about
A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencingAtaxin-7 is a subunit of GCN5 histone acetyltransferase-containing complexesThe structural plasticity of SCA7 domains defines their differential nucleosome-binding propertiesLessons from genome-wide studies: an integrated definition of the coactivator function of histone acetyl transferasesClinical, molecular, and genotype-phenotype correlation studies from 25 cases of oral-facial-digital syndrome type 1: a French and Belgian collaborative studyGlutamine-expanded ataxin-7 alters TFTC/STAGA recruitment and chromatin structure leading to photoreceptor dysfunction.SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexesCellular localization of the Huntington's disease protein and discrimination of the normal and mutated formGcn5 and SAGA regulate shelterin protein turnover and telomere maintenance.In vivo chromatin organization of mouse rod photoreceptors correlates with histone modificationsThe tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elementsThe SAGA coactivator complex acts on the whole transcribed genome and is required for RNA polymerase II transcription.The human TREX-2 complex is stably associated with the nuclear pore basket.H2B mono-ubiquitylation facilitates fork stalling and recovery during replication stress by coordinating Rad53 activation and chromatin assembly.Transcriptional alterations and chromatin remodeling in polyglutamine diseases.DNA binding by Sgf11 protein affects histone H2B deubiquitination by Spt-Ada-Gcn5-acetyltransferase (SAGA).Histone H2B ubiquitination: signaling not scrapping.Xq28 duplication including MECP2 in six unreported affected females: what can we learn for diagnosis and genetic counselling?Progressive retinal degeneration and dysfunction in R6 Huntington's disease mice.Hsp70 and Hsp40 chaperones do not modulate retinal phenotype in SCA7 mice.Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions.Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms.Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias.Polyglutamine expansion induces a protein-damaging stress connecting heat shock protein 70 to the JNK pathway.Disease progression despite early loss of polyglutamine protein expression in SCA7 mouse model.Differential distribution of the normal and mutated forms of huntingtin in the human brain.Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID.Deciphering the causes of sporadic late-onset cerebellar ataxias: a prospective study with implications for diagnostic work.Zinc-finger UBPs: regulators of deubiquitylation.Hereditary systemic angiopathy (HSA) with cerebral calcifications, retinopathy, progressive nephropathy, and hepatopathy.Polyglutamine expansion causes neurodegeneration by altering the neuronal differentiation program.SAGA Is a General Cofactor for RNA Polymerase II Transcription.Transcription of Nearly All Yeast RNA Polymerase II-Transcribed Genes Is Dependent on Transcription Factor TFIID.Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions.Rapid antibody test for fragile X syndrome.Homozygous TAF8 mutation in a patient with intellectual disability results in undetectable TAF8 protein, but preserved RNA Polymerase II transcription.LBR and lamin A/C sequentially tether peripheral heterochromatin and inversely regulate differentiation.Mediator is essential for small nuclear and nucleolar RNA transcription in yeastJuvenile Huntington disease in an 18-month-old boy revealed by global developmental delay and reduced cerebellar volumeARX polyalanine expansions are highly implicated in familial cases of mental retardation with infantile epilepsy and/or hand dystonia
P50
Q24307408-399D2F50-57B3-414F-9664-D72D466EAFBDQ24338317-6C0DF5EA-2CFC-4E01-A99A-A850E5572829Q24338865-67A38697-3383-472B-AF5A-366B1D3AF7B9Q24616312-C9131F29-75D1-403C-B739-9D443CC882C6Q24655227-AB512A1B-49A6-4E0A-8A80-51716437EFA3Q25256616-717AA0C9-45F5-4014-A371-B9266EFB7A94Q28306460-3B1FCB86-0D79-486B-B2F8-B723CF5A94B3Q28509836-6A0A640D-C10C-4EBA-B2BF-F62BB236BBFDQ33493740-6DE1C9D9-18F6-4D0F-88DF-08864F77ABA9Q33603017-CF5D2AE4-F997-4C62-A176-AFA335E6EE13Q34199540-87C1D1DC-5D74-4979-AD98-0F6EFC6F9C01Q34235677-1DCB7206-F361-4274-AA0E-B3E862996180Q34339638-5B1A8CAB-8678-4AF4-A285-66AF1E054E61Q35294605-D6379CBC-2DE7-46CB-A0CD-09CCFE484B7AQ36566966-663408A6-C762-4E1B-8030-2EC67104CE09Q37691637-8E6CAD28-554D-4FA1-97F7-DB3A361B2CC6Q38229848-0B53CF40-602F-4F2A-BD4A-95102D5E1456Q38985861-906ED63A-4D4B-4A60-9402-13E2FCEFA60BQ39063165-972A734F-5B69-4AFE-BB3A-8BB88A6ACEE1Q40502075-91D69280-AFE3-4D7A-81A2-FB21D3270864Q40709427-7EF751D8-D05D-4A73-8AF5-097217A72154Q41249427-3F89E388-5839-407C-BA39-08DF88DE44CDQ41269608-7C5C00A3-A1C3-443C-AB96-6CC11F7CEB96Q44323344-1E542AB1-F8F0-42A3-986D-5C99BBAF5F0BQ44777520-238275D4-E583-4688-9EA6-6B3EE24B320EQ45295367-901257E1-9C06-407D-A4E1-FC84555FDA8BQ45373088-18BBCF8F-D2E9-417F-BDB6-04FD4F7BED13Q46512356-EC5EAF06-B419-455A-9D05-BE0CBC661B7EQ46728959-16009744-56DD-4EA5-8996-7A114425C704Q46801611-0B917F90-7500-4FD9-B281-536138B0E888Q46909987-352E14E1-06F4-4D56-99A0-A649138509C9Q47790116-00A2D861-0078-433C-9B0B-118723E9DE0AQ47790162-4505CBEC-7990-4BCC-ACA5-30892CC3F22BQ48373564-79392C87-3CFB-415A-92A0-B1D64EF7687BQ52016309-1B97D5A1-010B-4FFB-84A9-06208728FD1BQ52323784-13A6FBFC-1A7A-4109-977E-7DE37EA9D5DDQ52633974-59239BE1-8C2F-4C4A-AC19-61CCAFB5E1FFQ57059661-38D4A32C-1B0E-47D6-8E10-771E3F3E4F0CQ57083854-EB49A691-236C-46E1-AB6F-6A925B639DBCQ57387330-6677FF89-A78A-42D3-BF6B-CBDEA37C9A12
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Didier Devys
@ast
Didier Devys
@en
Didier Devys
@es
Didier Devys
@nl
Didier Devys
@sl
type
label
Didier Devys
@ast
Didier Devys
@en
Didier Devys
@es
Didier Devys
@nl
Didier Devys
@sl
prefLabel
Didier Devys
@ast
Didier Devys
@en
Didier Devys
@es
Didier Devys
@nl
Didier Devys
@sl
P106
P1153
57191351330
6701813137
P21
P31
P496
0000-0001-9655-3512