about
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.Insights into newly discovered marks and readers of epigenetic information.Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2.Diverse Activities of Histone Acylations Connect Metabolism to Chromatin Function.KATapulting toward Pluripotency and Cancer.Metabolic regulation of gene expression through histone acylations.The Current State of NAD(+) -Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets.Histone Post-Translational Modifications and Nucleosome Organisation in Transcriptional Regulation: Some Open Questions.Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS DomainReading and Interpreting the Histone Acylation Code.Characterization of histone acylations links chromatin modifications with metabolismYEATS2 links histone acetylation to tumorigenesis of non-small cell lung cancer.Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway.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.Recognition of histone acetylation by the GAS41 YEATS domain promotes H2A.Z deposition in non-small cell lung cancer.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.Global profiling of crotonylation on non-histone proteins.re-TAMD: exploring interactions between H3 peptide and YEATS domain using enhanced sampling.Structure and function of archaeal histonesStructural insights into the π-π-π stacking mechanism and DNA-binding activity of the YEATS domain
P2860
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P2860
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
YEATS2 is a selective histone crotonylation reader.
@en
type
label
YEATS2 is a selective histone crotonylation reader.
@en
prefLabel
YEATS2 is a selective histone crotonylation reader.
@en
P2093
P2860
P356
P1433
P1476
YEATS2 is a selective histone crotonylation reader
@en
P2093
C David Allis
Haipeng Guan
Shuai Zhao
Yingming Zhao
Yuanyuan Li
P2860
P2888
P304
P356
10.1038/CR.2016.49
P577
2016-04-22T00:00:00Z