Prog Neurobiol 2012 May 10;97(2):67-82. Epub 2011 Sep 10.
Department of Medical Genetics, Cambridge Institute for Medical Research, Addenbrooke's Hospital, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK.
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Brain Res Rev 2008 Nov 23;59(1):245-52. Epub 2008 Aug 23.
Department of Human Genetics, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
A number of neurodegenerative diseases, including Alzheimer's, Parkinson's, and polyglutamine diseases, are characterized by the age-dependent formation of intracellular protein aggregates and neurodegeneration. Although there is some debate surrounding the role of these aggregates in neurotoxicity, the formation of aggregates is known to reflect the accumulation of misfolded and toxic proteins. The degradation of misfolded proteins occurs mainly via the ubiquitin-proteasome and autophagy pathways. Read More
Curr Top Dev Biol 2006 ;76:89-101
Department of Medical Genetics Cambridge Institute for Medical Research Addenbrooke's Hospital, Cambridge CB2 2XY United Kingdom.
Intracellular protein misfolding/aggregation are features of many late-onset neurodegenerative diseases, called proteinopathies. These include Alzheimer's disease, Parkinson's disease, tauopathies, and polyglutamine expansion diseases [e.g. Read More
Nature 2007 Jun;447(7146):859-63
Department of Neurology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA.
A prominent feature of late-onset neurodegenerative diseases is accumulation of misfolded protein in vulnerable neurons. When levels of misfolded protein overwhelm degradative pathways, the result is cellular toxicity and neurodegeneration. Cellular mechanisms for degrading misfolded protein include the ubiquitin-proteasome system (UPS), the main non-lysosomal degradative pathway for ubiquitinated proteins, and autophagy, a lysosome-mediated degradative pathway. Read More
PLoS One 2013 21;8(11):e81313. Epub 2013 Nov 21.
Department of Peripheral Nervous System Research, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Kodaira, Tokyo, Japan.
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 polyglutamine aggregates. Basal autophagy constitutively occurs at low levels in cells for the performance of homeostatic function, but the regulatory mechanism for basal autophagy remains elusive. Read More