 mediates the epigenetic modification of light and carbon responsive genes in plants.The many faces of plant chromatin: Meeting summary of the 4th European workshop on plant chromatin 2015, Uppsala, SwedenMORC Proteins: Novel Players in Plant and Animal Health.HISTONE DEACETYLASE19 interacts with HSL1 and participates in the repression of seed maturation genes in Arabidopsis seedlings.Potential targets of VIVIPAROUS1/ABI3-LIKE1 (VAL1) repression in developing Arabidopsis thaliana embryos.H3K23me1 is an evolutionarily conserved histone modification associated with CG DNA methylation in Arabidopsis.Structure and mechanism of plant histone mark readers.A cis cold memory element and a trans epigenome reader mediate Polycomb silencing of FLC by vernalization in Arabidopsis.Oslo Epigenetics Symposium 2012. Oslo, Norway, 8-9 November 2012.HSI2/VAL1 Silences AGL15 to Regulate the Developmental Transition from Seed Maturation to Vegetative Growth in Arabidopsis.[Reciprocity between active transcription and histone methylation].MORF-RELATED GENE702, a Reader Protein of Trimethylated Histone H3 Lysine 4 and Histone H3 Lysine 36, Is Involved in Brassinosteroid-Regulated Growth and Flowering Time Control in Rice.HSI2 Repressor Recruits MED13 and HDA6 to Down-Regulate Seed Maturation Gene Expression Directly During Arabidopsis Early Seedling Growth.Uncovering the mechanistic basis for specific recognition of monomethylated H3K4 by the CW domain of Arabidopsis histone methyltransferase SDG8.Position-specific intron retention is mediated by the histone methyltransferase SDG725.KDM1A microenvironment, its oncogenic potential, and therapeutic significance.Prominent role of histone lysine demethylases in cancer epigenetics and therapyA fruitful chromatin harvest: Meeting summary of the Second European Workshop on Plant Chromatin 2011 in Versailles, FranceChromatin-Based Regulation of Plant Root DevelopmentZmMBD101 is a DNA-binding protein that maintains Mutator elements chromatin in a repressive state in maize
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P2860
The CW domain, a new histone recognition module in chromatin proteins
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
The CW domain, a new histone recognition module in chromatin proteins
@ast
The CW domain, a new histone recognition module in chromatin proteins
@en
The CW domain, a new histone recognition module in chromatin proteins
@nl
type
label
The CW domain, a new histone recognition module in chromatin proteins
@ast
The CW domain, a new histone recognition module in chromatin proteins
@en
The CW domain, a new histone recognition module in chromatin proteins
@nl
prefLabel
The CW domain, a new histone recognition module in chromatin proteins
@ast
The CW domain, a new histone recognition module in chromatin proteins
@en
The CW domain, a new histone recognition module in chromatin proteins
@nl
P2093
P2860
P356
P1433
P1476
The CW domain, a new histone recognition module in chromatin proteins
@en
P2093
Kenneth Finne
Per Eugen Kristiansen
Reidunn B Aalen
Rein Aasland
Silje Veie Veiseth
Verena Hoppmann
P2860
P304
P356
10.1038/EMBOJ.2011.108
P407
P577
2011-04-26T00:00:00Z