Beyond Folding Enzymes: A Redox-Active "Solid Chaperone" Unlocks Recyclable, HPLC-Free Oxidative Protein Folding.

Shunpei Iwamoto, Yuya Nishizawa, Hayato Yokose, Osamu Kanie, Yosuke Okamura, Takahiro Muraoka, Kenta Arai

Abstract read

In one paragraph

Article in JACS Au, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Shunpei IwamotoDepartment of Chemistry, School of Science, Tokai University, 4-1-1 Kitakaname, Hiratsuka-Shi, Kanagawa 259-1292, Japan.

Yuya NishizawaDepartment of Chemistry, School of Science, Tokai University, 4-1-1 Kitakaname, Hiratsuka-Shi, Kanagawa 259-1292, Japan.

Hayato YokoseCourse of Science and Technology, Graduate School of Science and Technology, Tokai University, 4-1-1 Kitakaname, Hiratsuka-Shi, Kanagawa 259-1292, Japan.

Osamu KanieDepartment of Bioengineering, School of Engineering, Tokai University, 4-1-1 Kitakaname, Hiratsuka-Shi, Kanagawa 259-1292, Japan.ORCID https://orcid.org/0000-0003-4147-6868

Yosuke OkamuraCourse of Science and Technology, Graduate School of Science and Technology, Tokai University, 4-1-1 Kitakaname, Hiratsuka-Shi, Kanagawa 259-1292, Japan.ORCID https://orcid.org/0000-0002-8811-9377

Takahiro MuraokaDepartment of Applied Chemistry, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-Cho, Koganei, Tokyo 184-8588, Japan.

Kenta AraiDepartment of Chemistry, School of Science, Tokai University, 4-1-1 Kitakaname, Hiratsuka-Shi, Kanagawa 259-1292, Japan.ORCID https://orcid.org/0000-0003-0785-2559

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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

Indexed as

enzyme modelsheterogeneous catalysismaterials scienceprotein disulfide isomeraseprotein foldingseleniumsustainable chemistry

Identifiers

PMID41755826

DOI10.1021/jacsau.5c01572

PMCPMC12933366

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.