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prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation Destination: title_link Children: Item: Title: Results Destination: A1 Children: Item: Title: Human PrLDs with predicted coiled-coil domains overlap with polyQ tracts Destination: B1 Item: Title: MED15 contains an N-terminal Q-rich coiled-coil PrLD Destination: B2 Item: Title: MED15 interactors are predicted to have coiled-coil domains Destination: B3 Item: Title: Soluble MED15-PrLD characterization Destination: B4 Item: Title: MED15-PrLD aggregates into β-sheet enriched amyloid-like fibrillar structures Destination: B5 Item: Title: MED15-PrLD aggregation kinetics Destination: B6 Item: Title: MED15-PrLD aggregation is governed by its coiled-coil conformation Destination: B7 Item: Title: MED15-PrLD forms insoluble cytoplasmic inclusions in mammalian cells and kidnaps the endogenous protein Destination: B8 Item: Title: Discussion Destination: A2 Item: Title: Methods Destination: A3 Children: Item: Title: Bioinformatics analysis Destination: B9 Item: Title: MED15’sequences Destination: B10 Item: Title: Protein expression and purification Destination: B11 Item: Title: Size exclusion chromatography Destination: B12 Item: Title: Native page Destination: B13 Item: Title: Dynamic light scattering Destination: B14 Item: Title: GFP absorption Destination: B15 Item: Title: Protein aggregation Destination: B16 Item: Title: GFP fluorescence Destination: B17 Item: Title: Synchronous light scattering Destination: B18 Item: Title: Congo Red precipitation Destination: B19 Item: Title: Circular Dichroism Destination: B20 Item: Title: Fourier transform infrared spectroscopy Destination: B21 Item: Title: Transmission electron microscopy Destination: B22 Item: Title: Mammalian molecular cloning Destination: B23 Item: Title: Mammalian cell culture Destination: B24 Item: Title: Production of lentivirus and infection of recipient cells Destination: B25 Item: Title: Mammalian cells transfection Destination: B26 Item: Title: Immunofluorescence Destination: B27 Item: Title: Soluble/insoluble fractionation Destination: B28 Item: Title: Nuclear/cytoplasmic fractionation Destination: B29 Item: Title: Statistics and reproducibility Destination: B30 Item: Title: Reporting summary Destination: A4 Item: Title: Data availability Destination: M1 Item: Title: References Destination: A5 Item: Title: Acknowledgements Destination: A6 Item: Title: Author contributions Destination: A7 Item: Title: Competing interests Destination: A8 Item: Title: Additional information Destination: M3 Info: Title: MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation Author: Cristina Batlle Subject: Communications Biology, doi:10.1038/s42003-021-01930-8 Keywords: Creator: Springer Producer: iText® 5.3.5 ©2000-2012 1T3XT BVBA (SPRINGER SBM; licensed version) CreationDate: Sat Mar 20 04:48:15 CET 2021 ModDate: Mon Mar 22 11:48:53 CET 2021 ID: 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