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Prion protein oligomer and its neurotoxicity
Huang, Pei ; Lian, Fulin ; Wen, Yi ; Guo, Chenyun ; Lin, Donghai ; Guo CY(郭晨云) ; Lin DH(林东海)
刊名http://dx.doi.org/10.1093/abbs/gmt037
2013
关键词MOLTEN GLOBULE INTERMEDIATE NUCLEAR-MAGNETIC-RESONANCE AMYLOID-BETA OLIGOMERS ALPHA-LACTALBUMIN IN-VITRO PEPTIDE AGGREGATION MISFOLDING DISEASES CARBONIC-ANHYDRASE ALZHEIMERS-DISEASE FOLDING PATHWAY
英文摘要National Natural Science Foundation of China [31170717, 91129713, 30900233]; The prion diseases, also known as transmissible spongiform encephalopathies, are fatal neurodegenerative disorders. According to the protein only hypothesis, the key molecular event in the pathogenesis of prion disease is the conformational conversion of the host-derived cellular prion protein (PrPC) into a misfolded form (scrapie PrP, PrPSc). Increasing evidence has shown that the most infectious factor is the smaller subfibrillar oligomers formed by prion proteins. Both the prion oligomer and PrPSc are rich in -sheet structure and resistant to the proteolysis of proteinase K. The prion oligomer is soluble in physiologic environments whereas PrPSc is insoluble. Various prion oligomers are formed in different conditions. Prion oligomers exhibited more neurotoxicity both in vitro and in vivo than the fibrillar forms of PrPSc, implying that prion oligomers could be potential drug targets for attacking prion diseases. In this article, we describe recent experimental evidence regarding prion oligomers, with a special focus on prion oligomer formation and its neurotoxicity.
语种英语
出版者OXFORD UNIV PRESS
内容类型期刊论文
源URL[http://dspace.xmu.edu.cn/handle/2288/89023]  
专题化学化工-已发表论文
推荐引用方式
GB/T 7714
Huang, Pei,Lian, Fulin,Wen, Yi,et al. Prion protein oligomer and its neurotoxicity[J]. http://dx.doi.org/10.1093/abbs/gmt037,2013.
APA Huang, Pei.,Lian, Fulin.,Wen, Yi.,Guo, Chenyun.,Lin, Donghai.,...&林东海.(2013).Prion protein oligomer and its neurotoxicity.http://dx.doi.org/10.1093/abbs/gmt037.
MLA Huang, Pei,et al."Prion protein oligomer and its neurotoxicity".http://dx.doi.org/10.1093/abbs/gmt037 (2013).
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