Identification of human proteins that modify misfolding and proteotoxicity of pathogenic ataxin-1
S Petrakis, T Raskó, J Russ, RP Friedrich, M Stroedicke… - 2012 - journals.plos.org
Proteins with long, pathogenic polyglutamine (polyQ) sequences have an enhanced
propensity to spontaneously misfold and self-assemble into insoluble protein aggregates …
propensity to spontaneously misfold and self-assemble into insoluble protein aggregates …
Aggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: implication in a loss-of-function pathology
Expansion of polyglutamine (polyQ) tract may cause protein misfolding and aggregation that
lead to cytotoxicity and neurodegeneration, but the underlying mechanism remains to be …
lead to cytotoxicity and neurodegeneration, but the underlying mechanism remains to be …
PolyQ-expanded proteins impair cellular proteostasis of ataxin-3 through sequestering the co-chaperone HSJ1 into aggregates
HW Yue, JY Hong, SX Zhang, LL Jiang, HY Hu - Scientific Reports, 2021 - nature.com
Polyglutamine (polyQ) expansion of proteins can trigger protein misfolding and amyloid-like
aggregation, which thus lead to severe cytotoxicities and even the respective …
aggregation, which thus lead to severe cytotoxicities and even the respective …
Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity
Background Misfolding-and aggregation-prone proteins underlying Parkinson's,
Huntington's and Machado-Joseph diseases, namely α-synuclein, huntingtin, and ataxin-3 …
Huntington's and Machado-Joseph diseases, namely α-synuclein, huntingtin, and ataxin-3 …
Polyglutamine expansion diseases: More than simple repeats
A Silva, AV de Almeida, S Macedo-Ribeiro - Journal of Structural Biology, 2018 - Elsevier
Polyglutamine (polyQ) repeat-containing proteins are widespread in the human proteome
but only nine of them are associated with highly incapacitating neurodegenerative disorders …
but only nine of them are associated with highly incapacitating neurodegenerative disorders …
Yeast as a platform to explore polyglutamine toxicity and aggregation
ML Duennwald - Tandem repeats in genes, proteins, and Disease …, 2013 - Springer
Protein misfolding is associated with many neurodegenerative diseases, including
neurodegenerative diseases caused by polyglutamine expansion proteins, such as …
neurodegenerative diseases caused by polyglutamine expansion proteins, such as …
Splice isoforms of the polyglutamine disease protein ataxin-3 exhibit similar enzymatic yet different aggregation properties
GM Harris, K Dodelzon, L Gong, P Gonzalez-Alegre… - PloS one, 2010 - journals.plos.org
Protein context clearly influences neurotoxicity in polyglutamine diseases, but the
contribution of alternative splicing to this phenomenon has rarely been investigated. Ataxin …
contribution of alternative splicing to this phenomenon has rarely been investigated. Ataxin …
In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis
AJ Williams, TM Knutson, VFC Gould… - Neurobiology of disease, 2009 - Elsevier
Perturbations in neuronal protein homeostasis likely contribute to disease pathogenesis in
polyglutamine (polyQ) neurodegenerative disorders. Here we provide evidence that the co …
polyglutamine (polyQ) neurodegenerative disorders. Here we provide evidence that the co …
AQAMAN, a bisamidine-based inhibitor of toxic protein inclusions in neurons, ameliorates cytotoxicity in polyglutamine disease models
Polyglutamine (polyQ) diseases are a group of dominantly inherited neurodegenerative
disorders caused by the expansion of an unstable CAG repeat in the coding region of the …
disorders caused by the expansion of an unstable CAG repeat in the coding region of the …
Flanking sequences profoundly alter polyglutamine toxicity in yeast
ML Duennwald, S Jagadish… - Proceedings of the …, 2006 - National Acad Sciences
Protein misfolding is the molecular basis for several human diseases. How the primary
amino acid sequence triggers misfolding and determines the benign or toxic character of the …
amino acid sequence triggers misfolding and determines the benign or toxic character of the …