about
SUMO modification of the Ets-related transcription factor ERM inhibits its transcriptional activityArsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodiesDistinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomicsPosttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)Ribosomal proteins are targets for the NEDD8 pathwayRNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradationSingle-stranded DNA-binding protein hSSB1 is critical for genomic stabilitySIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1SUMO-1 modification of human transcription factor (TF) IID complex subunits: inhibition of TFIID promoter-binding activity through SUMO-1 modification of hsTAF5Purification and identification of endogenous polySUMO conjugatesStructural basis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme NEDP1.SUMO-1 modification activates the transcriptional response of p53The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processingSUMO protease SENP1 induces isomerization of the scissile peptide bondStructure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysisMechanism of ubiquitylation by dimeric RING ligase RNF4Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.Role of two residues proximal to the active site of Ubc9 in substrate recognition by the Ubc9.SUMO-1 thiolester complex.System-wide changes to SUMO modifications in response to heat shock.Post-translational modification by SUMO.Comparative proteomic analysis identifies a role for SUMO in protein quality control.betaTrCP-mediated proteolysis of NF-kappaB1 p105 requires phosphorylation of p105 serines 927 and 932.Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selectionRole of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugationNEDP1, a highly conserved cysteine protease that deNEDDylates CullinsSUMO: a history of modificationIn vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategyOMERO: flexible, model-driven data management for experimental biologyA proteomic study of SUMO-2 target proteinsMdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activityA mechanism for inhibiting the SUMO pathwaySUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damageSUMO and transcriptional regulationSUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targetingDynamic SUMO modification regulates mitotic chromosome assembly and cell cycle progression in Caenorhabditis elegans.Identification of sites of ubiquitination in proteins: a fourier transform ion cyclotron resonance mass spectrometry approach.Mutations in the IkBa gene in Hodgkin's disease suggest a tumour suppressor role for IkappaBalpha.Family-wide analysis of poly(ADP-ribose) polymerase activityAndrogen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function.
P50
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P50
description
moleculair bioloog
@nl
molecular biologist
@en
name
Ronald Hay
@ast
Ronald Hay
@en
Ronald Hay
@es
Ronald Hay
@fr
Ronald Hay
@nl
type
label
Ronald Hay
@ast
Ronald Hay
@en
Ronald Hay
@es
Ronald Hay
@fr
Ronald Hay
@nl
altLabel
Ron Hay
@en
Ronald Thomas Hay
@en
prefLabel
Ronald Hay
@ast
Ronald Hay
@en
Ronald Hay
@es
Ronald Hay
@fr
Ronald Hay
@nl
P166
P1053
F-9338-2011
P1153
7202248496
P2070
ronald-hay-11600
P21
P31
P3829
P496
0000-0001-7113-9024
P5463
Hay_Ronald_Thomas
P569
2000-01-01T00:00:00Z