{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["6(2)"],"submitter":["Iwamoto S"],"pubmed_abstract":["Oxidative protein folding, which is critical to proteins achieving their functional structures, is catalyzed in cells by protein disulfide isomerase (PDI)an enzyme that couples redox catalysis with the transient capture of folding intermediates to promote native disulfide formation while preventing aggregation. Although PDI improves oxidative folding in both chemically synthesized and recombinantly produced proteins, its use is restricted to homogeneous systems, limiting reusability and operational robustness. Artificial PDI mimics have advanced <i>in vitro</i> folding; however, no system has yet combined sufficient redox activity for native disulfide formation with a folding environment that suppresses aggregation, nor demonstrated true reusability. Here, we introduce a polymer-based \"so"],"journal":["JACS Au"],"pagination":["1197-1205"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12933366"],"repository":["biostudies-literature"],"pubmed_title":["Beyond Folding Enzymes: A Redox-Active \"Solid Chaperone\" Unlocks Recyclable, HPLC-Free Oxidative Protein Folding."],"pmcid":["PMC12933366"],"pubmed_authors":["Yokose H","Nishizawa Y","Kanie O","Okamura Y","Muraoka T","Arai K","Iwamoto S"],"additional_accession":[]},"is_claimable":false,"name":"Beyond Folding Enzymes: A Redox-Active \"Solid Chaperone\" Unlocks Recyclable, HPLC-Free Oxidative Protein Folding.","description":"Oxidative protein folding, which is critical to proteins achieving their functional structures, is catalyzed in cells by protein disulfide isomerase (PDI)an enzyme that couples redox catalysis with the transient capture of folding intermediates to promote native disulfide formation while preventing aggregation. Although PDI improves oxidative folding in both chemically synthesized and recombinantly produced proteins, its use is restricted to homogeneous systems, limiting reusability and operational robustness. Artificial PDI mimics have advanced <i>in vitro</i> folding; however, no system has yet combined sufficient redox activity for native disulfide formation with a folding environment that suppresses aggregation, nor demonstrated true reusability. Here, we introduce a polymer-based \"so","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-16T22:58:29.246Z","creation":"2026-07-12T03:09:43.679Z"},"accession":"S-EPMC12933366","cross_references":{"pubmed":["41755826"],"doi":["10.1021/jacsau.5c01572"]}}