Prion-like C-Terminal Domain of TDP-43 and α-Synuclein Interact Synergistically to Generate Neurotoxic Hybrid Fibrils

Biophysical characteristics of lipid‐induced Aβ oligomers correlate to distinctive phenotypes in transgenic mice

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Granulins modulate liquid–liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43

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Polymorphic α-Synuclein Strains Modified by Dopamine and Docosahexaenoic Acid Interact Differentially with Tau Protein

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Tau interacts with the C-terminal region of α-synuclein, promoting formation of toxic aggregates with distinct molecular conformations

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The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD

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Patient-derived frontotemporal lobar degeneration brain extracts induce formation and spreading of TDP-43 pathology in vivo

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DOPAL derived alpha-synuclein oligomers impair synaptic vesicles physiological function

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Strain-specific Fibril Propagation by an Aβ Dodecamer

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ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain

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Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation

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Low molecular weight species of TDP-43 generated by abnormal splicing form inclusions in amyotrophic lateral sclerosis and result in motor neuron death

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Pathological Interface Between Oligomeric Alpha-Synuclein and Tau in Synucleinopathies

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Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

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Alpha-synuclein and tau: teammates in neurodegeneration?

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The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease

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Competitive Interactions of Ligands and Macromolecular Crowders with Maltose Binding Protein

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ALS-Associated TDP-43 Induces Endoplasmic Reticulum Stress, Which Drives Cytoplasmic TDP-43 Accumulation and Stress Granule Formation

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TDP-43 Potentiates Alpha-synuclein Toxicity to Dopaminergic Neurons in Transgenic Mice

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Epitope mapping of antibodies against TDP-43 and detection of protease-resistant fragments of pathological TDP-43 in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

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Molecular properties of TAR DNA binding protein-43 fragments are dependent upon its cleavage site

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TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1

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C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stress

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The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism

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Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer’s disease

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The structure of dopamine induced α-synuclein oligomers

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Molecular Cross Talk between Misfolded Proteins in Animal Models of Alzheimer's and Prion Diseases

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Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: A spectrum of TDP-43 proteinopathies

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Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies

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Cell death: protein misfolding and neurodegenerative diseases

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Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43

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TDP-43 is recruited to stress granules in conditions of oxidative insult

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Role of Synucleins in Alzheimer’s Disease

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Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

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Temporal lobar predominance of TDP-43 neuronal cytoplasmic inclusions in Alzheimer disease

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Enrichment of C-Terminal Fragments in TAR DNA-Binding Protein-43 Cytoplasmic Inclusions in Brain but not in Spinal Cord of Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

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Protein Misfolding and Neurodegeneration

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Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease

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