Structural basis for the role of the Sir3 AAA+ domain in silencing: interaction with Sir4 and unmethylated histone H3K79
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Structural Basis of Silencing: Sir3 BAH Domain in Complex with a Nucleosome at 3.0 A ResolutionDimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formationHeterochromatin protein Sir3 induces contacts between the amino terminus of histone H4 and nucleosomal DNAThe N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particleRegulating repression: roles for the sir4 N-terminus in linker DNA protection and stabilization of epigenetic statesThe Nuts and Bolts of Transcriptionally Silent Chromatin in Saccharomyces cerevisiae.A D53 repression motif induces oligomerization of TOPLESS corepressors and promotes assembly of a corepressor-nucleosome complex.Epigenetics in Saccharomyces cerevisiae.Direct interactions promote eviction of the Sir3 heterochromatin protein by the SWI/SNF chromatin remodeling enzyme.Cooperative stabilization of the SIR complex provides robust epigenetic memory in a model of SIR silencing in Saccharomyces cerevisiae.Mechanism for epigenetic variegation of gene expression at yeast telomeric heterochromatinThe origin recognition complex: a biochemical and structural view.Changes in the genome-wide localization pattern of Sir3 in Saccharomyces cerevisiae during different growth stages.Getting down to the core of histone modifications.Heterochromatin structure: lessons from the budding yeast.The Yeast Heterochromatin Protein Sir3 Experienced Functional Changes in the AAA+ Domain After Gene Duplication and Subfunctionalization.The upstreams and downstreams of H3K79 methylation by DOT1L.Variants of the Sir4 Coiled-Coil Domain Improve Binding to Sir3 for Heterochromatin Formation in Saccharomyces cerevisiae.Heterochromatin assembly by interrupted Sir3 bridges across neighboring nucleosomes.Detection of an altered heterochromatin structure in the absence of the nucleotide excision repair protein Rad4 in Saccharomyces cerevisiae.Sir3 Polymorphisms in Candida glabrata clinical isolates.Recruitment and allosteric stimulation of a histone deubiquitinating enzyme during heterochromatin assembly.The interplay of histone H2B ubiquitination with budding and fission yeast heterochromatin.Yeast heterochromatin regulators Sir2 and Sir3 act directly at euchromatic DNA replication origins.
P2860
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P2860
Structural basis for the role of the Sir3 AAA+ domain in silencing: interaction with Sir4 and unmethylated histone H3K79
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2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年論文
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2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
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name
Structural basis for the role ...... and unmethylated histone H3K79
@ast
Structural basis for the role ...... and unmethylated histone H3K79
@en
Structural basis for the role ...... and unmethylated histone H3K79
@nl
type
label
Structural basis for the role ...... and unmethylated histone H3K79
@ast
Structural basis for the role ...... and unmethylated histone H3K79
@en
Structural basis for the role ...... and unmethylated histone H3K79
@nl
prefLabel
Structural basis for the role ...... and unmethylated histone H3K79
@ast
Structural basis for the role ...... and unmethylated histone H3K79
@en
Structural basis for the role ...... and unmethylated histone H3K79
@nl
P2093
P2860
P50
P3181
P356
P1433
P1476
Structural basis for the role ...... and unmethylated histone H3K79
@en
P2093
Ann E Ehrenhofer-Murray
Jan M Weber
Mariano Oppikofer
Stefan Ehrentraut
Stephanie Kueng
P2860
P304
P3181
P356
10.1101/GAD.17175111
P577
2011-09-01T00:00:00Z