ArticlePloS one2014
Oxidation enhances human serum albumin thermal stability and changes the routes of amyloid fibril formation.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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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.
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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
17 citing papers in PubMed.
- Micro/Nanoplastics Drive Amyloid‑β Colloidal and Oxidative Reorganization: A Real-World Contaminant Stressor.ACS omega · 2026Article
- Is uric acid a true antioxidant? Identification of uric acid oxidation products and their biological effects.Redox report : communications in free radical research · 2025Review
- Coomassie Brilliant Blue Induces Coiled-Coil Aggregation in Lysozyme at pH 7.4 by Hydrophobic and Electrostatic Forces.ACS omega · 2025Article
- Molecular Serum Albumin Unmask Nanobio Properties of Molecular Graphenes in Shungite Carbon Nanoparticles.International journal of molecular sciences · 2024Article
- Zwitterionic polymers-armored amyloid-like protein surface combats thrombosis and biofouling.Bioactive materials · 2024Article
- Altered Thermal Behavior of Blood Plasma Proteome Related to Inflammatory Cytokines in Early Pregnancy Loss.International journal of molecular sciences · 2022Article
- A Comprehensive Investigation of Interactions between Antipsychotic Drug Quetiapine and Human Serum Albumin Using Multi-Spectroscopic, Biochemical, and Molecular Modeling Approaches.Molecules (Basel, Switzerland) · 2022Article
- Modulation of amyloid fibrillation of bovine β-lactoglobulin by selective methionine oxidation.RSC advances · 2021Article
- Aging-Related and Gender Specific Albumin Misfolding in Alzheimer's Disease.Journal of Alzheimer's disease reports · 2020Article
- Pathogenesis of Molar Hypomineralisation: Aged Albumin Demarcates Chalky Regions of Hypomineralised Enamel.Frontiers in physiology · 2020Article
- Fatty acid transfer between serum albumins and shungite carbon nanoparticles and its effect on protein aggregation and association.European biophysics journal : EBJ · 2020Article
- Applicability of FTIR-ATR Method to Measure Carbonyls in Blood Plasma after Physical and Mental Stress.BioMed research international · 2019Article
- Quantitative Comparison of Protein Adsorption and Conformational Changes on Dielectric-Coated Nanoplasmonic Sensing Arrays.Sensors (Basel, Switzerland) · 2018Article
- Multi-site binding of epigallocatechin gallate to human serum albumin measured by NMR and isothermal titration calorimetry.Bioscience reports · 2017Article
- Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry.Analytical chemistry · 2017Article
- Article
- Tripping up Trp: Modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences.Free radical biology & medicine · 2015Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oxidative damages are linked to several aging-related diseases and are among the chemical pathways determining protein degradation. Specifically, interplay of oxidative stress and protein aggregation is recognized to have a link to the loss of cellular function in pathologies like Alzheimer's and Parkinson's diseases. Interaction between protein and reactive oxygen species may indeed induce small changes in protein structure and lead to the inhibition/modification of protein aggregation process, potentially determining the formation of species with different inherent toxicity. Understanding the temperate relationship between these events can be of utmost importance in unraveling the molecular basis of neurodegeneration. In this work, we investigated the effect of hydrogen peroxide oxidation on Human Serum Albumin (HSA) structure, thermal stability and aggregation properties. In the selected conditions, HSA forms fibrillar aggregates, while the oxidized protein undergoes aggregation via new routes involving, in different extents, specific domains of the molecule. Minute variations due to oxidation of single residues affect HSA tertiary structure leading to protein compaction, increased thermal stability, and reduced association propensity.
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