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| 001 | 140086 | ||
| 005 | 20240321220735.0 | ||
| 024 | 7 | _ | |a 1069-5524 |2 ISSN |
| 024 | 7 | _ | |a 10.1128/MCB.00111-18 |2 doi |
| 024 | 7 | _ | |a pmid:29784771 |2 pmid |
| 024 | 7 | _ | |a pmc:PMC6048315 |2 pmc |
| 024 | 7 | _ | |a 0270-7306 |2 ISSN |
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| 024 | 7 | _ | |a 1069-5524 |2 ISSN |
| 037 | _ | _ | |a DZNE-2020-06408 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Dürnberger, Yvonne |0 P:(DE-2719)2810519 |b 0 |e First author |u dzne |
| 245 | _ | _ | |a Prion Replication in the Mammalian Cytosol: Functional Regions within a Prion Domain Driving Induction, Propagation, and Inheritance. |
| 260 | _ | _ | |a Washington, DC |c 2018 |b Soc. |
| 264 | _ | 1 | |3 online |2 Crossref |b American Society for Microbiology |c 2018-07-16 |
| 264 | _ | 1 | |3 print |2 Crossref |b American Society for Microbiology |c 2018-05-21 |
| 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 1590753255_15073 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Prions of lower eukaryotes are transmissible protein particles that propagate by converting homotypic soluble proteins into growing protein assemblies. Prion activity is conferred by so-called prion domains, regions of low complexity that are often enriched in glutamines and asparagines (Q/N). The compositional similarity of fungal prion domains with intrinsically disordered domains found in many mammalian proteins raises the question of whether similar sequence elements can drive prion-like phenomena in mammals. Here, we define sequence features of the prototype Saccharomyces cerevisiae Sup35 prion domain that govern prion activities in mammalian cells by testing the ability of deletion mutants to assemble into self-perpetuating particles. Interestingly, the amino-terminal Q/N-rich tract crucially important for prion induction in yeast was dispensable for the prion life cycle in mammalian cells. Spontaneous and template-assisted prion induction, growth, and maintenance were preferentially driven by the carboxy-terminal region of the prion domain that contains a putative soft amyloid stretch recently proposed to act as a nucleation site for prion assembly. Our data demonstrate that preferred prion nucleation domains can differ between lower and higher eukaryotes, resulting in the formation of prions with strikingly different amyloid cores. |
| 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 CrossRef, PubMed, |
| 650 | _ | 7 | |a Peptide Termination Factors |2 NLM Chemicals |
| 650 | _ | 7 | |a Prion Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Prions |2 NLM Chemicals |
| 650 | _ | 7 | |a Protein Aggregates |2 NLM Chemicals |
| 650 | _ | 7 | |a Recombinant Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a SUP35 protein, S cerevisiae |2 NLM Chemicals |
| 650 | _ | 7 | |a Saccharomyces cerevisiae Proteins |2 NLM Chemicals |
| 650 | _ | 2 | |a Amino Acid Sequence |2 MeSH |
| 650 | _ | 2 | |a Animals |2 MeSH |
| 650 | _ | 2 | |a Binding Sites |2 MeSH |
| 650 | _ | 2 | |a Cell Line |2 MeSH |
| 650 | _ | 2 | |a Cytosol: metabolism |2 MeSH |
