期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 60, 期 1, 页码 133-143出版社
SPRINGER BASEL AG
DOI: 10.1007/s000180300009
关键词
protein conformational disorders; prion protein misfolding; transmissible spongiform encephalopathies; neuronal apoptosis; brain inflammation; prion protein function
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.
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