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referenced object 'cor1' cannot be found ID: PDF-HUL-149 ErrorMessage: edu.harvard.hul.ois.jhove.module.pdf.PdfInvalidException: Invalid indirect destination - referenced object 'cor1' cannot be found ID: PDF-HUL-122 Offset: 3285493 MIMEtype: application/pdf Profile: Linearized PDF PDFMetadata: Objects: 1202 FreeObjects: 1 IncrementalUpdates: 1 DocumentCatalog: PageLayout: SinglePage PageMode: UseOutlines Language: en Outlines: Item: Title: MIA40 circumvents the folding constraints imposed by TRIAP1 function Destination: titlink1 Children: Item: Title: Results Destination: flink1 Children: Item: Title: TRIAP1 sequence intrinsic properties differ from that of canonic MIA40 substrates Destination: slink1 Item: Title: TRIAP1 disulfide reduction leads to partially folded species Destination: slink2 Item: Title: Reduced TRIAP1 resembles a molten globule Destination: slink3 Item: Title: Equilibrium denaturation of the molten globule state of reduced TRIAP1 Destination: slink4 Item: Title: TRIAP1 air-oxidizes to spontaneously attain its native folded state Destination: slink5 Item: Title: Disulfide-pairing analysis of TRIAP1 folding intermediates i, i1, and i2 Destination: slink6 Item: Title: Molten globule state of reduced TRIAP1 favors the accumulation of an off-pathway folding kinetic trap Destination: slink7 Item: Title: MIA40 funnels the oxidative folding of TRIAP1, bypassing the kinetic trap Destination: slink8 Item: Title: Discussion Destination: flink2 Item: Title: Experimental procedures Destination: flink3 Children: Item: Title: Proteins expression and purification Destination: slink9 Item: Title: Oxidative folding and reductive unfolding experiments Destination: slink10 Item: Title: Far-UV CD and fluorescence spectroscopy Destination: slink11 Item: Title: NMR measurements Destination: slink12 Item: Title: Urea equilibrium denaturation fit to two-state model Destination: slink13 Item: Title: Disulfide scrambling Destination: slink14 Item: Title: Disulfide-bond content and disulfide pairing analysis of the major intermediates of oxidative folding and reductive unfoldi ... Destination: slink15 Item: Title: Stop/Go folding and Mia40-catalyzed reaction of Cys18-Cys37 TRIAP1 intermediate Destination: slink16 Item: Title: MALDI-TOF analyses Destination: slink17 Item: Title: Data availability Destination: flink4 Item: Title: Supporting information Destination: flink18 Item: Title: Author contributions Destination: flink5 Item: Title: Funding and additional information Destination: flink6 Item: Title: References Destination: blink1 Info: Title: MIA40 circumvents the folding constraints imposed by TRIAP1 function Author: Jordi Pujols Subject: Journal of Biological Chemistry, 301 (2025) 108268. doi:10.1016/j.jbc.2025.108268 Creator: Elsevier Producer: Acrobat Distiller 8.1.0 (Windows) CreationDate: Sat Mar 29 10:45:49 CET 2025 ModDate: Sat Mar 29 10:48:02 CET 2025 ID: 0x4c2dcd145cae5821d6a041057e229cfe, 0x3669b44616f6564ab5a12657b64256a2 Filters: FilterPipeline: FlateDecode FilterPipeline: DCTDecode Images: Image: NisoImageMetadata: FormatName: image/png 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FontName: HAHKDD+AdvP4C4E46 Flags: Symbolic FontBBox: 13, -2359, 999, 40 FontFile3: true EncodingDictionary: Differences: true ToUnicode: true Font: BaseFont: HAGKKG+AdvOT46dcae81 FontSubset: true FirstChar: 37 LastChar: 225 FontDescriptor: FontName: HAGKKG+AdvOT46dcae81 Flags: Nonsymbolic FontBBox: -41, -250, 833, 875 FontFile3: true Encoding: WinAnsiEncoding Font: BaseFont: HAHKEE+AdvOTf0bf83d5.I+20 FontSubset: true FirstChar: 151 LastChar: 151 FontDescriptor: FontName: HAHKEE+AdvOTf0bf83d5.I+20 Flags: Nonsymbolic FontBBox: -218, -218, 1052, 812 FontFile3: true Encoding: WinAnsiEncoding XMP: application/pdf doi:10.1016/j.jbc.2025.108268 MIA40 circumvents the folding constraints imposed by TRIAP1 function Jordi Pujols Marc Fornt-Suñé Marcos Gil-García Andrea Bartolomé-Nafría Francesc Canals Linda Cerofolini Kaare Teilum Lucia Banci Sebastián A. Esperante Salvador Ventura oxidative folding folding intermediates TRIAP1 MIA40 pathway molten globule disorder-to-order transition Journal of Biological Chemistry, 301 (2025) 108268. doi:10.1016/j.jbc.2025.108268 The Authors journal Journal of Biological Chemistry © 2025 The Authors. 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