Results 11 to 20 of about 20,303 (218)
Current Opinion in Neurobiology, 2022 Polyglutamine diseases are a collection of nine CAG trinucleotide expansion disorders, presenting with a spectrum of neurological and clinical phenotypes. Recent human, mouse and cell studies of Huntington's disease have highlighted the role of DNA repair genes in somatic expansion of the CAG repeat region, modifying disease pathogenesis.
Emma L, Bunting +2 more
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Autophagy and polyglutamine diseases [PDF]
Progress in Neurobiology, 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, Maria +3 more
openaire +5 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.
Orr, Harry T., Harry T. Orr
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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.
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Skeletal Muscle Pathogenesis in Polyglutamine Diseases [PDF]
Cells, 2022 Polyglutamine diseases are characterized by selective dysfunction and degeneration of specific types of neurons in the central nervous system. In addition, nonneuronal cells can also be affected as a consequence of primary degeneration or due to neuronal
Caterina Marchioretti +5 more
doaj +2 more sources
Activation of p38MAPK contributes to expanded polyglutamine-induced cytotoxicity.
PLoS ONE, 2008 BackgroundThe signaling pathways that may modulate the pathogenesis of diseases induced by expanded polyglutamine proteins are not well understood.Methodologies/principal findingsHerein we demonstrate that expanded polyglutamine protein cytotoxicity is ...
Maria Tsirigotis +4 more
doaj +2 more sources
An accurate model of polyglutamine
Proteins: Structure, Function, and Bioinformatics, 2011 AbstractPolyglutamine repeats in proteins are highly correlated with amyloid formation and neurological disease. To better understand the molecular basis of glutamine repeat diseases, structural analysis of polyglutamine peptides as soluble monomers, oligomers, and insoluble amyloid fibrils is necessary.
Digambaranath, Jyothi L. +6 more
openaire +4 more sources
Polyglutamine makes the switch
Science Signaling, 2017 In worms, a regulator of noncoding RNA directly catalyzes formation of toxic protein aggregates in the presence of polyglutamine.
Alexandra A. Mushegian
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Altered Metabolic Signaling and Potential Therapies in Polyglutamine Diseases
MetabolitesPolyglutamine diseases comprise a cluster of genetic disorders involving neurodegeneration and movement disabilities. In polyglutamine diseases, the target proteins become aberrated due to polyglutamine repeat formation.
Alisha Vohra +2 more
doaj +2 more sources
Polyglutamine Repeat Length-Dependent Proteolysis of Huntingtin [PDF]
Neurobiology of Disease, 2002 Amino-terminal fragments of huntingtin, which contain the expanded polyglutamine repeat, have been proposed to contribute to the pathology of Huntington's disease (HD).
Banghua Sun +20 more
doaj +2 more sources