ReviewMolecules (Basel, Switzerland)2021
Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments.
Review in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Metal-Responsive Up-Regulation of Bifunctional Disulfides for Suppressing Protein Misfolding and Promoting Oxidative Folding.Angewandte Chemie (International ed. in English) · 2025Article
- Oxidative Folding of a Two-Chain Protein Having Three Interchain Disulfide Bonds. Synthesis of Bromelain Inhibitor VI Through Native Chain Assembly.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Seleno-relaxin analogues: effect of internal and external diselenide bonds on the foldability and a fibrosis-related factor of endometriotic stromal cells.RSC chemical biology · 2024Article
- Diselenide-bond replacement of the external disulfide bond of insulin increases its oligomerization leading to sustained activity.Communications chemistry · 2023Article
- Semi-enzymatic acceleration of oxidative protein folding byChemical science · 2023Article
- Cysteine Redox Chemistry in Peptide Self-Assembly to Modulate Hydrogelation.Molecules (Basel, Switzerland) · 2023Article
- Cysteine-based protein folding modulators for trapping intermediates and misfolded forms.RSC advances · 2022Article
- Survey of the Intermolecular Disulfide Bonds Observed in Protein Crystal Structures Deposited in the Protein Data Bank.Life (Basel, Switzerland) · 2022Article
- Article
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2 authors.
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Abstract
In the last few decades, development of novel experimental techniques, such as new types of disulfide (SS)-forming reagents and genetic and chemical technologies for synthesizing designed artificial proteins, is opening a new realm of the oxidative folding study where peptides and proteins can be folded under physiologically more relevant conditions. In this review, after a brief overview of the historical and physicochemical background of oxidative protein folding study, recently revealed folding pathways of several representative peptides and proteins are summarized, including those having two, three, or four SS bonds in the native state, as well as those with odd Cys residues or consisting of two peptide chains. Comparison of the updated pathways with those reported in the early years has revealed the flexible nature of the protein folding pathways. The significantly different pathways characterized for hen-egg white lysozyme and bovine milk α-lactalbumin, which belong to the same protein superfamily, suggest that the information of protein folding pathways, not only the native folded structure, is encoded in the amino acid sequence. The application of the flexible pathways of peptides and proteins to the engineering of folded three-dimensional structures is an interesting and important issue in the new realm of the current oxidative protein folding study.
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