Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain (Q27685366)

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English	Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain	scientific article

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scholarly article

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title

Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain (English)

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author name string

Dongxue Yang

series ordinal

1

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Qianglin Fang

series ordinal

2

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Mingzhu Wang

series ordinal

3

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Ren Ren

series ordinal

4

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Hong Wang

series ordinal

5

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Meng He

series ordinal

6

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Youwei Sun

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7

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Na Yang

series ordinal

8

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Rui-Ming Xu

series ordinal

9

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publication date

September 2013

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published in

Nature Structural & Molecular Biology

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volume

20

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issue

9

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page(s)

1116-8

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cites work

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Role of interactions between the origin recognition complex and SIR1 in transcriptional silencing

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21 April 2017

Structure and function of the Saccharomyces cerevisiae Sir3 BAH domain

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Structural Basis of Silencing: Sir3 BAH Domain in Complex with a Nucleosome at 3.0 A Resolution

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21 April 2017

Structure and function of the BAH-containing domain of Orc1p in epigenetic silencing

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21 April 2017

Structural Conservation of Distinctive N-terminal Acetylation-Dependent Interactions across a Family of Mammalian NEDD8 Ligation Enzymes

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21 April 2017

N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex

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21 April 2017

The CCP4 suite: programs for protein crystallography

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21 April 2017

Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions

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

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The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae

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21 April 2017

Spreading of transcriptional repressor SIR3 from telomeric heterochromatin

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21 April 2017

Structural basis for origin recognition complex 1 protein-silence information regulator 1 protein interaction in epigenetic silencing

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21 January 2018

Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing

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21 January 2018

Structure and function of the BAH domain in chromatin biology

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21 January 2018

Steps in assembly of silent chromatin in yeast: Sir3-independent binding of a Sir2/Sir4 complex to silencers and role for Sir2-dependent deacetylation

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21 January 2018

Ordered nucleation and spreading of silenced chromatin in Saccharomyces cerevisiae.

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21 January 2018

Functional characterization of the N terminus of Sir3p

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21 January 2018

Importance of the Sir3 N terminus and its acetylation for yeast transcriptional silencing

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21 January 2018

Mutational analysis of the Sir3 BAH domain reveals multiple points of interaction with nucleosomes.

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21 January 2018

Structure of the Sir3 protein bromo adjacent homology (BAH) domain from S. cerevisiae at 1.95 A resolution

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21 January 2018

Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans

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21 January 2018

Processing of X-ray diffraction data collected in oscillation mode

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reference URL

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retrieved

21 January 2018

Role of the conserved Sir3-BAH domain in nucleosome binding and silent chromatin assembly

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reference URL

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retrieved

31 March 2020

Characterization of nucleosome core particles containing histone proteins made in bacteria

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reference URL

https://api.crossref.org/works/10.1038%2FNSMB.2637

retrieved

31 March 2020

Identifiers

DOI

10.1038/NSMB.2637

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2209860

Dimensions Publication ID

1032245381

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OpenCitations bibliographic resource ID

2209860

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2209860

PubMed publication ID

23934152

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2209860

ResearchGate publication ID

255735185

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