| 650 | _ | 2 | |a Mice |2 MeSH |
| 650 | _ | 2 | |a Models, Molecular |2 MeSH |
| 650 | _ | 2 | |a Mutation |2 MeSH |
| 650 | _ | 2 | |a Peptide Termination Factors: biosynthesis |2 MeSH |
| 650 | _ | 2 | |a Peptide Termination Factors: chemistry |2 MeSH |
| 650 | _ | 2 | |a Peptide Termination Factors: genetics |2 MeSH |
| 650 | _ | 2 | |a Prion Proteins: biosynthesis |2 MeSH |
| 650 | _ | 2 | |a Prion Proteins: chemistry |2 MeSH |
| 650 | _ | 2 | |a Prion Proteins: genetics |2 MeSH |
| 650 | _ | 2 | |a Prions: biosynthesis |2 MeSH |
| 650 | _ | 2 | |a Prions: chemistry |2 MeSH |
| 650 | _ | 2 | |a Prions: genetics |2 MeSH |
| 650 | _ | 2 | |a Protein Aggregates: genetics |2 MeSH |
| 650 | _ | 2 | |a Protein Aggregation, Pathological: genetics |2 MeSH |
| 650 | _ | 2 | |a Protein Aggregation, Pathological: metabolism |2 MeSH |
| 650 | _ | 2 | |a Protein Domains |2 MeSH |
| 650 | _ | 2 | |a Protein Folding |2 MeSH |
| 650 | _ | 2 | |a Recombinant Proteins: biosynthesis |2 MeSH |
| 650 | _ | 2 | |a Recombinant Proteins: chemistry |2 MeSH |
| 650 | _ | 2 | |a Recombinant Proteins: genetics |2 MeSH |
| 650 | _ | 2 | |a Saccharomyces cerevisiae Proteins: biosynthesis |2 MeSH |
| 650 | _ | 2 | |a Saccharomyces cerevisiae Proteins: chemistry |2 MeSH |
| 650 | _ | 2 | |a Saccharomyces cerevisiae Proteins: genetics |2 MeSH |
| 650 | _ | 2 | |a Sequence Deletion |2 MeSH |
| 693 | _ | _ | |0 EXP:(DE-2719)IDAF-20190308 |5 EXP:(DE-2719)IDAF-20190308 |e Image and Data Analysis Facility (CRFS-IDAF) / Bonn |x 0 |
| 700 | 1 | _ | |a Liu, Shu |0 P:(DE-2719)2810461 |b 1 |u dzne |
| 700 | 1 | _ | |a Riemschoß, Katrin |0 P:(DE-2719)2811067 |b 2 |u dzne |
| 700 | 1 | _ | |a Paulsen, Lydia |0 P:(DE-2719)2651099 |b 3 |u dzne |
| 700 | 1 | _ | |a Bester, Romina |b 4 |
| 700 | 1 | _ | |a Kuhn, Peer-Hendrik |0 P:(DE-2719)2810327 |b 5 |u dzne |
| 700 | 1 | _ | |a Schölling, Manuel |0 P:(DE-2719)2810990 |b 6 |u dzne |
| 700 | 1 | _ | |a Lichtenthaler, Stefan F |0 P:(DE-2719)2181459 |b 7 |u dzne |
| 700 | 1 | _ | |a Vorberg, Ina |0 P:(DE-2719)2481765 |b 8 |u dzne |
| 773 | 1 | 8 | |a 10.1128/mcb.00111-18 |b : American Society for Microbiology, 2018-05-21 |n 15 |3 journal-article |2 Crossref |t Molecular and Cellular Biology |v 38 |y 2018 |x 0270-7306 |
| 773 | _ | _ | |a 10.1128/MCB.00111-18 |g Vol. 38, no. 15, p. e00111-18/mcb/38/15/e00111-18.atom |0 PERI:(DE-600)1474919-1 |n 15 |q 38:15 |t Molecular and cellular biology |v 38 |y 2018 |x 0270-7306 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6048315 |
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| 913 | 1 | _ | |a DE-HGF |b Forschungsbereich Gesundheit |l Erkrankungen des Nervensystems |1 G:(DE-HGF)POF3-340 |0 G:(DE-HGF)POF3-342 |2 G:(DE-HGF)POF3-300 |v Disease Mechanisms and Model Systems |x 0 |
| 914 | 1 | _ | |y 2018 |
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| 920 | 1 | _ | |0 I:(DE-2719)1013004 |k AG Vorberg |l Prion Cell Biology |x 0 |
| 920 | 1 | _ | |0 I:(DE-2719)1110006 |k AG Lichtenthaler |l Neuroproteomics |x 1 |
| 920 | 1 | _ | |0 I:(DE-2719)1040200 |k IDAF |l Image and Data Analysis (IDAF) |x 2 |
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