Evidence map›Paper›PMID 41599399›Full record

ArticleMolecules (Basel, Switzerland)2026

Structural and Catalytic Roles of the Disulfide Bonds Cys19-Cys154 and Cys134-Cys199 in Trypsin-like Proteases: Evolutionary Insights for Disulfide Bond Acquisition.

Maiko Minakata, Yuri Murakami, Orika Ashida, Miki Matsuzaki, Kairi Ogawa, Nanako Saeki, Shigeru Shimamoto, Mitsuhiro Miyazawa, Yuji Hidaka, Nana Sakata

Abstract read
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In one paragraph

Article in Molecules (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
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

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Maiko MinakataFaculty of Science and Engineering, Kindai University, 3-4-1 Kowakae, Higashi-Osaka, Osaka 577-8502, Japan.
Yuri MurakamiFaculty of Science and Engineering, Kindai University, 3-4-1 Kowakae, Higashi-Osaka, Osaka 577-8502, Japan.
Orika AshidaFaculty of Science and Engineering, Kindai University, 3-4-1 Kowakae, Higashi-Osaka, Osaka 577-8502, Japan.
Miki MatsuzakiFaculty of Science and Engineering, Kindai University, 3-4-1 Kowakae, Higashi-Osaka, Osaka 577-8502, Japan.
Kairi OgawaFaculty of Science and Engineering, Kindai University, 3-4-1 Kowakae, Higashi-Osaka, Osaka 577-8502, Japan.
Nanako SaekiFaculty of Science and Engineering, Kindai University, 3-4-1 Kowakae, Higashi-Osaka, Osaka 577-8502, Japan.
Shigeru ShimamotoFaculty of Science and Engineering, Kindai University, 3-4-1 Kowakae, Higashi-Osaka, Osaka 577-8502, Japan.ORCID 0000-0002-9470-0352
Mitsuhiro MiyazawaInstitute of Agrobiological Sciences, National Agriculture and Food Research Organization, Tsukuba 305-8634, Japan.
Yuji HidakaFaculty of Science and Engineering, Kindai University, 3-4-1 Kowakae, Higashi-Osaka, Osaka 577-8502, Japan.ORCID 0000-0002-3131-2619
Nana SakataFaculty of Science and Engineering, Kindai University, 3-4-1 Kowakae, Higashi-Osaka, Osaka 577-8502, Japan.

Funding

Japan Society for the Promotion of Science 24KJ2163Japan Society for the Promotion of Science 25K08952
6 · The paper itself

Abstract

Trypsin is one of the most extensively studied enzymes in biochemistry. However, little information is available on the role of the disulfide bonds to establish the correct conformation and enzyme activity during molecular evolution. To obtain this information, two additional disulfide bonds corresponding to those found in human trypsin were individually or simultaneously introduced into the trypsin-like protease cocoonase (

Indexed as

CysteineDisulfidesSerine EndopeptidasesTrypsinAmino Acid SequenceAnimalsCatalysisEvolution, MolecularHumansKineticsModels, MolecularProtein ConformationSubstrate SpecificityCysteineDisulfidesSerine EndopeptidasesTrypsintrypsin-like serine proteasedenaturationdisulfidefoldingmolecular evolutionmutation

Identifiers

PMID41599399
PMCPMC12844481

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

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.