ArticleMolecules (Basel, Switzerland)2022
Degradation-Suppressed Cocoonase for Investigating the Propeptide-Mediated Activation Mechanism.
Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 5 citations in OpenAlex.
- Structural and Catalytic Roles of the Disulfide Bonds Cys19-Cys154 and Cys134-Cys199 in Trypsin-like Proteases: Evolutionary Insights for Disulfide Bond Acquisition.Molecules (Basel, Switzerland) · 2026Article
- Molecular, Structural and Functional Characterization of Antheraea mylitta Expressed Cocoonase: An Integrative Approach.The protein journal · 2025Article
- Impression of Insect's Proteolytic Enzyme Cocoonase and Its Application: A Comprehensive Review.The protein journal · 2025Review
- Mutational Analysis of Substrate Recognition in Trypsin-like Protease Cocoonase: Protein Memory Induced by Alterations in Substrate-Binding Site.Molecules (Basel, Switzerland) · 2024Article
- The Cell Adhesion Activity of the Joining Peptide of Proopiomelanocortin.Molecules (Basel, Switzerland) · 2023Article
- A Novel Peptide Reagent for Investigating Disulfide-Coupled Folding Intermediates of Mid-Size Proteins.Molecules (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cocoonase is folded in the form of a zymogen precursor protein (prococoonase) with the assistance of the propeptide region. To investigate the role of the propeptide sequence on the disulfide-coupled folding of cocoonase and prococoonase, the amino acid residues at the degradation sites during the refolding and auto-processing reactions were determined by mass spectrometric analyses and were mutated to suppress the numerous degradation reactions that occur during the reactions. In addition, the Lys
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Registered trials
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