ReviewAnnual review of chemical and biomolecular engineering2016
Thiol-Disulfide Exchange Reactions in the Mammalian Extracellular Environment.
Review in Annual review of chemical and biomolecular engineering, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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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.
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.
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Who cites it
48 citing papers in PubMed.
- Did diet compliance and remission reduce oxidative stress in celiac patients?Revista da Associacao Medica Brasileira (1992) · 2024Trial
- Effects of different preoxygenation strategies on dynamic thiol-disulfide homeostasis and blood gas parameters in patients undergoing laparoscopic cholecystectomy.Perioperative medicine (London, England) · 2026Article
- Endoplasmic Reticulum Redoxome: Protein Folding and Beyond.Biochemistry · 2026Review
- Enhancing effects of diphenyl diselenide and β-hydroxy β-methylbutyrate combined with exercise on neuroprotection, memory, mitochondrial function, muscle function, and inflammation regulation in older adults and age-related diseases.Frontiers in nutrition · 2026Review
- Design of cationic ionizable lipids for the delivery of therapeutic nucleic acids.Molecular therapy. Methods & clinical development · 2025Review
- Ketoboronate as a Minimal Covalent-Reversible Tag for Targeted Lysosomal Degradation of Extracellular and Membrane Proteins.Journal of the American Chemical Society · 2025Article
- Gadolinium-Conjugated Lipoic Acid Hydrogels for Magnetic Resonance Imaging.ACS applied bio materials · 2025Article
- Structure and post-translational modification of the prostaglandin transporter.Communications biology · 2025Article
- New Ibuprofen Cystamine Salts With Improved Solubility and Anti-Inflammatory Effect.ChemistryOpen · 2024Article
- Conserved residues of the immunosuppressive domain of MLV are essential for regulating the fusion-critical SU-TM disulfide bond.Journal of virology · 2024Article
- A platform for mapping reactive cysteines within the immunopeptidome.Nature communications · 2024Article
- Analytical Methods for Assessing Thiol Antioxidants in Biological Fluids: A Review.Molecules (Basel, Switzerland) · 2024Review
- Investigating the relationship between lymphocyte cells apoptosis and DNA damage and oxidative stress and therapeutic and clinical outcomes of COVID-19 elderly patients.BMC infectious diseases · 2024Article
- Cyclization increases bactericidal activity of arginine-rich cationic cell-penetrating peptide forMicrobiology spectrum · 2024Article
- Modification of extracellular matrix proteins by oxidants and electrophiles.Biochemical Society transactions · 2024Review
- Sulfinamide Crossover Reaction.The Journal of organic chemistry · 2024Article
- Unraveling redox pathways of the disulfide bond in dimethyl disulfide: Ab initio modeling.Journal of molecular modeling · 2024Review
- Assessment of CRISPRa-mediatedFrontiers in bioengineering and biotechnology · 2024Article
- Synthesis and glutathione peroxidase (GPx)-like activity of selenocystine (SeC) bioconjugates of biotin and lipoic acid.Amino acids · 2023Article
- Degradation Kinetics of Disulfide Cross-Linked Microgels: Real-Time Monitoring by Confocal Microscopy.Gels (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Disulfide bonds represent versatile posttranslational modifications whose roles encompass the structure, catalysis, and regulation of protein function. Due to the oxidizing nature of the extracellular environment, disulfide bonds found in secreted proteins were once believed to be inert. This notion has been challenged by the discovery of redox-sensitive disulfides that, once cleaved, can lead to changes in protein activity. These functional disulfides are twisted into unique configurations, leading to high strain and potential energy. In some cases, cleavage of these disulfides can lead to a gain of function in protein activity. Thus, these motifs can be referred to as switches. We describe the couples that control redox in the extracellular environment, examine several examples of proteins with switchable disulfides, and discuss the potential applications of disulfides in molecular biology.
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Registered trials
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.