91f2bb6903bf051213e2212406da82c2 miccelfac_a2015v14p174.pdf 2713ddbaa094725a2c5dacd3c7e6dff14e4483ea miccelfac_a2015v14p174.pdf 2ba1ea43d00b1a1a10b9b659d838398737d6066816b69c70996cf91e26297f49 miccelfac_a2015v14p174.pdf Title: Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria Subject: Microbial Cell Factories, doi:10.1186/s12934-015-0361-y Keywords: Mammalian prions; Protein aggregation; Protein conformation; Inclusion bodies; Amyloids; E. coli Author: Bruno Macedo Creator: Springer Producer: Acrobat Distiller 10.1.8 (Windows); modified using iText® 5.3.5 ©2000-2012 1T3XT BVBA (AGPL-version) CreationDate: Tue Nov 3 14:44:02 2015 CET ModDate: Wed Nov 4 16:13:19 2015 CET Tagged: no UserProperties: no Suspects: no Form: AcroForm JavaScript: no Pages: 16 Encrypted: no Page size: 595.276 x 793.701 pts Page rot: 0 File size: 4007626 bytes Optimized: no PDF version: 1.6 name type encoding emb sub uni object ID 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Rel. 1.12.1 (2019-04-17) LastModified: 2020-07-07 13:32:39 CEST Size: 4007626 Format: PDF Version: 1.6 Status: Well-Formed and valid SignatureMatches: PDF-hul MIMEtype: application/pdf PDFMetadata: Objects: 1389 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: ViewerPreferences: HideToolbar: false HideMenubar: false HideWindowUI: false FitWindow: false CenterWindow: false DisplayDocTitle: false NonFullScreenPageMode: UseNone Direction: L2R ViewArea: CropBox ViewClip: CropBox PrintArea: CropBox PageClip: CropBox PageLayout: SinglePage PageMode: UseOutlines Language: EN Outlines: Item: Title: Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria Children: Item: Title: Abstract Children: Item: Title: Background: Item: Title: Results: Item: Title: Conclusions: Item: Title: Background Item: Title: Results and discussion Children: Item: Title: Aggregation of PrPWT and PrP90–231 into IBs in bacteria Item: Title: PrPWT and PrP90–231 form β-sheet enriched IBs Item: Title: Stability of PrPs IBs towards chemical denaturation Item: Title: PrPWT and PrP90–231 IBs bind to thioflavin-S in living cells Item: Title: Amyloid properties of PrPWT and PrP90–231 IBs Item: Title: Amyloid morphology of PrPs IBs Item: Title: Amyloid seeding capacity of PrPWT IBs Item: Title: PrPs IBs display a proteinase K resistant core Item: Title: Conclusions Item: Title: Methods Children: Item: Title: Prion proteins expression and purification Item: Title: PrPWT and PrP90–231 IBs extraction Item: Title: Secondary structure determination Item: Title: Congo red binding Item: Title: Thioflavin T (Th-T) binding assay Item: Title: Thioflavin-S binding in living cells Item: Title: Chemical denaturation Item: Title: Transmission electron microscopy (TEM) Item: Title: In vitro conversion of PrP into amyloid fibrils Item: Title: Seeding assays Item: Title: Confocal microscopy and image processing Item: Title: Proteinase K (PK) resistance assay Item: 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