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ProteomicsThe effect of Scp160p on polyQ-mediated protein aggregation
We have previously shown that the yeast homolog of the RNA-binding vigilin proteins – Scp160p – is involved in enhancing translation efficiency in the context of codon usage. In the current study, we investigated the influence of Scp160p on the biology of polyQ reporters which differ in the codon us...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-07-03 | PXD008175 | Pride
Rna-binding protein Vigilin Prions Aggregation Polyglutamine Polyq 
TranscriptomicsDisrupting SUMOylation potentiates transactivation function and ameliorates polyglutamine AR-mediated disease
Our findings demonstrate beneficial effects of enhancing transactivation function of the ligand-activated polyQ AR and indicate that the SUMOylation pathway may provide new targets for therapeutic intervention. We mutated conserved lysines in the polyQ AR that are targeted by SUMO, a modification th...
ORGANISM(S): Mus musculus 
2015-12-21 | E-GEOD-60691 | biostudies-arrayexpress
ProteomicsArabidopsis thaliana polyQ - interactors
We've demonstrated that plants are resistant to the overexpression of polyglutamine (polyQ) extended proteins that cause protein aggregation and Huntington's disease in human cells. To investigate which proteins, maintain polyQ proteins correctly folded and avoid polyQ aggregates in plant cells. Ou...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2023-07-17 | PXD041001 | Pride
Arabidopsis thaliana Polyq-extended proteins Huntington's disease 
TranscriptomicsPolyglutamine Atrophin provokes neurodegeneration in Drosophila
Dentatorubral-pallidoluysian Atrophy (DRPLA) is a human polyQ disease caused by the expansion of a CAG strech in the atrophin-1 (at-1) gene. In all vertebrates, a second atrophin gene (at-2) is present and it encodes a related protein void of polyQ tracks. In D.melanogaster there is one conserved At...
ORGANISM(S): Drosophila melanogaster 
2011-03-01 | E-GEOD-26246 | biostudies-arrayexpress
ProteomicsFormation of toxic oligomers of polyQ-expanded Huntingtin by prion-mediated cross-seeding
Manifestation of aggregate pathology in Huntington’s disease is thought to be facilitated by a preferential vulnerability of affected brain cells to age-dependent proteostatic decline. To understand how specific cellular backgrounds may facilitate pathologic aggregation, we utilized the yeast model ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-10-21 | PXD031337 | Pride
Aggregation Proteostasis Oligomers Polyq Huntington’s disease Rnq1 Yeast Neurodegeneration Optogenetics Prions 
GenomicsTranscriptomics profile of polyQ expressing U2OS cells and clofazimine treated polyQ expressing U2OS cells
Transcriptomics profile of polyQ expressing U2OS cells and clofazimine treated polyQ expressing U2OS cells
PRJNA923331 | ENA
UnknownSmall-molecule modulators of TRMT2A decrease PolyQ aggregation and PolyQ-induced cell death.
Not available
S-EPMC8759985 | biostudies-literature
UnknownPolyQ 2.0: an improved version of PolyQ, a database of human polyglutamine proteins.
Not available
S-EPMC4792530 | biostudies-literature
UnknownCoaggregation of polyglutamine (polyQ) proteins is mediated by polyQ-tract interactions and impairs cellular proteostasis.
Not available
S-EPMC10281877 | biostudies-literature
UnknownAnti-PolyQ Antibodies Recognize a Short PolyQ Stretch in Both Normal and Mutant Huntingtin Exon 1.
Not available
S-EPMC4520773 | biostudies-literature
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