Progressive Disruption of Cellular Protein Folding in Models of Polyglutamine Diseases

By Tali Gidalevitz, Anat Ben-Zvi, K. H. Ho, Heather R. Brignull, Richard I. Morimoto. Science, 2006

660 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/1d8afcda612473f7ed0b1e617918219222895ab0

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In Cellular and Molecular Neuroscience

In Molecular Biology

Citations in the corpus

Molecular chaperones in protein folding and proteostasis (2011, background): “This is consistent with recent evidence that aberrantly folded protein species may interfere with central proteostasis functions, including protein folding and clearance mechanism”
Widespread Protein Aggregation as an Inherent Part of Aging in C. elegans (2010, background): “Surprisingly, we found a slight, albeit statistically significant, decrease in Q35 aggregates in animals with the aggregation-prone protein (Figure S6, Kruskal-Wallis test, p,0.0001).”
Understanding the contribution of synonymous mutations to human disease (2011, methodology): “A vivid experimental demonstration of this is provided by the work of Morimoto and colleague”
Cellular strategies for controlling protein aggregation (2010, background): “There seems to be a preference for the co-aggregation of the same type of protei”
Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. (2006, result): “This is consistent with recent results showing that global alteration of Ins2- and HSF1-mediated stress-response pathways arrest and reverse onset of aggressive misfolding amyloid diseases in C. elegans ( Gidalevitz et al., 2006; Morley and Morimoto, 2004).”
Pathways of cellular proteostasis in aging and disease (2018, background): “, 1999; Gusella and MacDonald, 2006), manifestation is age dependent and triggered by PN decline (Morley et al., 2002; Gidalevitz et al., 2006).”
In vivo demonstration that α-synuclein oligomers are toxic (2011, background): “Another important issue is whether the observed toxicity of α-syn variants is specific or whether any protein aggregate expressed at high levels might be toxic in vivo (26).”
In and out of the ER: protein folding, quality control, degradation, and related human diseases. (2007, background): “Certainly, folding and degradation are strongly interconnected as it has been established that a functional degradation machinery is required for maintenance of protein folding capacity (86, 114, 268).”
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. (2011, background): “In another model, misfolding proteins, by engaging the chaperone machinery, are thought to interfere with central protein quality control and clearance mechanisms, possibly resulting in a propagation of folding defects (Balch et al., 2008; Bence et al., 2001; Gidalevitz et al., 2006).”