Francesca Tonelli

The paper identifies PPM1M as a phosphatase that reverses LRRK2-mediated Rab phosphorylation and links a rare mutation to Parkinson's disease.

The paper shows that LRRK2 kinase inhibitor treatment restores cilia, Hedgehog signaling, neuroprotective factors, and dopamine processes in Parkinson's linked-LRRK2 mutant mice striatum.

The paper shows that VPS13C senses lysosome damage, relocates to lysosomes, and tethers them to the ER, suggesting a protective lipid transport response.

This study shows LRRK2 and PINK1 function in parallel neuroprotective pathways affecting ciliogenesis in Parkinson's disease, suggesting shared therapeutic targets.

The paper shows that LRRK2 mutations cause loss of primary cilia and Neurturin in striatal Parvalbumin interneurons, impairing neuroprotective signaling.

The paper shows that loss of primary cilia in specific striatal cell types reduces dopaminergic neuroprotection in Parkinson's disease, linked to impaired Hedgehog signaling.

This study shows that the VPS35[D620N] mutation causes lysosomal dysfunction, activates LRRK2, and promotes the lysosomal association of RILPL1 and TMEM55B through phosphorylation of Rab proteins.

This study evaluates 100 LRRK2 variants linked to Parkinson's disease, identifying those that enhance kinase activity and microtubule binding, and highlights their implications for clinical trials.

The paper identifies mtDNA damage as a blood-based biomarker for Parkinson's disease, showing increased levels in early-stage patients and mutation carriers, suggesting its potential for patient stratification in clinical trials.

The paper develops and validates a multiplexed mass spectrometry assay to quantify LRRK2-phosphorylated Rab proteins and biomarker sites, showing VPS35[D620N] enhances Rab1 phosphorylation in Parkinson's disease.