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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 
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 
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
UnknownPolyQ length co-evolution in neural proteins.
Not available
S-EPMC8121095 | biostudies-literature
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 
UnknownOverexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome.
Not available
S-EPMC4280636 | biostudies-literature
ProteomicsIncreased levels of the mitochondrial import factor Mia40 can prevent the aggregation of polyQ proteins in the cytosol
The formation of protein aggregates is a hallmark of neurodegenerative diseases. Observations on patient material and model systems demonstrated links between aggregate formation and declining mitochondrial functionality, but the causalities remained unclear. We used yeast as model system to analyze...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-08-05 | PXD023902 | Pride
Huntingtin / mia40 / mitochondria / protein aggregation / protein translocation 
UnknownAmyloid-like fibril formation by polyQ proteins: a critical balance between the polyQ length and the constraints imposed by the host protein.
Not available
S-EPMC3305072 | biostudies-literature
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