Evidence that a complex of SIR proteins interacts with the silencer and telomere-binding protein RAP1.
about
Shelterin-like proteins and Yku inhibit nucleolytic processing of Saccharomyces cerevisiae telomeresStructural basis of selective ubiquitination of TRF1 by SCFFbx4The human Rap1 protein complex and modulation of telomere lengthComponents of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing.Chromatin affinity-precipitation using a small metabolic molecule: its application to analysis of O-acetyl-ADP-riboseCharacterization of the yeast telomere nucleoprotein core: Rap1 binds independently to each recognition siteFunctional proteomics establishes the interaction of SIRT7 with chromatin remodeling complexes and expands its role in regulation of RNA polymerase I transcriptionIsolation of a SIR-like gene, SIR-T8, that is overexpressed in thyroid carcinoma cell lines and tissuesLysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein associationThe many faces of histone H3K79 methylationLinking replication stress with heterochromatin formationStructural and Functional Studies of the Rap1 C-Terminus Reveal Novel Separation-of-Function MutantsStn1-Ten1 is an Rpa2-Rpa3-like complex at telomeresStructural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase αA conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organismsStructural basis for the role of the Sir3 AAA+ domain in silencing: interaction with Sir4 and unmethylated histone H3K79Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formationStructural basis for allosteric stimulation of Sir2 activity by Sir4 bindingThe orientation of the C-terminal domain of the Saccharomyces cerevisiae Rap1 protein is determined by its binding to DNAHeterochromatin protein Sir3 induces contacts between the amino terminus of histone H4 and nucleosomal DNAThe Saccharomyces cerevisiae suppressor of choline sensitivity (SCS2) gene is a multicopy Suppressor of mec1 telomeric silencing defectsRegulating repression: roles for the sir4 N-terminus in linker DNA protection and stabilization of epigenetic statesLocalization of Sir2p: the nucleolus as a compartment for silent information regulatorsIdentification of a member of a DNA-dependent ATPase family that causes interference with silencing.The Ku complex in silencing the cryptic mating-type loci of Saccharomyces cerevisiae.Mcm10 is required for the maintenance of transcriptional silencing in Saccharomyces cerevisiae.Functional differences and interactions among the putative RecA homologs Rad51, Rad55, and Rad57.DOT4 links silencing and cell growth in Saccharomyces cerevisiaeA class of single-stranded telomeric DNA-binding proteins required for Rap1p localization in yeast nuclei.Separation-of-function mutants of yeast Ku80 reveal a Yku80p-Sir4p interaction involved in telomeric silencing.Multiple interactions in Sir protein recruitment by Rap1p at silencers and telomeres in yeast.Mcm10 mediates the interaction between DNA replication and silencing machineriesRestoration of silencing in Saccharomyces cerevisiae by tethering of a novel Sir2-interacting protein, Esc8.A protein-counting mechanism for telomere length regulation in yeast.Sir proteins, Rif proteins, and Cdc13p bind Saccharomyces telomeres in vivo.Rap1p and other transcriptional regulators can function in defining distinct domains of gene expression.Silent information regulator protein complexes in Saccharomyces cerevisiae: a SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3.Hir1p and Hir2p function as transcriptional corepressors to regulate histone gene transcription in the Saccharomyces cerevisiae cell cycle.A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2BThe yeast RNA polymerase II-associated factor Iwr1p is involved in the basal and regulated transcription of specific genes.
P2860
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P2860
Evidence that a complex of SIR proteins interacts with the silencer and telomere-binding protein RAP1.
description
1994 nî lūn-bûn
@nan
1994 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Evidence that a complex of SIR ...... telomere-binding protein RAP1.
@ast
Evidence that a complex of SIR ...... telomere-binding protein RAP1.
@en
Evidence that a complex of SIR ...... telomere-binding protein RAP1.
@nl
type
label
Evidence that a complex of SIR ...... telomere-binding protein RAP1.
@ast
Evidence that a complex of SIR ...... telomere-binding protein RAP1.
@en
Evidence that a complex of SIR ...... telomere-binding protein RAP1.
@nl
prefLabel
Evidence that a complex of SIR ...... telomere-binding protein RAP1.
@ast
Evidence that a complex of SIR ...... telomere-binding protein RAP1.
@en
Evidence that a complex of SIR ...... telomere-binding protein RAP1.
@nl
P2093
P3181
P356
P1433
P1476
Evidence that a complex of SIR ...... telomere-binding protein RAP1.
@en
P2093
P304
P3181
P356
10.1101/GAD.8.19.2257
P407
P577
1994-10-01T00:00:00Z