Protein Misfolding Diseases

Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation.- Ultrasensitive RT-QuIC Seed Amplification Assays for Disease-Associated Tau, α-Synuclein, and Prion Aggregates.- Vesicle-Based Assays to Study Membrane Interactions of Amyloid Peptides.- Differential Scanning Fluorimetry and Hydrogen Deuterium Exchange Mass Spectrometry to Monitor the Conformational Dynamics of NBD1 in Cystic Fibrosis.- A Multipronged Method for Unveiling Subtle Structural-Functional Defects of Mutant Chaperone Molecules Causing Human Chaperonopathies.- High-Throughput Microplate-Based Fluorescence Assays for Studying Stochastic Aggregation of Superoxide Dismutase-1.- Methods for Structural Analysis of Amyloid Fibrils in Misfolding Diseases.- Assays for Light Chain Amyloidosis Formation and Cytotoxicity.- Monitoring Aggregate Clearance and Formation in Cell-Based Assays.- Monitoring Proteome Stress in Live Cells Using HaloTag-Based Fluorogenic Sensor.- Quantification ofProtein Aggregates Using Bimolecular Fluorescence Complementation.- Screening Protein Aggregation in Cells Using Fluorescent Labels Coupled to Flow Cytometry.- Induction of Cu/Zn Superoxide Dismutase (SOD1) Aggregation in Living Cells.- A Cell Model for HSP60 Deficiencies: Modeling Different Levels of Chaperonopathies Leading to Oxidative Stress and Mitochondrial Dysfunction.- Super-Resolution Fluorescence Imaging of Mutant Huntingtin Aggregation in Cells.- Thermal Shift and Stability Assays of Disease-Related Misfolded Proteins Using Differential Scanning Fluorimetry.- Methods to Screen Compounds against Mutant p53 Misfolding and Aggregation for Cancer Therapeutics.- Early Stage Discovery and Validation of Pharmacological Chaperones for the Correction of Protein Misfolding Diseases.- Constructing Kinetically Controlled Denaturation Isotherms of Folded Proteins Using Denaturant-Pulse Chaperonin Binding.- In Vitro Prion Amplification Methodology for Inhibitor Screening.- SolubiS: Optimizing Protein Solubility by Minimal Point Mutations.