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

Volumn 14, Issue 1, 2016, Pages

  Lim, Liangzhong ^a   Wei, Yuanyuan ^b   Lu, Yimei ^a   Song, Jianxing ^a,b  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

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;

EID: 84956713967     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1002338     Document Type: Article

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