David A. Harris

Leveraging the dominant-negative effect of the kuru-protective G127Vprion protein variant as a novel therapeutic strategy

This paper demonstrates that the G127V prion protein variant can prevent and suppress prion infection through a dominant-negative effect, suggesting its potential as a therapeutic strategy.

Chemo-omic pipeline enables discovery of prion synaptotoxic pathways and inhibitory drugs

The paper identifies prion synaptotoxic pathways and inhibitory drugs using phosphoproteomic and transcriptomic data from prion-treated neurons.

Membrane-anchored PrPSc is the trigger for prion synaptotoxicity

This paper investigates the role of membrane-anchored PrPSc in prion-induced synaptotoxicity and shows that preventing its formation reduces synaptic damage.

Lysosomal Enhancement Prevents Infection with PrPSc, α-Synuclein & Tau Prions

This paper identifies elacridar as a compound that prevents prion infection by enhancing lysosomal function, showing effects against PrPSc, α-synuclein, and tau prions.

NMDA receptor misalignment in iPSC-derivedneurons from a multi-generational family withinherited Creutzfeldt-Jakob disease

This study uses iPSC-derived neurons from a family with the E200K prion mutation to model disease-relevant phenotypes, including PrP accumulations and NMDA receptor misalignment.

Sigma receptor ligands are potent anti-prion compounds that act independently of sigma receptor binding

The paper identifies sigma receptor ligands as potent anti-prion compounds that are effective regardless of sigma receptor binding.

N-Glycosylation is a Potent Regulator of Prion Protein Neurotoxicity

This study shows that N-linked glycans on PrPC are essential for maintaining a non-toxic structure and suppressing neurotoxicity through intramolecular interactions.

Ligands binding to the cellular prion protein induce its protective proteolytic release with therapeutic potential in neurodegenerative proteinopathies

The paper shows that ligands binding to PrPC induce its proteolytic release, which has neuroprotective effects, and identifies mechanisms and exceptions in this process.

Aβ receptors specifically recognize molecular features displayed by fibril ends and neurotoxic oligomers

This study identifies how Aβ receptors interact with fibril ends and neurotoxic oligomers, suggesting common molecular mechanisms that could be targeted for Alzheimer's disease therapy.