ReviewMolecules (Basel, Switzerland)2020
Revisiting the Formation of a Native Disulfide Bond: Consequences for Protein Regeneration and Beyond.
Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Disulfidptosis and its molecular mechanisms in cancer: mechanisms, regulation, and therapeutic potential.Medical oncology (Northwood, London, England) · 2026Review
- Approaches to deorphanize secretome: Classical, computational, and next generation strategies to reveal ligand-receptor networks.EXO : beyond the cell · 2026Article
- 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
- Redox regulation: mechanisms, biology and therapeutic targets in diseases.Signal transduction and targeted therapy · 2025Review
- Review
- Protein aggregation and biomolecular condensation in hypoxic environments (Review).International journal of molecular medicine · 2024Review
- Article
- Mechanism of Reduced Glutathione Induced Lysozyme Defolding and Molecular Self-Assembly.Foods (Basel, Switzerland) · 2023Article
- Host and viral proteins involved in SARS-CoV-2 infection differentially bind heme.Protein science : a publication of the Protein Society · 2022Article
- Article
- The Formation of Native Disulfide Bonds: Treading a Fine Line in Protein Folding.The protein journal · 2021Review
- Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments.Molecules (Basel, Switzerland) · 2021Review
- A systematic structural comparison of all solved small proteins deposited in PDB. The effect of disulfide bonds in protein fold.Computational and structural biotechnology journal · 2021Article
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Authors and funding
1 author.
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Abstract
Oxidative protein folding involves the formation of disulfide bonds and the regeneration of native structure (N) from the fully reduced and unfolded protein (R). Oxidative protein folding studies have provided a wealth of information on underlying physico-chemical reactions by which disulfide-bond-containing proteins acquire their catalytically active form. Initially, we review key events underlying oxidative protein folding using bovine pancreatic ribonuclease A (RNase A), bovine pancreatic trypsin inhibitor (BPTI) and hen-egg white lysozyme (HEWL) as model disulfide bond-containing folders and discuss consequential outcomes with regard to their folding trajectories. We re-examine the findings from the same studies to underscore the importance of forming native disulfide bonds and generating a "native-like" structure early on in the oxidative folding pathway. The impact of both these features on the regeneration landscape are highlighted by comparing ideal, albeit hypothetical, regeneration scenarios with those wherein a native-like structure is formed relatively "late" in the R→N trajectory. A special case where the desired characteristics of oxidative folding trajectories can, nevertheless, stall folding is also discussed. The importance of these data from oxidative protein folding studies is projected onto outcomes, including their impact on the regeneration rate, yield, misfolding, misfolded-flux trafficking from the endoplasmic reticulum (ER) to the cytoplasm, and the onset of neurodegenerative disorders.
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