Daryl A. Bosco

Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules.

Genetic determinants of amyotrophic lateral sclerosis as therapeutic targets.

Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS.

Amyotrophic lateral sclerosis-linked FUS/TLS alters stress granule assembly and dynamics.

Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis.

Functions of FUS/TLS from DNA repair to stress response: implications for ALS.

Structural basis for mutation-induced destabilization of profilin 1 in ALS.

ALS-linked FUS exerts a gain of toxic function involving aberrant p38 MAPK activation.

Translation dysregulation in neurodegenerative disorders.

The RNA-binding protein FUS/TLS undergoes calcium-mediated nuclear egress during excitotoxic stress and is required for mRNA processing.

Interactions between ALS-linked FUS and nucleoporins are associated with defects in the nucleocytoplasmic transport pathway.

ALS-linked PFN1 variants exhibit loss and gain of functions in the context of formin-induced actin polymerization.

Excessive release of inorganic polyphosphate by ALS/FTD astrocytes causes non-cell-autonomous toxicity to motoneurons.

Anti-SOD1 Nanobodies That Stabilize Misfolded SOD1 Proteins Also Promote Neurite Outgrowth in Mutant SOD1 Human Neurons.

Interactions between FUS and the C-terminal Domain of Nup62 are Sufficient for their Co-phase Separation into Amorphous Assemblies.