MBD5 and MBD6 interact with the human PR-DUB complex through their methyl-CpG-binding domain.
about
Towards elucidating the stability, dynamics and architecture of the nucleosome remodeling and deacetylase complex by using quantitative interaction proteomicsModifiers and Readers of DNA Modifications and Their Impact on Genome Structure, Expression, and Stability in DiseaseMBD2 and MBD3: elusive functions and mechanismsGenome-wide binding studies reveal DNA binding specificity mechanisms and functional interplay amongst Forkhead transcription factorsMolecular architecture of polycomb repressive complexesThe forkhead transcription factor FOXK2 acts as a chromatin targeting factor for the BAP1-containing histone deubiquitinase complexAn epigenetic regulator: methyl-CpG-binding domain protein 1 (MBD1).Drosophila Cyclin G and epigenetic maintenance of gene expression during developmentThe dynamic interactome and genomic targets of Polycomb complexes during stem-cell differentiationMethyl-CpG-binding domain proteins: readers of the epigenome.Methyl-CpG-Binding Protein (MBD) Family: Epigenomic Read-Outs Functions and Roles in Tumorigenesis and Psychiatric Diseases.Forkhead box K2 modulates epirubicin and paclitaxel sensitivity through FOXO3a in breast cancer.Epigenetic Regulation.Unfolding the pathogenesis of scleroderma through genomics and epigenomics.BAP1/ASXL1 recruitment and activation for H2A deubiquitination.Proteins That Read DNA Methylation.Modulating BAP1 expression affects ROS homeostasis, cell motility and mitochondrial function.Ubiquitin recognition of BAP1: understanding its enzymatic function.Stabilization of the methyl-CpG binding protein ZBTB38 by the deubiquitinase USP9X limits the occurrence and toxicity of oxidative stress in human cells.DNA Methylation and Adult Neurogenesis.BAP1 links metabolic regulation of ferroptosis to tumour suppressionA bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes
P2860
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P2860
MBD5 and MBD6 interact with the human PR-DUB complex through their methyl-CpG-binding domain.
description
2014 nî lūn-bûn
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2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
@zh-my
2014年学术文章
@zh-sg
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name
MBD5 and MBD6 interact with th ...... eir methyl-CpG-binding domain.
@en
MBD5 and MBD6 interact with th ...... eir methyl-CpG-binding domain.
@nl
type
label
MBD5 and MBD6 interact with th ...... eir methyl-CpG-binding domain.
@en
MBD5 and MBD6 interact with th ...... eir methyl-CpG-binding domain.
@nl
prefLabel
MBD5 and MBD6 interact with th ...... eir methyl-CpG-binding domain.
@en
MBD5 and MBD6 interact with th ...... eir methyl-CpG-binding domain.
@nl
P2093
P2860
P50
P356
P1433
P1476
MBD5 and MBD6 interact with th ...... eir methyl-CpG-binding domain.
@en
P2093
Alexandra Fournier
Andrew Sharrocks
Anneloes Mensinga
Laure Ferry
Pascal W T C Jansen
Sophie Laget
Zongling Ji
P2860
P304
P356
10.1002/PMIC.201400013
P577
2014-04-24T00:00:00Z