发布求助
文献互助 智能选刊 最新文献

Prions - Some Physiological and Pathophysiological Aspects最新文献

筛选
英文 中文
Introductory Chapter: Prions 导论:朊病毒
Prions - Some Physiological and Pathophysiological Aspects Pub Date : 2018-12-26 DOI: 10.5772/INTECHOPEN.82716
I. Sirakov
{"title":"Introductory Chapter: Prions","authors":"I. Sirakov","doi":"10.5772/INTECHOPEN.82716","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.82716","url":null,"abstract":"","PeriodicalId":433646,"journal":{"name":"Prions - Some Physiological and Pathophysiological Aspects","volume":"175 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-12-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"133445570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Prion Proteins and Neuronal Death in the Cerebellum 朊蛋白与小脑神经元死亡
Prions - Some Physiological and Pathophysiological Aspects Pub Date : 2018-11-05 DOI: 10.5772/INTECHOPEN.80701
A. Ragagnin, Qili Wang, A. Guillemain, Siaka Dole, Anne-Sophie Wilding, V. Demais, C. Royer, A. Haeberlé, N. Vitale, S. Gasman, N. Grant, Y. Bailly
{"title":"Prion Proteins and Neuronal Death in the Cerebellum","authors":"A. Ragagnin, Qili Wang, A. Guillemain, Siaka Dole, Anne-Sophie Wilding, V. Demais, C. Royer, A. Haeberlé, N. Vitale, S. Gasman, N. Grant, Y. Bailly","doi":"10.5772/INTECHOPEN.80701","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.80701","url":null,"abstract":"The cellular prion protein, a major player in the neuropathology of prion diseases, is believed to control both death and survival pathways in central neurons. However, the cellular and molecular mechanisms underlying these functions remain to be deciphered. This chapter presents cytopathological studies of the neurotoxic effects of infectious prions and cellular prion protein-deficiency on cerebellar neurons in wild-type and transgenic mice. The immunochemical and electron microscopy data collected in situ and ex vivo in cultured organotypic cerebellar slices indicate that an interplay between apoptotic and autophagic pathways is involved in neuronal death induced either by the infectious prions or by prion protein-deficiency.","PeriodicalId":433646,"journal":{"name":"Prions - Some Physiological and Pathophysiological Aspects","volume":"89 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"123138948","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Prion Protein Strain Diversity and Disease Pathology 朊蛋白品系多样性与疾病病理学
Prions - Some Physiological and Pathophysiological Aspects Pub Date : 2018-11-05 DOI: 10.5772/INTECHOPEN.80702
Saima Zafar, N. Younas, M. Shafiq, I. Zerr
{"title":"Prion Protein Strain Diversity and Disease Pathology","authors":"Saima Zafar, N. Younas, M. Shafiq, I. Zerr","doi":"10.5772/INTECHOPEN.80702","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.80702","url":null,"abstract":"The infectious agents, prions, are composed mainly of conformational isomers of the cellular prion protein (PrPc) in its abnormal accumulated scrapie forms (PrPSc). The distinct prion isolates or strains have been associated with different PrPSc prion protein conformations and patterns of glycosylation and are associated with disease progression and severity. In humans, sporadic Creutzfeldt-Jakob disease (sCJD) is the most common form and has been divided into six subtypes, based on PrPSc electrophoretic mobility and allelic variation at codon 129, among which sCJD MM1 and sCJD VV2 are the two most commonly occurring subtypes with known clinical manifestations. The strain-specific response of PrPSc suggests both the molecular classification and the pathogenesis of prion diseases along with posttranslational modification of PrP in humans and animals.","PeriodicalId":433646,"journal":{"name":"Prions - Some Physiological and Pathophysiological Aspects","volume":"49 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"126269891","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 4
A Molecular Mechanism for Abnormal Prion Protein Accumulation 异常朊蛋白积累的分子机制
Prions - Some Physiological and Pathophysiological Aspects Pub Date : 2018-11-05 DOI: 10.5772/INTECHOPEN.78951
K. Uchiyama, S. Sakaguchi
{"title":"A Molecular Mechanism for Abnormal Prion Protein Accumulation","authors":"K. Uchiyama, S. Sakaguchi","doi":"10.5772/INTECHOPEN.78951","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.78951","url":null,"abstract":"A fundamental event in the pathogenesis of prion disease is the conversion of cellular prion protein into an abnormally folded isoform (PrP Sc ), which is the infectious causative agent of disease. With progression of disease, PrP Sc is replicated and excessively accumulated in most cases. However, the molecular mechanism for excessive accumulation of PrP Sc is not well understood. Recently, Sortilin, a member of the VPS10P domain receptor family, has been identified as a sorting receptor that directs prion protein (PrP) to the lysosomal degradation pathway. Moreover, it has been shown that prion infection impairs Sortilin function, resulting in delayed PrP Sc degradation. In this chapter, we explain the mechanisms for PrP trafficking into the lysosomal degradation pathway mediated by Sortilin and overaccumulation of PrP Sc caused by Sortilin dysfunction.","PeriodicalId":433646,"journal":{"name":"Prions - Some Physiological and Pathophysiological Aspects","volume":"291 2","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"120879003","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整，为了账户安全，请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
请完成安全验证×
相关产品
×
本文献相关产品
联系我们：info@booksci.cn Book学术提供免费学术资源搜索服务，方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号：481959085
Book学术官方微信