Lin E. Guo

The paper engineers chimeric proteins to replace ALS-causing FUS and TDP-43, improving neuronal health by reducing aggregation and restoring nuclear functions.

This study develops a human neuronal model with the TDP-43 A315T mutation to study ALS-related protein dysfunction and therapeutic responses.

This study identifies RNA G-quadruplexes as tunable regulators of FUS phase separation, showing they can inhibit or nucleate aggregation depending on structure and concentration.

This study shows DNA damage induces alternative splicing of RIF1, generating isoforms that affect DNA repair complex assembly and phase separation.

This study shows that injecting human FUS fibrils into mice with human FUS causes FUS aggregation and FTLD-like disease progression, with prion-like spread and cognitive deficits.

This study shows that Kapβ2 protein interacts with poly(GR) and reduces its neurotoxicity in C9orf72-linked ALS/FTD by improving neuron survival.

The paper identifies heterozygous frameshift variants in hnRNPA2B1 causing early-onset oculopharyngeal muscular dystrophy by altering nucleocytoplasmic transport.

The paper characterizes HNRNPA1 mutations in patients with neurodegenerative diseases, showing varied effects on fibrillization, phase separation, and stress granule dynamics.

The paper shows stress induces TDP-43 nuclear bodies via NEAT1-promoted phase separation, which protects cells from toxicity and is disrupted by an ALS mutation.