[The information embedded into protein conformation: the mammalian prion protein is not the only one which "prionized"].
Identifieur interne : 000B72 ( PubMed/Curation ); précédent : 000B71; suivant : 000B73[The information embedded into protein conformation: the mammalian prion protein is not the only one which "prionized"].
Auteurs : Karine Toupet [France] ; Sylvain LehmannSource :
- Medecine sciences : M/S [ 0767-0974 ] ; 2009.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Prions.
- Animals, Mammals, Models, Molecular, Protein Conformation, Protein Folding.
Abstract
Basic research on prions and on protein and peptide aggregation generated a new vision of the pathologic mechanisms of many disorders regrouped under the term "proteinopathies". The latter include several neurodegenerative disorders (Alzheimer, Parkinson disease...) which could benefit for their diagnosis and therapeutics of this type of research. Importantly, the presence of proteins behaving like prions in yeast also contributed to the advance of knowledge in this area by showing that the transmission of a conformational information could be considered as a new epigenetic mechanism. In addition yeast models allow to study the molecular mechanism of protein aggregation, the role of accessory factors, like chaperones, and the screening of therapeutic agents.
DOI: 10.1051/medsci/2009253307
PubMed: 19361397
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pubmed:19361397Le document en format XML
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The latter include several neurodegenerative disorders (Alzheimer, Parkinson disease...) which could benefit for their diagnosis and therapeutics of this type of research. Importantly, the presence of proteins behaving like prions in yeast also contributed to the advance of knowledge in this area by showing that the transmission of a conformational information could be considered as a new epigenetic mechanism. 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