In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis

AJ Williams, TM Knutson, VFC Gould… - Neurobiology of disease, 2009 - Elsevier
Perturbations in neuronal protein homeostasis likely contribute to disease pathogenesis in
polyglutamine (polyQ) neurodegenerative disorders. Here we provide evidence that the co …

CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo

VM Miller, RF Nelson, CM Gouvion… - Journal of …, 2005 - Soc Neuroscience
Huntington's disease (HD) and other polyglutamine (polyQ) neurodegenerative diseases
are characterized by neuronal accumulation of the disease protein, suggesting that the …

[HTML][HTML] Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes

NR Jana, P Dikshit, A Goswami, S Kotliarova… - Journal of Biological …, 2005 - ASBMB
A major hallmark of the polyglutamine diseases is the formation of neuronal intranuclear
inclusions of the disease proteins that are ubiquitinated and often associated with various …

Role of heat shock proteins during polyglutamine neurodegeneration: mechanisms and hypothesis

A Wyttenbach - Journal of Molecular Neuroscience, 2004 - Springer
A common feature of many neurodegenerative diseases, including Alzheimer's and
Parkinsons's disease, the prion disorders, and the CAG repeat polyglutamine (polyQ) …

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 …

Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin

A Wyttenbach, O Sauvageot… - Human molecular …, 2002 - academic.oup.com
Neuronal loss and intraneuronal protein aggregates are characteristics of Huntington's
disease (HD), which is one of 10 known neurodegenerative disorders caused by an …

[HTML][HTML] The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease

Y Chai, L Wu, JD Griffin, HL Paulson - Journal of Biological Chemistry, 2001 - ASBMB
Intracellular inclusions are a unifying feature of polyglutamine (polyQ) neurodegenerative
diseases, yet each polyQ disease displays a unique pattern of neuronal degeneration. This …

Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and cell death in polyglutamine diseases

R de Pril, DF Fischer, RAC Roos… - Molecular and Cellular …, 2007 - Elsevier
Polyglutamine diseases are characterized by neuronal intranuclear inclusions of expanded
polyglutamine proteins, which are also ubiquitinated, indicating impairment of the ubiquitin …

Targeting Hsp70 facilitated protein quality control for treatment of polyglutamine diseases

AK Davis, WB Pratt, AP Lieberman, Y Osawa - Cellular and Molecular Life …, 2020 - Springer
The polyglutamine (polyQ) diseases are a group of nine fatal, adult-onset
neurodegenerative disorders characterized by the misfolding and aggregation of mutant …

[HTML][HTML] Defining the role of ubiquitin-interacting motifs in the polyglutamine disease protein, ataxin-3

SJS Berke, Y Chai, GL Marrs, H Wen… - Journal of Biological …, 2005 - ASBMB
Polyglutamine (polyQ) expansions cause neurodegeneration that is associated with protein
misfolding and influenced by functional properties of the host protein. The polyQ disease …