ArticleThe Journal of biological chemistry2012
Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathway.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Prion propagation is controlled by discrete structural regions of PrP rather than overall stability.The Journal of biological chemistry · 2026Article
- Practical Real-Time Quaking-Induced Conversion for Detecting Classical Bovine Spongiform Encephalopathy and Classical and Atypical Scrapie Prions.Pathogens (Basel, Switzerland) · 2026Article
- Persistence of Methionine Side Chain Mobility at Low Temperatures in a Nine-Residue Low Complexity Peptide, as Probed byChemphyschem : a European journal of chemical physics and physical chemistry · 2024Article
- Copper drives prion protein phase separation and modulates aggregation.Science advances · 2023Article
- Methionine Sulfoxide Reductases Suppress the Formation of the [Antioxidants (Basel, Switzerland) · 2023Article
- Protein folding stabilities are a major determinant of oxidation rates for buried methionine residues.The Journal of biological chemistry · 2022Article
- Methionine oxidation within the prion protein.Prion · 2020Review
- Oxidative and Inflammatory Events in Prion Diseases: Can They Be Therapeutic Targets?Current aging science · 2019Review
- Unique methionine-aromatic interactions govern the calmodulin redox sensor.Biochemical and biophysical research communications · 2018Article
- Characterizing the conformational landscape of MDM2-binding p53 peptides using Molecular Dynamics simulations.Scientific reports · 2017Article
- Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.PLoS genetics · 2017Article
- Spectroscopic and Theoretical Study of Cu(I) Binding to His111 in the Human Prion Protein Fragment 106-115.Inorganic chemistry · 2016Article
- Unfolded Protein Response and Macroautophagy in Alzheimer's, Parkinson's and Prion Diseases.Molecules (Basel, Switzerland) · 2015Review
- Redox control of protein degradation.Redox biology · 2015Review
- Oxidative stress conditions increase the frequency of de novo formation of the yeast [PSI+] prion.Molecular microbiology · 2015Article
- Conformation-dependent epitopes recognized by prion protein antibodies probed using mutational scanning and deep sequencing.Journal of molecular biology · 2015Article
- Impact of methionine oxidation on calmodulin structural dynamics.Biochemical and biophysical research communications · 2015Article
- Review
- Redox-sensitive residue in the actin-binding interface of myosin.Biochemical and biophysical research communications · 2014Article
- Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins.Exercise and sport sciences reviews · 2014Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Oxidative stress and misfolding of the prion protein (PrP(C)) are fundamental to prion diseases. We have therefore probed the effect of oxidation on the structure and stability of PrP(C). Urea unfolding studies indicate that H(2)O(2) oxidation reduces the thermodynamic stability of PrP(C) by as much as 9 kJ/mol. (1)H-(15)N NMR studies indicate methionine oxidation perturbs key hydrophobic residues on one face of helix-C as follows: Met-205, Val-209, and Met-212 together with residues Val-160 and Tyr-156. These hydrophobic residues pack together and form the structured core of the protein, stabilizing its ternary structure. Copper-catalyzed oxidation of PrP(C) causes a more significant alteration of the structure, generating a monomeric molten globule species that retains its native helical content. Further copper-catalyzed oxidation promotes extended β-strand structures that lack a cooperative fold. This transition from the helical molten globule to β-conformation has striking similarities to a misfolding intermediate generated at low pH. PrP may therefore share a generic misfolding pathway to amyloid fibers, irrespective of the conditions promoting misfolding. Our observations support the hypothesis that oxidation of PrP destabilizes the native fold of PrP(C), facilitating the transition to PrP(Sc). This study gives a structural and thermodynamic explanation for the high levels of oxidized methionine in scrapie isolates.
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