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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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

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spelling	sg-nus-scholar.10635-1653872024-11-15T20:15:58Z ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43 Lim L. Wei Y. Lu Y. Song J. BIOLOGICAL SCIENCES 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 amyotrophic lateral sclerosis genetic procedures genetics human metabolism mutation 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 10.1371/journal.pbio.1002338 PLoS Biology 14 1 e1002338 2020-03-13T05:23:50Z 2020-03-13T05:23:50Z 2016 Article Lim L., Wei Y., Lu Y., Song J. (2016). ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. PLoS Biology 14 (1) : e1002338. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pbio.1002338 15449173 https://scholarbank.nus.edu.sg/handle/10635/165387 Public Library of Science Unpaywall 20200320
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	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 amyotrophic lateral sclerosis genetic procedures genetics human metabolism mutation 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
spellingShingle	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 amyotrophic lateral sclerosis genetic procedures genetics human metabolism mutation 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 Lim L. Wei Y. Lu Y. Song J. ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43
description	10.1371/journal.pbio.1002338
author2	BIOLOGICAL SCIENCES
author_facet	BIOLOGICAL SCIENCES Lim L. Wei Y. Lu Y. Song J.
format	Article
author	Lim L. Wei Y. Lu Y. Song J.
author_sort	Lim L.
title	ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43
title_short	ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43
title_full	ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43
title_fullStr	ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43
title_full_unstemmed	ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43
title_sort	als-causing mutations significantly perturb the self-assembly and interaction with nucleic acid of the intrinsically disordered prion-like domain of tdp-43
publisher	Public Library of Science
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/165387
_version_	1821234644791590912

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

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