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ProteomicsSite-Specific Ubiquitination of Pathogenic Huntingtin Attenuates its Deleterious Effects
Huntington’s disease (HD) is a progressive incurable neurodegenerative disorder characterized by motor and neuropsychiatric symptoms. It is caused by expansion of a CAG triplet in the N-terminal domain of exon 1 in the huntingtin (HTT) gene that codes for an expanded polyglutamine (polyQ) stretch in...
ORGANISM(S): Rattus rattus (Black rat) 
2020-06-30 | PXD019553 | Pride
Huntingtin ubiquitination 
ProteomicsSite-Specific Ubiquitination of Pathogenic Huntingtin Attenuates its Deleterious Effects- PART2
Huntington’s disease (HD) is a progressive incurable neurodegenerative disorder characterized by motor and neuropsychiatric symptoms. It is caused by expansion of a CAG triplet in the N-terminal domain of exon 1 in the huntingtin (HTT) gene that codes for an expanded polyglutamine (polyQ) stretch in...
ORGANISM(S): Homo sapiens (Human) 
2020-06-30 | PXD019552 | Pride
Ubiquitination huntingtin 
UnknownSite-specific ubiquitination of pathogenic huntingtin attenuates its deleterious effects.
Not available
S-EPMC7414096 | biostudies-literature
UnknownElucidation of Site-Specific Ubiquitination on Chaperones in Response to Mutant Huntingtin.
Not available
S-EPMC11407140 | biostudies-literature
UnknownPeripheral sequestration of huntingtin delays neuronal death and depends on N-terminal ubiquitination.
Not available
S-EPMC11330980 | biostudies-literature
ProteomicsProteome and ubiquitinome changes in Huntington’s disease
Huntington’s disease is caused by a polyglutamine repeat expansion at the N-terminus of the huntingtin protein which affects the function and folding of the protein, and results in intracellular protein aggregates. Here, we examined whether this mutation leads to altered ubiquitination of huntingtin...
ORGANISM(S): Mus musculus (Mouse) 
2019-06-05 | PXD010161 | Pride
Ubiquitination Digly Ptms Brain Lfq Mouse Huntington 
TranscriptomicsChIP for H3K27me3 in Murine ES Cells: wild type and Ring1B-/- cells
Native ChIP on chip for H3K27me3 in murine ES cells comparing WT and Ring1B-/- cells. Paper Abstract: How polycomb group proteins repress gene expression in vivo is not known. Whilst histone modifying activities of the polycomb repressive complexes have been studied extensively, in vitro data has su...
ORGANISM(S): Mus musculus 
2010-05-14 | E-GEOD-20213 | biostudies-arrayexpress
UnknownHuntingtin Ubiquitination Mechanisms and Novel Possible Therapies to Decrease the Toxic Effects of Mutated Huntingtin.
Not available
S-EPMC8709430 | biostudies-literature
GenomicsFbxl10 regulates PRC1 recruitment to CpG islands and H2A ubiquitination
Polycomb repressive complex 1 (PRC1) catalyzes H2A monoubiquitination (uH2A) and regulates pluripotency in embryonic stem cells (ESCs). However the mechanisms controlling PRC1 recruitment and activity are largely unknown. Here we show that Fbxl10 interacts with Ring1B and Nspc1, forming a non-canoni...
ORGANISM(S): Mus musculus 
2012-12-31 | E-GEOD-37930 | biostudies-arrayexpress
GenomicsMouse ES cells expressing catalytically inactive Ring1B display impaired Ring1B and H3K27me3 deposition.
ChIP-seq for H3K27me3 and Ring1B was performed in WT mESCs and mESCs containing catalytically inactive Ring1B (I53A mutant). Cells expressing catalytically inactive Ring1B maintain the spatial distribution of Ring1B and H3K27me3 but at reduced levels. These findings support the notion that PRC2 recr...
ORGANISM(S): Mus musculus 
2015-09-20 | E-GEOD-69955 | biostudies-arrayexpress
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