ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43

• Main Authors: Lim L., Wei Y., Lu Y., Song J.
• Other Authors: BIOLOGICAL SCIENCES
• Format: Article
• Published: Public Library of Science 2020
• Subjects: amyloid; intrinsically disordered protein; mutant protein; nucleic acid; oligomer; TAR DNA binding protein; DNA binding protein; TDP-43 protein, human; amyotrophic lateral sclerosis; aqueous solution; Article; beta sheet; circular dichroism; electron microscopy; fluorescence spectroscopy; membrane; mutation; neurotoxicity; nuclear magnetic resonance spectroscopy; protein aggregation; protein analysis; protein assembly; protein conformation; protein domain; protein interaction; protein secondary structure; wild type; genetic procedures; genetics; human; metabolism; pH; protein tertiary structure; Amyotrophic Lateral Sclerosis; Circular Dichroism; DNA-Binding Proteins; Humans; Hydrogen-Ion Concentration; Microscopy, Electron; Molecular Probe Techniques; Mutation; Nucleic Acids; Protein Structure, Tertiary
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/165387
• Institution: National University of Singapore

10.1371/journal.pbio.1002338