Disruption of the toxic conformation of the expanded polyglutamine stretch leads to suppression of aggregate formation and cytotoxicity

HA Popiel, Y Nagai, O Onodera, T Inui… - Biochemical and …, 2004 - Elsevier
The polyglutamine (polyQ) diseases are a class of inherited neurodegenerative diseases
including Huntington's disease, caused by the expansion of a polyQ stretch within each …

Towards the treatment of polyglutamine diseases: the modulatory role of protein context

AL Robertson, SP Bottomley - Current medicinal chemistry, 2010 - ingentaconnect.com
Protein aggregation is a key mechanism involved in neurodegeneration associated with
Alzheimer's, Parkinson's and Huntington's diseases. Nine diseases (including Huntington's) …

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 …

Conformation polymorphism of polyglutamine proteins

X Feng, S Luo, B Lu - Trends in biochemical sciences, 2018 - cell.com
Expanded polyglutamine (polyQ) stretches within endogenous proteins cause at least nine
human diseases. The structural basis of polyQ pathogenesis is the key to understanding …

[HTML][HTML] A survey of protein interactions and posttranslational modifications that influence the polyglutamine diseases

SL Johnson, WL Tsou, MV Prifti, AL Harris… - Frontiers in Molecular …, 2022 - frontiersin.org
The presence and aggregation of misfolded proteins has deleterious effects in the nervous
system. Among the various diseases caused by misfolded proteins is the family of the …

[HTML][HTML] The structural impact of a polyglutamine tract is location-dependent

AL Robertson, J Horne, AM Ellisdon, B Thomas… - Biophysical journal, 2008 - cell.com
Polyglutamine (polyQ) expansion leads to protein aggregation and neurodegeneration in
Huntington's disease and eight other inherited neurological conditions. Expansion of the …

Pathogenic and non-pathogenic polyglutamine tracts have similar structural properties: towards a length-dependent toxicity gradient

FAC Klein, A Pastore, L Masino, G Zeder-Lutz… - Journal of molecular …, 2007 - Elsevier
Abnormally expanded polyglutamine (polyQ) tracts provide a gain of toxic functions to nine
otherwise unrelated human proteins and induce progressive neurodegenerative diseases …

Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity

H Sakahira, P Breuer… - Proceedings of the …, 2002 - National Acad Sciences
The formation of insoluble protein aggregates in neurons is a hallmark of neurodegenerative
diseases caused by proteins with expanded polyglutamine (polyQ) repeats. However, the …

Polyglutamine aggregation in Huntington and related diseases

S Polling, AF Hill, DM Hatters - Tandem Repeat Polymorphisms: Genetic …, 2012 - Springer
Polyglutamine (polyQ)-expansions in differentproteins cause nine neurodegenerative
diseases. While polyQ aggregation is a key pathological hallmark of these diseases, how …

Analyzing the aggregation of polyglutamine-expansion proteins and its modulation by molecular chaperones

H Kubota, A Kitamura, K Nagata - Methods, 2011 - Elsevier
Polyglutamine (polyQ)-expansion proteins cause protein aggregation in the cytosol and
nucleus of neuronal cells, leading to neurodegenerative diseases. For example, expansion …