• Publications
  • Influence
Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism
Significance Prions are proteins that assume alternate shapes that become self-propagating, and while some prions perform normal physiological functions, others cause disease. Prions were discoveredExpand
  • 381
  • 27
  • PDF
The CNS glycoprotein Shadoo has PrPC-like protective properties and displays reduced levels in prion infections
The cellular prion protein, PrPC, is neuroprotective in a number of settings and in particular prevents cerebellar degeneration mediated by CNS‐expressed Doppel or internally deleted PrP (‘ΔPrP’).Expand
  • 128
  • 27
  • PDF
Serial propagation of distinct strains of Aβ prions from Alzheimer’s disease patients
Significance The amyloid-β (Aβ) peptide, which plays a central role in Alzheimer’s disease (AD) pathogenesis, exhibits many properties that are reminiscent of prions (self-propagating proteins thatExpand
  • 203
  • 12
  • PDF
Purified and synthetic Alzheimer’s amyloid beta (Aβ) prions
The aggregation and deposition of amyloid-β (Aβ) peptides are believed to be central events in the pathogenesis of Alzheimer’s disease (AD). Inoculation of brain homogenates containing Aβ aggregatesExpand
  • 285
  • 11
  • PDF
Transmission of multiple system atrophy prions to transgenic mice
Significance Multiple system atrophy (MSA) is a neurodegenerative disorder characterized by the accumulation of misfolded α-synuclein protein in glial cells within the brain. Transgenic miceExpand
  • 272
  • 11
  • PDF
Interactome Analyses Identify Ties of PrPC and Its Mammalian Paralogs to Oligomannosidic N-Glycans and Endoplasmic Reticulum-Derived Chaperones
The physiological environment which hosts the conformational conversion of the cellular prion protein (PrPC) to disease-associated isoforms has remained enigmatic. A quantitative investigation of theExpand
  • 114
  • 9
  • PDF
Evolutionary Descent of Prion Genes from the ZIP Family of Metal Ion Transporters
In the more than twenty years since its discovery, both the phylogenetic origin and cellular function of the prion protein (PrP) have remained enigmatic. Insights into a possible function of PrP mayExpand
  • 111
  • 8
  • PDF
The prion protein family: diversity, rivalry, and dysfunction.
The prion gene family currently consists of three members: Prnp which encodes PrP(C), the precursor to prion disease associated isoforms such as PrP(Sc); Prnd which encodes Doppel, a testis-specificExpand
  • 113
  • 6
Protease-Resistant Prions Selectively Decrease Shadoo Protein
The central event in prion diseases is the conformational conversion of the cellular prion protein (PrPC) into PrPSc, a partially protease-resistant and infectious conformer. However, the mechanismExpand
  • 43
  • 5
Propagation of prions causing synucleinopathies in cultured cells
Significance Progressive supranuclear palsy (PSP) and multiple system atrophy (MSA) are neurodegenerative diseases caused by tau and α-synuclein prions, respectively. Prions, purified from humanExpand
  • 126
  • 4
  • PDF