Erica Stuart

Jan 7, 2025 | cell.com | Morgan G. Stykel |Carla L. Coackley |Ping Lu |Raphaella W.L. So |Erica Stuart |Jeffery Joseph | +12 more

Keywordsalpha-synucleinG6PDParkinson's diseaseoxidative stressdopaminehiPSCResearch topic(s)CP: NeuroscienceIntroductionThe decline of voluntary motor function in Parkinson’s disease (PD) is caused, in part, by loss of A9 dopaminergic neurons in the substantia nigra pars compacta.

Sep 12, 2024 | journals.plos.org | Temerty Faculty |Genki Amano |Erica Stuart |Aeen Ebrahim Amini |PLOS Pathogens

Loading metrics Open Access Peer-reviewedResearch Article Citation: So RWL, Amano G, Stuart E, Ebrahim Amini A, Aguzzi A, Collingridge GL, et al. (2024) α-Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model. PLoS Pathog 20(9): e1012517. https://doi.org/10.1371/journal.ppat.1012517Editor: Suzette A.

Aug 1, 2024 | jci.org | Surabhi Mehra |Matthew E.C. Bourkas |Lech Kaczmarczyk |Erica Stuart

AbstractMost cases of human prion disease arise due to spontaneous misfolding of WT or mutant prion protein, yet recapitulating this event in animal models has proven challenging. It remains unclear whether spontaneous prion generation can occur within the mouse lifespan in the absence of protein overexpression and how disease-causing mutations affect prion strain properties. To address these issues, we generated knockin mice that express the misfolding-prone bank vole prion protein (BVPrP).

Mar 30, 2024 | biorxiv.org | Erica Stuart |Adriano Aguzzi |Raphaella W.L. So |Aeen Ebrahim Amini

AbstractThe cellular prion protein, PrPC, has been postulated to function as a receptor for α-synuclein, potentially facilitating cell-to-cell spreading and/or toxicity of α-synuclein aggregates in neurodegenerative disorders such as Parkinson's disease. To test this hypothesis, we compared the propagation behavior of two different α-synuclein aggregate strains in M83 transgenic mice that either expressed or did not express PrPC.

Sep 27, 2023 | biorxiv.org | Surabhi Mehra |Matthew E.C. Bourkas |Lech Kaczmarczyk |Erica Stuart

AbstractMost cases of human prion disease arise due to spontaneous misfolding of wild-type or mutant prion protein. Though recapitulating spontaneous prion conversion in animal models has proven challenging, transgenic mice expressing the misfolding-prone bank vole prion protein (BVPrP) recreate certain key aspects of sporadic and genetic prion disease.