Four domains of Ada1 form a heterochromatin boundary through different mechanisms.

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Four domains of Ada1 form a heterochromatin boundary through different mechanisms.

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年學術文章

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2016年學術文章

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Four domains of Ada1 form a heterochromatin boundary through different mechanisms.

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Four domains of Ada1 form a heterochromatin boundary through different mechanisms.

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Four domains of Ada1 form a heterochromatin boundary through different mechanisms.

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Four domains of Ada1 form a heterochromatin boundary through different mechanisms.

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Four domains of Ada1 form a heterochromatin boundary through different mechanisms.

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Four domains of Ada1 form a heterochromatin boundary through different mechanisms.

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P1476

Four domains of Ada1 form a heterochromatin boundary through different mechanisms.

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P2093

Hiroyuki Uchida

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

Kaori Shinmyozu

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

Kazuma Kamata

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

Masanori Hatashita

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

Masaya Oki

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

P2860

Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo

Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.

Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein

RNA polymerase III and RNA polymerase II promoter complexes are heterochromatin barriers in Saccharomyces cerevisiae

The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs

Single cell visualization of yeast gene expression shows correlation of epigenetic switching between multiple heterochromatic regions through multiple generations

Proteasome subunit Rpn13 is a novel ubiquitin receptor

The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix

Blm10 binds to pre-activated proteasome core particles with open gate conformation.

Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction.

P304

1125-1136

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P31

scholarly article

P356

10.1111/GTC.12421

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P433

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

P478

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

P50

Jun-Ichi Nakayama

P577

2016-09-20T00:00:00Z

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P698

27647735

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