Laura A. Volpicelli‐Daley

This paper shows that a second-generation hypoxia-in-a-pill treatment rescues neurodegenerative phenotypes in multiple mouse models.

This study shows that α-synuclein aggregates in corticostriatal terminals impair glutamatergic transmission without causing neurodegeneration.

This paper develops a method to generate human midbrain organoids enriched in SNpc-like dopaminergic neurons using WNT modulation and bioreactor culture, showing improved functionality and vulnerability to Parkinson's disease pathology.

This study shows that Parkin is essential for neuronal differentiation and survival, and small molecule Parkin agonists like FB231 protect dopaminergic neurons in Parkinson's disease models.

This study shows formic acid treatment reduces α-synuclein seeding activity in fixed brain samples from humans and mice without compromising histopathological quality.

This study shows that myeloid FtH deficiency worsens kidney injury by promoting ferroptosis through Snca and Spic, linking iron trafficking to macrophage dysfunction.

This study shows that aggregated α-synuclein impairs corticostriatal synaptic function and reduces synaptic density in mice, with some synapses showing increased volume.

This study links phosphoproteome modifications to cortical circuit dysfunction in early-stage alpha-synuclein aggregation using multi-omics analysis in rat and mouse models.

This study investigates whether enhancing cathepsin D or disrupting ZKSCAN3 in the CNS can reduce α-synuclein aggregation and dopaminergic neurodegeneration, but finds no significant effect.

This study investigates how α-synuclein aggregates in the basolateral amygdala affect synaptic structure and function in a mouse model of Parkinson's disease.

This study identifies excitatory synapses as primary targets of α-synuclein aggregation in a Parkinson's disease mouse model, revealing spatial and temporal patterns of synaptic vulnerability.

This paper shows SIRT3 levels decrease with age and in Parkinson's disease, and over-expression of SIRT3 reduces α-synuclein aggregation, supporting AAV.SIRT3-myc as a potential therapy.

This study shows that the GBA1 L444P mutation increases glucosylsphingosine levels and hippocampal alpha-synuclein inclusions in mice, contributing to synucleinopathy pathology.

This study shows that inhibiting LRRK2 kinase activity increases α-synuclein presynaptic localization and anterograde axonal transport in neurons.

This study shows Rab27a/b knockout prevents alpha-synuclein aggregation, toxicity, and cell-to-cell transmission in vitro and in vivo.