H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1.

about

H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1.

Item

http://www.wikidata.org/entity/Q47139599

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1.

@en

H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1.

@nl

type

Item

label

H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1.

@en

H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1.

@nl

prefLabel

H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1.

@en

H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1.

@nl

P1476

H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1.

@en

P2093

Goran Kungulovski

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

Hong Wu

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

Jinrong Min

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

Judith Stiefelmaier

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

Ludmila Dombrovski

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

Pavel Bashtrykov

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

Peter Loppnau

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

Raluca Tamas

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

Sara Weirich

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

Srikanth Kudithipudi

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

P2860

Ultrafast and memory-efficient alignment of short DNA sequences to the human genome

Model-based analysis of ChIP-Seq (MACS)

Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains.

Tudor, MBT and chromo domains gauge the degree of lysine methylation

The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells

Targeting histone deacetylase complexes via KRAB-zinc finger proteins: the PHD and bromodomains of KAP-1 form a cooperative unit that recruits a novel isoform of the Mi-2alpha subunit of NuRD

Covalent histone modifications--miswritten, misinterpreted and mis-erased in human cancers

Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b

The role of human bromodomains in chromatin biology and gene transcription

P2888

s41467-017-02259-9

P304

2057

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

P31

scholarly article

P356

10.1038/S41467-017-02259-9

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

P407

English

P433

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

P478

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

P50

P577

2017-12-12T00:00:00Z

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

P698

29234025

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

P932

5727127

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