Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion
Published 2013 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion
Authors
Keywords
-
Journal
Prion
Volume 7, Issue 5, Pages 404-411
Publisher
Informa UK Limited
Online
2013-10-12
DOI
10.4161/pri.26745
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Multiple Substitutions of Methionine 129 in Human Prion Protein Reveal Its Importance in the Amyloid Fibrillation Pathway
- (2012) Sofie Nyström et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Methionine Oxidation Perturbs the Structural Core of the Prion Protein and Suggests a Generic Misfolding Pathway
- (2012) Nadine D. Younan et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Polyglutamine misfolding in yeast: Toxic and protective aggregation
- (2012) Martin L. Duennwald Prion
- Modulating protein activity and cellular function by methionine residue oxidation
- (2011) Zong Jie Cui et al. AMINO ACIDS
- Methionine Oxidation of Sup35 Protein Induces Formation of the [PSI+] Prion in a Yeast Peroxiredoxin Mutant
- (2011) Theodora C. Sideri et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- A Diversity of Assembly Mechanisms of a Generic Amyloid Fold
- (2011) Timo Eichner et al. MOLECULAR CELL
- In vivo demonstration that -synuclein oligomers are toxic
- (2011) B. Winner et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Amyloid in neurodegenerative diseases: Friend or foe?
- (2011) Katie J. Wolfe et al. SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
- Methionine-Oxidized Amyloid Fibrils Are Poor Substrates for Human Methionine Sulfoxide Reductases A and B2
- (2010) Katrina J. Binger et al. BIOCHEMISTRY
- Assessing the Role of Oxidized Methionine at Position 213 in the Formation of Prions in Hamsters
- (2010) Christopher J. Silva et al. BIOCHEMISTRY
- The structural intolerance of the PrP α-fold for polar substitution of the helix-3 methionines
- (2010) Silvia Lisa et al. CELLULAR AND MOLECULAR LIFE SCIENCES
- A causative link between the structure of aberrant protein oligomers and their toxicity
- (2010) Silvia Campioni et al. Nature Chemical Biology
- UV-light-induced conversion and aggregation of prion proteins
- (2009) Lars Redecke et al. FREE RADICAL BIOLOGY AND MEDICINE
- Peptide NMHRYPNQ of the Cellular Prion Protein (PrPC) Inhibits Aggregation and Is a Potential Key for Understanding Prion–Prion Interactions
- (2009) Dirk Rehders et al. JOURNAL OF MOLECULAR BIOLOGY
- Methionine Sulfoxides on Prion Protein Helix-3 Switch on the α-Fold Destabilization Required for Conversion
- (2009) Giorgio Colombo et al. PLoS One
- Folding kinetics of the human prion protein probed by temperature jump
- (2009) T. Hart et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein
- (2009) C. Wolschner et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Methionine Sulfoxides on PrPSc: A Prion-Specific Covalent Signature†
- (2008) Tamar Canello et al. BIOCHEMISTRY
- Proline-directed Pseudo-phosphorylation at AT8 and PHF1 Epitopes Induces a Compaction of the Paperclip Folding of Tau and Generates a Pathological (MC-1) Conformation
- (2008) Sadasivam Jeganathan et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Therapeutic Strategies for Alzheimer’s Disease
- (2008) Donna M. Barten et al. MOLECULAR NEUROBIOLOGY
- Molecular Model of an α-Helical Prion Protein Dimer and Its Monomeric Subunits as Derived from Chemical Cross-linking and Molecular Modeling Calculations
- (2007) T. Kaimann et al. JOURNAL OF MOLECULAR BIOLOGY
Become a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get StartedAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started