The aggravating role of the ubiquitin-proteasome system in neurodegeneration (Q36020204)

11 August 2017

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title

The aggravating role of the ubiquitin-proteasome system in neurodegeneration (English)

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ubiquitin-proteasome system

11 August 2017

main subject

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Helen C Ardley

1

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11 August 2017

Chao-Chun Hung

series ordinal

2

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11 August 2017

Philip A Robinson

series ordinal

3

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11 August 2017

language of work or name

English

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publication date

1 January 2005

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11 August 2017

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11 August 2017

volume

579

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11 August 2017

issue

3

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11 August 2017

page(s)

571-576

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Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodie

11 August 2017

cites work

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Pathological lesions of Alzheimer's disease and dementia with Lewy bodies brains exhibit immunoreactivity to an ATPase that is a regulatory subunit of the 26S proteasome

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Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression

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Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function.

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The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility

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Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases

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Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases

21 January 2018

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Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice

21 January 2018

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Association of ataxin-7 with the proteasome subunit S4 of the 19S regulatory complex

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CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity

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Siah-1 facilitates ubiquitination and degradation of synphilin-1

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SUMO-1 co-localized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death

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21 January 2018

Identifiers

DOI

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11 August 2017

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