Journal article
Polyglutamine neurodegeneration: protein misfolding revisited
Trends in neurosciences (Regular ed.), Vol.31(10), pp.521-528
10/2008
DOI: 10.1016/j.tins.2008.07.004
PMCID: PMC2580745
PMID: 18778858
Abstract
Polyglutamine diseases are a major cause of neurodegeneration worldwide. Recent studies highlight the importance of protein quality control mechanisms in regulating polyglutamine-induced toxicity. Here we discuss a model of disease pathogenesis that integrates current understanding of the role of protein folding in polyglutamine disease with emerging evidence that alterations in native protein interactions contribute to toxicity. We also incorporate new findings on other age-related neurodegenerative diseases in an effort to explain how protein aggregation and normal aging processes might be involved in polyglutamine disease pathogenesis.
Details
- Title: Subtitle
- Polyglutamine neurodegeneration: protein misfolding revisited
- Creators
- Aislinn J Williams - Program in Neuroscience and Medical Scientist Training Program, University of Iowa, 2206 MERF, Iowa City, IA 52242, USAHenry L Paulson
- Resource Type
- Journal article
- Publication Details
- Trends in neurosciences (Regular ed.), Vol.31(10), pp.521-528
- DOI
- 10.1016/j.tins.2008.07.004
- PMID
- 18778858
- PMCID
- PMC2580745
- NLM abbreviation
- Trends Neurosci
- ISSN
- 0166-2236
- eISSN
- 1878-108X
- Publisher
- Elsevier BV; England
- Grant note
- NS38712 / NINDS NIH HHS\nNS056609 / NINDS NIH HHS\nF31 NS056609 / NINDS NIH HHS\nT32 GM007337 / NIGMS NIH HHS\nR01 NS038712 / NINDS NIH HHS\nF31 NS056609-02 / NINDS NIH HHS\nR01 NS038712-01A1 / NINDS NIH HHS
- Language
- English
- Date published
- 10/2008
- Academic Unit
- Psychiatry; Iowa Neuroscience Institute
- Record Identifier
- 9984066137402771
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