Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4
about
Diversity in requirement of genetic and epigenetic factors for centromere function in fungiThe unconventional structure of centromeric nucleosomesIdentification of Functionally Conserved Regions in the Structure of the Chaperone/CenH3/H4 ComplexSet2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes.SWI/SNF-like chromatin remodeling factor Fun30 supports point centromere function in S. cerevisiae.SUMO-Targeted Ubiquitin Ligase (STUbL) Slx5 regulates proteolysis of centromeric histone H3 variant Cse4 and prevents its mislocalization to euchromatin.Misregulation of Scm3p/HJURP causes chromosome instability in Saccharomyces cerevisiae and human cells.Assembly of Drosophila centromeric chromatin proteins during mitosisA novel role of the N terminus of budding yeast histone H3 variant Cse4 in ubiquitin-mediated proteolysisLicensing of Centromeric Chromatin Assembly through the Mis18α-Mis18β Heterotetramer.Putting CENP-A in its placeHJURP uses distinct CENP-A surfaces to recognize and to stabilize CENP-A/histone H4 for centromere assembly.The kinetochoreA cooperative mechanism drives budding yeast kinetochore assembly downstream of CENP-A.Centromeres: unique chromatin structures that drive chromosome segregation.The FACT complex interacts with the E3 ubiquitin ligase Psh1 to prevent ectopic localization of CENP-A.The CENP-A nucleosome: a dynamic structure and role at the centromere.Phosphorylation by casein kinase 2 facilitates Psh1 protein-assisted degradation of Cse4 proteinCentromere-like regions in the budding yeast genomeEctopic centromere nucleation by CENP--a in fission yeast.Epigenetic centromere propagation and the nature of CENP-a nucleosomes.Cse4 (CenH3) association with the Saccharomyces cerevisiae plasmid partitioning locus in its native and chromosomally integrated states: implications in centromere evolution.Scm3 is a centromeric nucleosome assembly factorTelomeric repeats facilitate CENP-A(Cnp1) incorporation via telomere binding proteins.The centromere: epigenetic control of chromosome segregation during mitosisKinetochore function and chromosome segregation rely on critical residues in histones H3 and H4 in budding yeast.New clues to understand how CENP-A maintains centromere identity.Histone H3-variant Cse4-induced positive DNA supercoiling in the yeast plasmid has implications for a plasmid origin of a chromosome centromereCENP-A nucleosomes localize to transcription factor hotspots and subtelomeric sites in human cancer cellsDestroying the ring: Freeing DNA from Ku with ubiquitin.Pat1 protects centromere-specific histone H3 variant Cse4 from Psh1-mediated ubiquitinationCentromeric chromatin and the pathway that drives its propagation.Assembly of Drosophila centromeric nucleosomes requires CID dimerizationAssociation of a centromere specific nucleosome with the yeast plasmid partitioning locus: Implications beyond plasmid partitioning.Synergistic Control of Kinetochore Protein Levels by Psh1 and Ubr2.Regulation of Budding Yeast CENP-A levels Prevents Misincorporation at Promoter Nucleosomes and Transcriptional Defects.Protein purification technique that allows detection of sumoylation and ubiquitination of budding yeast kinetochore proteins Ndc10 and Ndc80.Methylation of CenH3 arginine 37 regulates kinetochore integrity and chromosome segregationShaping the landscape: mechanistic consequences of ubiquitin modification of chromatin.Ubiquitin-Activated Interaction Traps (UBAITs) identify E3 ligase binding partners
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P2860
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4
@ast
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4
@en
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4.
@nl
type
label
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4
@ast
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4
@en
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4.
@nl
prefLabel
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4
@ast
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4
@en
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4.
@nl
P2093
P2860
P1433
P1476
Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4
@en
P2093
Geetha Hewawasam
Jennifer L Gerton
Jerry L Workman
Manjunatha Shivaraju
Mark Mattingly
Skylar Martin-Brown
P2860
P304
P356
10.1016/J.MOLCEL.2010.10.014
P407
P5008
P577
2010-11-12T00:00:00Z