Protein misfolding and disease: The case of prion disorders
Author
dc.contributor.author
Hetz Flores, Claudio
Author
dc.contributor.author
Soto, C.
Admission date
dc.date.accessioned
2019-01-29T17:51:56Z
Available date
dc.date.available
2019-01-29T17:51:56Z
Publication date
dc.date.issued
2003
Cita de ítem
dc.identifier.citation
Cellular and Molecular Life Sciences, Volumen 60, Issue 1, 2018, Pages 133-143
Identifier
dc.identifier.issn
1420682X
Identifier
dc.identifier.other
10.1007/s000180300009
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/163615
Abstract
dc.description.abstract
Recent findings strongly support the hypothesis that diverse human disorders, including the most common neurodegenerative diseases, arise from misfolding and aggregation of an underlying protein. Despite the good evidence for the involvement of protein misfolding in disease pathogenesis, the mechanism by which protein conformational changes participate in the disease is still unclear. Among the best-studied diseases of this group are the transmissible spongiform encephalopathies or prion-related disorders, in which misfolding of the normal prion protein plays a key role in the disease. In this article we review recent data on the link between prion protein misfolding and the pathogensis of spongiform encephalopathies.