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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2010-5-31
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pubmed:abstractText |
Ubiquitinated protein aggregates are hallmarks of a range of human diseases, including neurodegenerative, liver and muscle disorders. These protein aggregates are typically positive for the autophagy receptor p62. Whereas the ubiquitin-proteasome system (UPS) degrades shortlived and misfolded ubiquitinated proteins that are small enough to enter the narrow pore of the barrel-shaped proteasome, the lysosomal pathway of autophagy can degrade larger structures including entire organelles or protein aggregates. This degradation requires autophagy receptors that link the cargo with the molecular machinery of autophagy and is enhanced by certain posttranslational modifications of the cargo. In this review we focus on how autophagy clears aggregate-prone proteins and the relevance of this process to protein aggregate associated diseases.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/HDAC6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/NBR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/P62 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitinated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/WDFY3 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1873-3468
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
584
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2635-45
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pubmed:meshHeading |
pubmed-meshheading:20412801-Acetylation,
pubmed-meshheading:20412801-Active Transport, Cell Nucleus,
pubmed-meshheading:20412801-Autophagy,
pubmed-meshheading:20412801-Histone Deacetylases,
pubmed-meshheading:20412801-Humans,
pubmed-meshheading:20412801-Membrane Proteins,
pubmed-meshheading:20412801-Models, Biological,
pubmed-meshheading:20412801-Multiprotein Complexes,
pubmed-meshheading:20412801-Neurodegenerative Diseases,
pubmed-meshheading:20412801-Phosphorylation,
pubmed-meshheading:20412801-Proteasome Endopeptidase Complex,
pubmed-meshheading:20412801-Protein Transport,
pubmed-meshheading:20412801-Proteins,
pubmed-meshheading:20412801-RNA-Binding Proteins,
pubmed-meshheading:20412801-Transcription Factors,
pubmed-meshheading:20412801-Ubiquitinated Proteins,
pubmed-meshheading:20412801-Ubiquitination,
pubmed-meshheading:20412801-Unfolded Protein Response
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pubmed:year |
2010
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pubmed:articleTitle |
Fighting disease by selective autophagy of aggregate-prone proteins.
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pubmed:affiliation |
Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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