Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8.
about
Seed dormancy and germination-emerging mechanisms and new hypothesesChromatin dynamics at DNA replication, transcription and repairWAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcriptionUSP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicingRole of histone H2A ubiquitination in Polycomb silencingThe putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progressionMetabolism, cytoskeleton and cellular signalling in the grip of protein Nepsilon - and O-acetylationHistone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUBUSP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2AA high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complexTrabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chainsCalcium/calmodulin regulates ubiquitination of the ubiquitin-specific protease TRE17/USP6The histone H2B-specific ubiquitin ligase RNF20/hBRE1 acts as a putative tumor suppressor through selective regulation of gene expressionThe U4/U6 recycling factor SART3 has histone chaperone activity and associates with USP15 to regulate H2B deubiquitinationA histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulationThe structural plasticity of SCA7 domains defines their differential nucleosome-binding propertiesHistone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modificationsTFIID and Spt-Ada-Gcn5-acetyltransferase functions probed by genome-wide synthetic genetic array analysis using a Saccharomyces cerevisiae taf9-ts alleleHistone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongationRegulation and cellular roles of ubiquitin-specific deubiquitinating enzymesCatalysis and substrate selection by histone/protein lysine acetyltransferasesRegulation of androgen receptor and histone deacetylase 1 by Mdm2-mediated ubiquitylationWriters, Readers, and Erasers of Histone Ubiquitylation in DNA Double-Strand Break RepairFunctions of Ubiquitin and SUMO in DNA Replication and Replication StressUbiquitin-specific peptidase 22 functions and its involvement in diseaseThe Importance of Ubiquitination and Deubiquitination in Cellular ReprogrammingRole of Deubiquitinating Enzymes in DNA RepairComposition of the SAGA complex in plants and its role in controlling gene expression in response to abiotic stressesFine-tuning the ubiquitin code at DNA double-strand breaks: deubiquitinating enzymes at workFunctional Role of G9a Histone Methyltransferase in CancerRNF20-SNF2H Pathway of Chromatin Relaxation in DNA Double-Strand Break RepairPost-translational modifications of histones that influence nucleosome dynamicsSingle molecule and single cell epigenomics.Structural basis for the interaction between yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex components Sgf11 and Sus1.Structural Insights into the Assembly and Function of the SAGA Deubiquitinating ModuleStructural Basis for Assembly and Activation of the Heterotetrameric SAGA Histone H2B Deubiquitinase ModuleA Role for Intersubunit Interactions in Maintaining SAGA Deubiquitinating Module Structure and ActivityRtf1 is a multifunctional component of the Paf1 complex that regulates gene expression by directing cotranscriptional histone modification.Sgf29p facilitates the recruitment of TATA box binding protein but does not alter SAGA's global structural integrity in vivo.Mutational analysis of the C-terminal FATC domain of Saccharomyces cerevisiae Tra1.
P2860
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P2860
Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8.
description
2003 nî lūn-bûn
@nan
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Transcriptional activation via ...... iated by SAGA-associated Ubp8.
@ast
Transcriptional activation via ...... iated by SAGA-associated Ubp8.
@en
Transcriptional activation via ...... iated by SAGA-associated Ubp8.
@nl
type
label
Transcriptional activation via ...... iated by SAGA-associated Ubp8.
@ast
Transcriptional activation via ...... iated by SAGA-associated Ubp8.
@en
Transcriptional activation via ...... iated by SAGA-associated Ubp8.
@nl
prefLabel
Transcriptional activation via ...... iated by SAGA-associated Ubp8.
@ast
Transcriptional activation via ...... iated by SAGA-associated Ubp8.
@en
Transcriptional activation via ...... iated by SAGA-associated Ubp8.
@nl
P2093
P2860
P3181
P356
P1433
P1476
Transcriptional activation via ...... iated by SAGA-associated Ubp8.
@en
P2093
Anastasia Wyce
Cheng-Fu Kao
Karl W Henry
Laura J Duggan
Lorraine Pillus
Mary Ann Osley
N C Tolga Emre
Wan-Sheng Lo
P2860
P304
P3181
P356
10.1101/GAD.1144003
P407
P577
2003-11-01T00:00:00Z