About Our Lab
The Mazzulli Lab is interested in determining how protein misfolding and amyloid formation results in cell death. Many chronic neurodegenerative disorders such as Parkinson’s and Alzheimer’s disease are characterized by the accumulation of misfolded proteins within the nervous system. We use patient neurons derived from induced pluripotent stem cells (iPSC) coupled with analytic biochemical techniques to study protein accumulation and lysosomal clearance mechanisms.
Please join us for Parkinson's Disease Gordon Research Conference: "Pathogenesis, Pathophysiology and Experimental Therapeutics in Parkinson's Disease" in Newry ME, June 23-28, 2019. https://www.grc.org/parkinson-s-disease-conference/2019/
Zunke F, et al. Reversible Conformational Conversion of α-Synuclein into Toxic Assemblies by Glucosylceramide. Neuron, Jan 3rd, 2018. 97(1), 92-107e10. PMID:29290548
Mazzulli JR, et al. Activation of b-Glucocerebrosidase Reduces Pathological a-Synuclein and Restores Lysosomal Function in Parkinson’s Patient Midbrain Neurons, J. Neurosci, Jul 20, 2016. 36(29):7693-706. PMID: 27445146
Mazzulli JR, et al. α-Synuclein-induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain synucleinopathy models. PNAS, Feb 2, 2016. 113(7):1931-6. PMID: 26839413
Mazzulli JR, et al. Detection of Free and Protein-Bound ortho-Quinones by Near-Infrared Fluorescence. Anal Chem, Feb 3, 2016, PMID: 26813311
Mazzulli JR, et al. Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell. July 2011; 146, 37-52. PMID: 21700325.
Tsika E, et al. Distinct region-specific alpha-synuclein oligomers in A53T transgenic mice: implications for neurodegeneration. J. Neurosci. 2010; 30:3409-3418. PMID: 20203200.