The Taf14 YEATS domain is a reader of histone crotonylation. - Test2 - elhamkhani - TriplyDB

The Taf14 YEATS domain is a reader of histone crotonylation.

The Taf14 YEATS domain is a reader of histone crotonylation.

http://www.wikidata.org/entity/Q34522555

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YEATS domain: Linking histone crotonylation to gene regulation.MOF as an evolutionarily conserved histone crotonyltransferase and transcriptional activation by histone acetyltransferase-deficient and crotonyltransferase-competent CBP/p300.First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum.A meta-analysis reveals complex regulatory properties at Taf14-repressed genes.Insights into newly discovered marks and readers of epigenetic information.Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2.Transcription control by the ENL YEATS domain in acute leukaemia Selective targeting of epigenetic reader domains.Diverse Activities of Histone Acylations Connect Metabolism to Chromatin Function.Metabolic regulation of gene expression through histone acylations.Histone Post-Translational Modifications and Nucleosome Organisation in Transcriptional Regulation: Some Open Questions.Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain Expanding the Reader Landscape of Histone Acylation.Acetylation- and Methylation-Related Epigenetic Proteins in the Context of Their Targets.Reading and Interpreting the Histone Acylation Code.The C Terminus of the RNA Polymerase II Transcription Factor IID (TFIID) Subunit Taf2 Mediates Stable Association of Subunit Taf14 into the Yeast TFIID Complex.Characterization of histone acylations links chromatin modifications with metabolism YEATS2 links histone acetylation to tumorigenesis of non-small cell lung cancer.Loss of Snf5 Induces Formation of an Aberrant SWI/SNF Complex.H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1.Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway.Structure of p300 in complex with acyl-CoA variants.Microbiota derived short chain fatty acids promote histone crotonylation in the colon through histone deacetylases.Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain.Identification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation.HIV latency is reversed by ACSS2-driven histone crotonylation.Histone Marks in the 'Driver's Seat': Functional Roles in Steering the Transcription Cycle.Recognition of Histone H3K14 Acylation by MORF.Class I histone deacetylases are major histone decrotonylases: evidence for critical and broad function of histone crotonylation in transcription.Histone H3K4 and H3K36 Methylation Independently Recruit the NuA3 Histone Acetyltransferase in Saccharomyces cerevisiae.The INO80 remodeller in transcription, replication and repair.Bioorthogonal pro-metabolites for profiling short chain fatty acylation.Structure and function of archaeal histones Structural insights into the π-π-π stacking mechanism and DNA-binding activity of the YEATS domain

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P2860

The Taf14 YEATS domain is a reader of histone crotonylation.

http://www.wikidata.org/entity/Q34522555

description

2016 nî lūn-bûn

@nan

2016 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի ապրիլին հրատարակված գիտական հոդված

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2016年の論文

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2016年論文

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2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

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2016年论文

@wuu

name

The Taf14 YEATS domain is a reader of histone crotonylation.

@ast

The Taf14 YEATS domain is a reader of histone crotonylation.

@en

The Taf14 YEATS domain is a reader of histone crotonylation.

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type

label

The Taf14 YEATS domain is a reader of histone crotonylation.

@ast

The Taf14 YEATS domain is a reader of histone crotonylation.

@en

The Taf14 YEATS domain is a reader of histone crotonylation.

@nl

prefLabel

The Taf14 YEATS domain is a reader of histone crotonylation.

@ast

The Taf14 YEATS domain is a reader of histone crotonylation.

@en

The Taf14 YEATS domain is a reader of histone crotonylation.

@nl

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Nature Chemical Biology

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The Taf14 YEATS domain is a reader of histone crotonylation.

@en

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Erin K Shanle

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

Forest H Andrews

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

Ian K Tsun

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

Joseph B Bridgers

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Histone recognition and large-scale structural analysis of the human bromodomain family

Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Protein lysine acylation and cysteine succination by intermediates of energy metabolism

Molecular basis for chromatin binding and regulation of MLL5

A Subset of Human Bromodomains Recognizes Butyryllysine and Crotonyllysine Histone Peptide Modifications

Phasercrystallographic software

Features and development of Coot

The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex.

Anc1 interacts with the catalytic subunits of the general transcription factors TFIID and TFIIF, the chromatin remodeling complexes RSC and INO80, and the histone acetyltransferase complex NuA3.

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396-398

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10.1038/NCHEMBIO.2065

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6

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12

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

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Stephen A Shinsky

Krzysztof Krajewski

Tatiana G Kutateladze

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2016-04-18T00:00:00Z

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27089029

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4871749

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