Results 31 to 40 of about 2,129,859 (190)
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
Journal of Neuroinflammation, 2017 Background Polyglutamine diseases constitute a class of neurodegenerative disorders associated with expansion of the cytosine-adenine-guanine (CAG) triplet, in protein coding genes.
Reema Roshan +5 more
doaj +1 more source
Polyglutamine disease in peripheral tissues
Human Molecular Genetics, 2023 Abstract This year is a milestone anniversary of the discovery that Huntington’s disease is caused by the presence of expanded polyglutamine repeats in the huntingtin gene leading to the formation of huntingtin aggregates. 30 years have elapsed and there is still no cure and the only FDA-approved treatment to alleviate the debilitating ...
Barwell, Taylor, Seroude, Laurent
openaire +3 more sources
Na+/H+ exchangers induce autophagy in neurons and inhibit polyglutamine-induced aggregate formation.
PLoS ONE, 2013 In polyglutamine diseases, an abnormally elongated polyglutamine results in protein misfolding and accumulation of intracellular aggregates. Autophagy is a major cellular degradative pathway responsible for eliminating unnecessary proteins, including ...
Kazuya Togashi +5 more
doaj +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
Ataxin-1 fusion partners alter polyQ lethality and aggregation [PDF]
, 2007 Intranuclear inclusion bodies (IBs) are the histopathologic markers of multiple protein folding diseases. IB formation has been extensively studied using fluorescent fusion products of pathogenic polyglutamine (polyQ) expressing proteins.
Rich, T. +5 more
core +2 more sources
Polyglutamine-Specific Gold Nanoparticle Complex Alleviates Mutant Huntingtin-Induced Toxicity
, 2021 Huntington’s disease (HD) belongs to protein misfolding disorders associated with polyglutamine (polyQ)-rich mutant huntingtin (mHtt) protein inclusions. Currently, it is indicated that the aggregation of polyQ-rich mHtt participates in neuronal toxicity
Chun-Hong Kuo (1448776) +33 more
core +1 more source
Population genetics of spinoсerebellar ataxias caused by polyglutamine expansions
Вавиловский журнал генетики и селекции, 2019 Hereditary disorders of the neuronal system are some of the most important problems of medicine in the XXI century. The most interesting representatives of this group are highly prevalent polyglutamine spinocerebellar ataxias (SCAs).
A. N. Shuvaev +8 more
doaj +1 more source
Metallothioneins and copper metabolism are candidate therapeutic targets in Huntington’s disease [PDF]
, 2010 HD (Huntington's disease) is caused by a polyQ (polyglutamine) expansion in the huntingtin protein, which leads to protein misfolding and aggregation of this protein. Abnormal copper accumulation in the HD brain was first reported more than 15 years ago.
Giorgini, Flaviano +18 more
core +1 more source
Degenerate codon mixing for PCR-based manipulation of highly repetitive sequences
BMC Research Notes, 2018 Objective Repeat expansion of polyglutamine tracks leads to a group of inherited human neurodegenerative disorders. Studying such repetitive sequences is required to gain insight into the pathophysiology of these diseases.
Dhanushika Ratnayake +2 more
doaj +1 more source