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

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

10.1371/journal.pbio.1002338

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Bibliographic Details
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
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Institution:	National University of Singapore

Description
Summary:	10.1371/journal.pbio.1002338