Results 31 to 40 of about 22,723 (239)
Autophagy and polyglutamine diseases.
Prog Neurobiol, 2012 In polyglutamine diseases, an abnormally elongated polyglutamine tract results in protein misfolding and accumulation of intracellular aggregates. The length of the polyglutamine expansion correlates with the tendency of the mutant protein to aggregate, as well as with neuronal toxicity and earlier disease onset.
Jimenez-Sanchez M +3 more
europepmc +5 more sources
Brain Sciences, 2014 Huntington disease and other diseases of polyglutamine expansion are each caused by a different protein bearing an excessively long polyglutamine sequence and are associated with neuronal death.
Guylaine Hoffner, Philippe Djian
doaj +1 more source
Hosting Neurotoxicity in Polyglutamine Disease [PDF]
Cell, 2006 Polyglutamine diseases are caused by an expanded glutamine domain thought to confer a toxic activity onto the respective disease proteins. In this issue, propose that toxicity of the polyglutamine protein Ataxin-1 may not be due to abberant protein interactions mediated by the polyglutamine expansion.
Liu, Nan, Bonini, Nancy M.
openaire +2 more sources
Are Polyglutamine Diseases Expanding? [PDF]
Neuron, 2011 It remains a matter of speculation as to whether the sense CUG-containing RNA and/or the antisense CAG-encoding polyglutamine peptide serves as the pathogenic moiety in Huntington's disease like-2 (HDL2). In this issue of Neuron, Wilburn et al. show that in a HDL2 mouse model, the polyglutamine peptide drives disease progression.
openaire +2 more sources
Are long-range structural correlations behind the aggregration phenomena of polyglutamine diseases? [PDF]
PLoS Comput Biol, 2012 Moradi M, Babin V, Roland C, Sagui C.
europepmc +3 more sources
Proteasome degrades soluble expanded polyglutamine completely and efficiently
Neurobiology of Disease, 2004 To date, nine progressive neurodegenerative diseases are caused by expansion of the CAG repeat coding for polyglutamine, including Huntington's disease and several forms of spinocerebellar ataxia.
Andrej Michalik +1 more
doaj +1 more source
A Variable Polyglutamine Repeat Affects Subcellular Localization and Regulatory Activity of a Populus ANGUSTIFOLIA Protein. [PDF]
, 2018 Polyglutamine (polyQ) stretches have been reported to occur in proteins across many organisms including animals, fungi and plants. Expansion of these repeats has attracted much attention due their associations with numerous human diseases including ...
Barry, Kerrie +12 more
core +1 more source
Cysteine String Protein Controls Two Routes of Export for Misfolded Huntingtin
Frontiers in Neuroscience, 2022 Extracellular vesicles (EVs) are secreted vesicles of diverse size and cargo that are implicated in the cell-to-cell transmission of disease-causing-proteins in several neurodegenerative diseases.
Desmond Pink +4 more
doaj +1 more source
RNA-mediated pathogenic mechanisms in polyglutamine diseases and amyotrophic lateral sclerosis. [PDF]
Front Cell Neurosci, 2014 Chan HY.
europepmc +3 more sources
ATXN2-CAG42 sequesters PABPC1 into insolubility and induces FBXW8 in cerebellum of old ataxic knock-in mice [PDF]
, 2012 Spinocerebellar Ataxia Type 2 (SCA2) is caused by expansion of a polyglutamine encoding triplet repeat in the human ATXN2 gene beyond (CAG)31. This is thought to mediate toxic gain-of-function by protein aggregation and to affect RNA processing ...
Auburger, Georg +8 more
core +3 more sources