Using mass spectrometry-based methods to understand amyloid formation and inhibition of alpha-synuclein and amyloid beta

Keyphrases

• Mass Spectrometry 100%
• Amyloid beta 100%
• Alpha-synuclein (α-syn) 100%
• Amyloid Formation 100%
• Amyloid Inhibition 100%
• Approaches to Studying 40%
• High-resolution 40%
• Spatial Resolution 40%
• Amyloid Fibrils 40%
• Ion Mobility 40%
• Hydrogen/deuterium Exchange 40%
• Sheet Structure 20%
• Amino Acids 20%
• Small Molecules 20%
• Protein Misfolding 20%
• Protein Aggregation 20%
• Chemical Cross-linking 20%
• Structural Change 20%
• Fluorescence Method 20%
• Higher-order Structure 20%
• Protein Footprinting 20%
• Oligomeric 20%
• Labeling Method 20%
• Native Mass Spectrometry 20%
• Resolution Approach 20%
• Fast Photochemical Oxidation of Proteins 20%
• ThT Fluorescence 20%
• Gas-phase Ions 20%
• Cross-linking Mass Spectrometry 20%
• Polymorph 20%
• Amyloid Fibrillation 20%
• β-synuclein 20%
• Neurodegenerative Disorders 20%

Biochemistry, Genetics and Molecular Biology

• Mass Spectrometry 100%
• Amyloid Beta 100%
• Alpha-Synuclein 100%
• Amyloid Protein 100%
• Cross-Link 28%
• Hydrogen-Deuterium Exchange 28%
• Amino Acids 14%
• Protein Misfolding 14%
• Small Molecule 14%
• Conformation 14%
• Protein Aggregation 14%
• Beta-Synuclein 14%

Chemistry

• Mass Spectrometry 100%
• Beta-Amyloid 100%
• formation 100%
• Amyloid Fibril 42%
• Ion Mobility 28%
• Deuterium 28%
• Hydrogen 28%
• Fluorescence Method 14%
• Photochemical Oxidation 14%
• Amino Acid 14%
• Protein Aggregation 14%