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000136016 0247_ $$2ISSN$$a1467-3037
000136016 0247_ $$2ISSN$$a1467-3045
000136016 037__ $$aDZNE-2020-02338
000136016 041__ $$aEnglish
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000136016 1001_ $$0P:(DE-2719)9000214$$aMiesbauer, Margit$$b0$$eFirst author
000136016 245__ $$aTargeting of the prion protein to the cytosol: mechanisms and consequences.
000136016 260__ $$aWymondham, Norfolk$$c2010
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000136016 520__ $$aPrion diseases are characterized by the conformational transition of the cellular prion protein (PrP(C)) into an aberrant protein conformer, designated scrapie-prion protein (PrP(Sc)). A causal link between protein misfolding and neurodegeneration has been established for a variety of neurodegenerative disease, such as Alzheimer's disease, Parkinson's disease and polyglutamine diseases, but there is an ongoing debate about the nature of the neurotoxic species and how non-native conformers can damage neuronal populations. PrP is normally imported into the endoplasmic reticulum (ER) and targeted to the outer leaflet of the plasma membrane via a glycosylphosphatidylinositol (GPI) anchor. However, several conditions, such as ER stress or some pathogenic mutations in the PrP gene, can induce the mislocalization of PrP in the cytosol, where it has a neurotoxic potential as demonstrated in cell culture and transgenic mouse models. In this review we focus on intrinsic factors and cellular pathways implicated in the import of PrP into the ER and its mistargeting to the cytosol. The findings summarized here not only reveal a complex regulation of the biogenesis of PrP, but also provide interesting new insight into toxic activities of pathogenic protein conformers and quality control pathways of ER-targeted proteins.
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000136016 650_7 $$2NLM Chemicals$$aGlycosylphosphatidylinositols
000136016 650_7 $$2NLM Chemicals$$aPrions
000136016 650_2 $$2MeSH$$aAnimals
000136016 650_2 $$2MeSH$$aCytosol: metabolism
000136016 650_2 $$2MeSH$$aEndoplasmic Reticulum: metabolism
000136016 650_2 $$2MeSH$$aGlycosylphosphatidylinositols: metabolism
000136016 650_2 $$2MeSH$$aHumans
000136016 650_2 $$2MeSH$$aModels, Biological
000136016 650_2 $$2MeSH$$aPrion Diseases: genetics
000136016 650_2 $$2MeSH$$aPrion Diseases: metabolism
000136016 650_2 $$2MeSH$$aPrions: genetics
000136016 650_2 $$2MeSH$$aPrions: metabolism
000136016 650_2 $$2MeSH$$aProtein Transport: genetics
000136016 650_2 $$2MeSH$$aProtein Transport: physiology
000136016 7001_ $$0P:(DE-HGF)0$$aRambold, Angelika S$$b1
000136016 7001_ $$0P:(DE-HGF)0$$aWinklhofer, Konstanze F$$b2
000136016 7001_ $$0P:(DE-HGF)0$$aTatzelt, Jörg$$b3
000136016 773__ $$0PERI:(DE-600)2090836-2$$gVol. 12, no. 2$$n2$$p10.21775/cimb.012.109$$q12:2$$tCurrent issues in molecular biology$$v12$$x1467-3037$$y2010
000136016 8564_ $$uhttps://www.mdpi.com/1467-3045/12/2/00109
000136016 8564_ $$uhttps://pub.dzne.de/record/136016/files/DZNE-2020-02338.pdf
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000136016 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)9000214$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b0$$kDZNE
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000136016 9141_ $$y2010
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