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TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA | PNAS
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Frontiers | A C-Terminally Truncated TDP-43 Splice Isoform Exhibits Neuronal Specific Cytoplasmic Aggregation and Contributes to TDP-43 Pathology in ALS
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Structural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation | Scientific Reports
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Frontiers | Expanding the TDP-43 Proteinopathy Pathway From Neurons to Muscle: Physiological and Pathophysiological Functions
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Domain structures and assembly of TDP-43 proteins. (A) TDP-43 has two... | Download Scientific Diagram
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Pleiotropic requirements for human TDP-43 in the regulation of cell and organelle homeostasis | Life Science Alliance
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Frontiers | Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
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IJMS | Free Full-Text | The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils
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Why TDP-43? Why Not? Mechanisms of Metabolic Dysfunction in Amyotrophic Lateral Sclerosis - Mara-Luciana Floare, Scott P. Allen, 2020
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Representation of the protein domain structure of TDP-43 and FUS. The... | Download Scientific Diagram
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ALS-linked TDP-43 mutations interfere with the recruitment of RNA recognition motifs to G-quadruplex RNA | Scientific Reports
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Pathogenic Mutation of TDP-43 Impairs RNA Processing in a Cell Type-Specific Manner: Implications for the Pathogenesis of ALS/FTLD | eNeuro
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The role of TDP-43 mislocalization in amyotrophic lateral sclerosis | Molecular Neurodegeneration | Full Text
A. Schematic representation of the primary structural architecture of... | Download Scientific Diagram
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