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The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase
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title
The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase
(English)
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author
Tony Kouzarides
series ordinal
9
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Annick Harel-Bellan
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8
object named as
Annick Harel-Bellan
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Olivier Kirsh
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1
object named as
Olivier Kirsh
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Stefan Müller
object named as
Stefan Müller
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5
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Frauke Melchior
object named as
Frauke Melchior
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10
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Eric A Miska
object named as
Eric Miska
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6
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author name string
Jacob-S Seeler
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2
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Andrea Pichler
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3
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Andreas Gast
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4
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Marion Mathieu
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7
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Anne Dejean
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11
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language of work or name
English
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publication date
3 June 2002
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published in
The EMBO Journal
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volume
21
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issue
11
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page(s)
2682-91
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cites work
Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR
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PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
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Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification
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Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization
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Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
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Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway
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SUMO-1 modification activates the transcriptional response of p53
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PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1
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24 March 2017
HDAC4 deacetylase associates with and represses the MEF2 transcription factor
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24 March 2017
MEF-2 function is modified by a novel co-repressor, MITR
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24 March 2017
SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation
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24 March 2017
SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex
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24 March 2017
Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
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24 March 2017
Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
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24 March 2017
A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
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24 March 2017
A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
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Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase
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Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates
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Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease with a role in chromosome condensation regulation
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The nucleoporin RanBP2 has SUMO1 E3 ligase activity
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24 March 2017
An E3-like factor that promotes SUMO conjugation to the yeast septins
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24 March 2017
Induction of apoptosis by protein inhibitor of activated Stat1 through c-Jun NH2-terminal kinase activation
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24 March 2017
Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
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24 March 2017
SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
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24 March 2017
Retinoblastoma protein represses transcription by recruiting a histone deacetylase
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24 March 2017
Retinoblastoma protein recruits histone deacetylase to repress transcription
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PubMed Central
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24 March 2017
Covalent modification of PML by the sentrin family of ubiquitin-like proteins
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=125385
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24 March 2017
Ubch9 conjugates SUMO but not ubiquitin
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=125385
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24 March 2017
The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3
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24 March 2017
SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
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7 April 2017
SUMO--nonclassical ubiquitin
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PubMed Central
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7 April 2017
Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C
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7 April 2017
A new RING for SUMO: wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases
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27 September 2017
SUMO: of branched proteins and nuclear bodies
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27 September 2017
SP-RING for SUMO: new functions bloom for a ubiquitin-like protein
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27 September 2017
SUMO-1 modification required for transformation by adenovirus type 5 early region 1B 55-kDa oncoprotein
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27 September 2017
The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family
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27 September 2017
SUMO, ubiquitin's mysterious cousin
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27 September 2017
Functional significance of histone deacetylase diversity
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27 September 2017
Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1).
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27 September 2017
A functional interaction between dorsal and components of the Smt3 conjugation machinery
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27 September 2017
Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies
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27 September 2017
Critical role for Ser20 of human p53 in the negative regulation of p53 by Mdm2.
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27 September 2017
Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A/B region.
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27 September 2017
Predicting coiled-coil regions in proteins
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30 May 2018
Functional analysis and intracellular localization of p53 modified by SUMO-1.
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29 November 2018
c-Jun and p53 Activity Is Modulated by SUMO-1 Modification
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PubMed
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retrieved
12 December 2020
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inferred from PubMed ID database lookup
Identifiers
DOI
10.1093/EMBOJ/21.11.2682
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2713385
Fatcat ID
release_ubkgbvs5vzftrk2ildsp73zsj4
0 references
OpenCitations bibliographic resource ID
2713385
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2713385
PMC publication ID
125385
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2713385
PubMed publication ID
12032081
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2713385
ResearchGate publication ID
11340597
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