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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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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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An accurate model of polyglutamine
Proteins: Structure, Function, and Bioinformatics, 2011AbstractPolyglutamine 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
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Autophagy and Polyglutamine Disease
2020Polyglutamine (polyQ) disease is a type of fatal neurodegenerative disease caused by an expansion of CAG repeats in a specific gene, resulting in a protein with an abnormal polyQ fragment. The age of onset and the degree of pathological deterioration are related to the length of the polyQ fragment.
Haigang, Ren +2 more
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Folding of polyglutamine chains
The Journal of Chemical Physics, 2008Long polyglutamine chains have been associated with a number of neurodegenerative diseases. These include Huntington’s disease, where expanded polyglutamine (PolyQ) sequences longer than 36 residues are correlated with the onset of symptoms. In this paper we study the folding pathway of a 54-residue PolyQ chain into a β-helical structure.
Manan, Chopra +3 more
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Solubilization and disaggregation of polyglutamine peptides [PDF]
Protein Science, 2001 AbstractA method is described for dissolving and disaggregating chemically synthesized polyglutamine peptides. Polyglutamine peptides longer than about Q20 have been reported to be insoluble in water, but dissolution in – and evaporation from ‐ a mixture of trifluoroacetic acid and hexafluoroisopropanol converts polyglutamine peptides up to at least ...
Ronald Wetzel
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Proteomics of Polyglutamine Aggregates
2006In nine members of polyglutamine (polyQ) diseases, CAG repeat expansions of their responsible genes are observed. The disease is considered to be caused by the formation of polyQ aggregates that sequester proteins essential for cell viability. To understand the pathological process of polyQ diseases, a proteomic approach was used to identify aggregate ...
Kenichi, Mitsui +2 more
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Polyglutamine makes the switch
Science Signaling, 2017In worms, a regulator of noncoding RNA directly catalyzes formation of toxic protein aggregates in the presence of polyglutamine.
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The role of chaperones in polyglutamine disease
Trends in Molecular Medicine, 2002The "triplet repeat" neurodegenerative diseases are linked by a common mode of pathogenicity, wherein a polyglutamine expansion within the relevant disease-causing protein induces toxicity. Although details underlying pathogenesis are largely unknown, protein chaperones appear to be effective suppressors of toxicity in various experimental models ...
Puneet, Opal, Huda Y, Zoghbi
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Conformation Polymorphism of Polyglutamine Proteins
Trends in Biochemical Sciences, 2018Expanded polyglutamine (polyQ) stretches within endogenous proteins cause at least nine human diseases. The structural basis of polyQ pathogenesis is the key to understanding fundamental mechanisms of these diseases, but it remains unclear and controversial due to a lack of polyQ protein structures at the single-atom level. Various hypotheses have been
Xinran Feng, Shouqing Luo, Boxun Lu
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Polyglutamine Diseases and Molecular Chaperones
IUBMB Life, 2003AbstractThe polyglutamine diseases, a group of diseases currently thought to consist of nine inherited neurodegenerative diseases, are caused by the expansion of unstable CAG trinucleotide repeats that code for polyglutamine tracts in the responsible genes.
Yoko, Kimura, Akira, Kakizuka
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