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| 001 | 136016 | ||
| 005 | 20240321220011.0 | ||
| 024 | 7 | _ | |a pmid:19767654 |2 pmid |
| 024 | 7 | _ | |a 1467-3037 |2 ISSN |
| 024 | 7 | _ | |a 1467-3045 |2 ISSN |
| 037 | _ | _ | |a DZNE-2020-02338 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Miesbauer, Margit |0 P:(DE-2719)9000214 |b 0 |e First author |
| 245 | _ | _ | |a Targeting of the prion protein to the cytosol: mechanisms and consequences. |
| 260 | _ | _ | |a Wymondham, Norfolk |c 2010 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1709562736_22645 |2 PUB:(DE-HGF) |x Review Article |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Prion 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. |
| 536 | _ | _ | |a 342 - Disease Mechanisms and Model Systems (POF3-342) |0 G:(DE-HGF)POF3-342 |c POF3-342 |f POF III |x 0 |
| 588 | _ | _ | |a Dataset connected to PubMed, |
| 650 | _ | 7 | |a Glycosylphosphatidylinositols |2 NLM Chemicals |
| 650 | _ | 7 | |a Prions |2 NLM Chemicals |
| 650 | _ | 2 | |a Animals |2 MeSH |
| 650 | _ | 2 | |a Cytosol: metabolism |2 MeSH |
| 650 | _ | 2 | |a Endoplasmic Reticulum: metabolism |2 MeSH |
| 650 | _ | 2 | |a Glycosylphosphatidylinositols: metabolism |2 MeSH |
| 650 | _ | 2 | |a Humans |2 MeSH |
| 650 | _ | 2 | |a Models, Biological |2 MeSH |
| 650 | _ | 2 | |a Prion Diseases: genetics |2 MeSH |
| 650 | _ | 2 | |a Prion Diseases: metabolism |2 MeSH |
| 650 | _ | 2 | |a Prions: genetics |2 MeSH |
| 650 | _ | 2 | |a Prions: metabolism |2 MeSH |
| 650 | _ | 2 | |a Protein Transport: genetics |2 MeSH |
| 650 | _ | 2 | |a Protein Transport: physiology |2 MeSH |
| 700 | 1 | _ | |a Rambold, Angelika S |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Winklhofer, Konstanze F |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Tatzelt, Jörg |0 P:(DE-HGF)0 |b 3 |
| 773 | _ | _ | |g Vol. 12, no. 2 |0 PERI:(DE-600)2090836-2 |n 2 |q 12:2 |p 10.21775/cimb.012.109 |t Current issues in molecular biology |v 12 |y 2010 |x 1467-3037 |
| 856 | 4 | _ | |u https://www.mdpi.com/1467-3045/12/2/00109 |
| 856 | 4 | _ | |u https://pub.dzne.de/record/136016/files/DZNE-2020-02338.pdf |
| 856 | 4 | _ | |u https://pub.dzne.de/record/136016/files/DZNE-2020-02338.pdf?subformat=pdfa |x pdfa |
| 909 | C | O | |p VDB |o oai:pub.dzne.de:136016 |
| 910 | 1 | _ | |a Deutsches Zentrum für Neurodegenerative Erkrankungen |0 I:(DE-588)1065079516 |k DZNE |b 0 |6 P:(DE-2719)9000214 |
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| 914 | 1 | _ | |y 2010 |
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