Different ataxin-3 amyloid aggregates induce intracellular Ca(2+) deregulation by different mechanisms in cerebellar granule cells.
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The Toxic Effects of Pathogenic Ataxin-3 Variants in a Yeast Cellular ModelMisfolding of amyloidogenic proteins and their interactions with membranes.From pathways to targets: understanding the mechanisms behind polyglutamine disease.Toxic species in amyloid disorders: Oligomers or mature fibrils.Biochemical and Electrophysiological Modification of Amyloid Transthyretin on Cardiomyocytes.Antisense Oligonucleotide-Mediated Removal of the Polyglutamine Repeat in Spinocerebellar Ataxia Type 3 MiceThe polyglutamine protein ataxin-3 enables normal growth under heat shock conditions in the methylotrophic yeast Pichia pastoris.Unbiased screen identifies aripiprazole as a modulator of abundance of the polyglutamine disease protein, ataxin-3.Epigallocatechin-3-gallate and related phenol compounds redirect the amyloidogenic aggregation pathway of ataxin-3 towards non-toxic aggregates and prevent toxicity in neural cells and Caenorhabditis elegans animal model.
P2860
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P2860
Different ataxin-3 amyloid aggregates induce intracellular Ca(2+) deregulation by different mechanisms in cerebellar granule cells.
description
2013 nî lūn-bûn
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name
Different ataxin-3 amyloid aggregates induce intracellular Ca
@nl
Different ataxin-3 amyloid agg ...... s in cerebellar granule cells.
@en
type
label
Different ataxin-3 amyloid aggregates induce intracellular Ca
@nl
Different ataxin-3 amyloid agg ...... s in cerebellar granule cells.
@en
prefLabel
Different ataxin-3 amyloid aggregates induce intracellular Ca
@nl
Different ataxin-3 amyloid agg ...... s in cerebellar granule cells.
@en
P2093
P50
P1476
Different ataxin-3 amyloid agg ...... s in cerebellar granule cells.
@en
P2093
Alessandra Gliozzi
Amanda Penco
Anna Maria Frana
Annalisa Relini
Daniele Nosi
Elena Gatta
Francesca Pellistri
Gaetano Invernizzi
Maria Elena Regonesi
Mauro Robello
P304
P356
10.1016/J.BBAMCR.2013.08.019
P577
2013-09-11T00:00:00Z