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KMID : 1100220120110020038
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Dementia and Neurocognitive Disorders
2012 Volume.11 No. 2 p.38 ~ p.52
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Misfolded Proteins in Neurodegenerative Dementias:
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Yang Hyun-Duk
Ho Dong-Hwan
Lee Myoung-Jea
Seol Wongi
Kim Sang-Yun
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Abstract
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During recent years, there has been remarkable progress with respect to the identification of molecular mechanisms and underlying pathology of neurodegenerative dementias. The latest evidence indicates that a common cause and pathological mechanism of diverse neurodegenerative dementias can be found in the increased production, misfolding, aggregation, and accumulation of specific proteins such as β-amyloid, tau protein, α-synuclein, prion protein, polyglutamine, transactive response DNA-binding protein (TARDBP or TDP-43), or fused in sarcoma (FUS). The conformational variants of these proteins range from small oligomers to the characteristic pathologic inclusions. However, it is noteworthy that a certain pathology can be a hallmark of a certain dementia, but there is a substantial overlap between different pathologies and different types of dementias. In this review, molecular mechanisms and pathologies of different neurodegenerative dementias will be summarized from the perspective of proteins rather than from the viewpoint of individual dementias. We will also review recent evidence surrounding these protein misfolding disorders, the role of toxic oligomers, cell-to-cell transmission, and the links between the misfolded proteins, along with the general therapeutic strategies for the protein misfolding disorders.
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KEYWORD
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Neurodegenerative disorders, Protein misfolding disorders, Dementia
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