ArticleJournal of the American Chemical Society2016
Conformational-Sensitive Fast Photochemical Oxidation of Proteins and Mass Spectrometry Characterize Amyloid Beta 1-42 Aggregation.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Design and commissioning of a new synchrotron beamline dedicated to X-ray footprinting mass spectrometry.Journal of synchrotron radiation · 2026Article
- Capturing Early Aggregation Transitions of Disordered Tau by Covalent Footprinting Mass Spectrometry.Analytical chemistry · 2026Article
- Recommendations and considerations for hydroxyl radical protein footprinting-mass spectrometry.Nature methods · 2026Review
- State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025Review
- High-Throughput Screening of Amyloid Inhibitors via Covalent-Labeling Mass Spectrometry.Analytical chemistry · 2025Article
- Mass-Spectrometry-Based GEE Footprinting Characterizes Kinetic Mechanisms and Sites of Conformational Change in Amyloid β 1-42 Aggregation.ACS chemical neuroscience · 2025Article
- Quantitative readout of methionine residue solvent accessibility in E. coli cells using radiolytic hydroxyl radical labeling and mass spectrometry.Biochemical and biophysical research communications · 2025Article
- Mass Spectrometry-Based Protein Footprinting for Protein Structure Characterization.Accounts of chemical research · 2025Article
- Using in vivo intact structure for system-wide quantitative analysis of changes in proteins.Nature communications · 2024Article
- Exploration of Resveratrol as a Potent Modulator of α-Synuclein Fibril Formation.ACS chemical neuroscience · 2024Article
- Mass spectrometric insights into protein aggregation.Essays in biochemistry · 2023Review
- Oxidative Damages on the Alzheimer's Related-Aβ Peptide Alters Its Ability to Assemble.Antioxidants (Basel, Switzerland) · 2023Article
- A Hybrid Structural Method for Investigating Low Molecular Weight Oligomeric Structures of Amyloid Beta.Chembiochem : a European journal of chemical biology · 2022Article
- In-Cell Labeling and Mass Spectrometry for Systems-Level Structural Biology.Chemical reviews · 2022Review
- Distinguishing Histidine Tautomers in Proteins Using Covalent Labeling-Mass Spectrometry.Analytical chemistry · 2022Article
- Bacteriophage-encoded lethal membrane disruptors: Advances in understanding and potential applications.Frontiers in microbiology · 2022Review
- Pulsed Hydrogen-Deuterium Exchange Reveals Altered Structures and Mechanisms in the Aggregation of Familial Alzheimer's Disease Mutants.ACS chemical neuroscience · 2021Article
- Protein Footprinting via Covalent Protein Painting Reveals Structural Changes of the Proteome in Alzheimer's Disease.Journal of proteome research · 2021Article
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Structural Proteomics Methods to Interrogate the Conformations and Dynamics of Intrinsically Disordered Proteins.Frontiers in chemistry · 2021Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Preventing and treating Alzheimer's disease require understanding the aggregation of amyloid beta 1-42 (Aβ1-42) to give oligomers, protofibrils, and fibrils. Here we describe footprinting of Aβ1-42 by hydroxyl radical-based fast photochemical oxidation of proteins (FPOP) and mass spectrometry (MS) to monitor the time-course of Aβ1-42 aggregation. We resolved five distinct stages characterized by two sigmoidal behaviors, showing the time-dependent transitions of monomers-paranuclei-protofibrils-fibrillar aggregates. Kinetic modeling allows deciphering the amounts and interconversion of the dominant Aβ1-42 species. Moreover, the irreversible footprinting probe provides insights into the kinetics of oligomerization and subsequent fibrillar growth by allowing the conformational changes of Aβ1-42 at subregional and even amino-acid-residue levels to be revealed. The middle domain of Aβ1-42 plays a major role in aggregation, whereas the N-terminus retains most of its solvent-accessibility during aggregation, and the hydrophobic C-terminus is involved to an intermediate extent. This approach affords an in situ, real-time monitoring of the solvent accessibility of Aβ1-42 at various stages of oligomerization, and provides new insights on site-specific aggregation of Aβ1-42 for a sample state beyond the capabilities of most other biophysical methods.
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