rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2008-6-16
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pubmed:abstractText |
Budding yeast Saccharomyces cerevisiae has proven to be a valuable model organism for studying fundamental cellular processes across the eukaryotic kingdom including man. In this respect, complementation assays, in which the yeast protein is replaced by a homologous protein from another organism, have been very instructive. A newer trend is to use the yeast cell factory as a toolbox to understand cellular processes controlled by proteins for which the yeast lacks functional counterparts. An increasing number of studies have indicated that S. cerevisiae is a suitable model system to decipher molecular mechanisms involved in a variety of neurodegenerative disorders caused by aberrant protein folding. Here we review the current knowledge gained by the use of so-called humanized yeasts in the field of Huntington's, Parkinson's and Alzheimer's diseases.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosis Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Synuclein,
http://linkedlifedata.com/resource/pubmed/chemical/polyglutamine,
http://linkedlifedata.com/resource/pubmed/chemical/tau Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0006-3002
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
1783
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1381-95
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:18298958-Alzheimer Disease,
pubmed-meshheading:18298958-Amyloid beta-Peptides,
pubmed-meshheading:18298958-Apoptosis,
pubmed-meshheading:18298958-Apoptosis Regulatory Proteins,
pubmed-meshheading:18298958-Heat-Shock Proteins,
pubmed-meshheading:18298958-Humans,
pubmed-meshheading:18298958-Huntington Disease,
pubmed-meshheading:18298958-Models, Biological,
pubmed-meshheading:18298958-Nerve Degeneration,
pubmed-meshheading:18298958-Nerve Tissue Proteins,
pubmed-meshheading:18298958-Nuclear Proteins,
pubmed-meshheading:18298958-Parkinson Disease,
pubmed-meshheading:18298958-Peptides,
pubmed-meshheading:18298958-Protein Folding,
pubmed-meshheading:18298958-Saccharomyces cerevisiae,
pubmed-meshheading:18298958-Yeasts,
pubmed-meshheading:18298958-alpha-Synuclein,
pubmed-meshheading:18298958-tau Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
Protein folding diseases and neurodegeneration: lessons learned from yeast.
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pubmed:affiliation |
Functional Biology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 31, Leuven-Heverlee, Belgium. joris.winderickx@bio.kuleuven.be
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|