This research was originally published in the Journal of Biological Chemistry. Younan, N. D., et al. (2018). "Prion protein stabilizes amyloid-β (Aβ) oligomers and enhances Aβ neurotoxicity in a Drosophila model of Alzheimer's disease." Journal of Biological Chemistry 293(34): 13090-13099. © the Author(s).This work was supported by Wellcome Trust Grant 093241/Z/10/Z and Biotechnology and Biological Sciences Research Council Grant BB/M023877/
Prion diseases are very rare, neurodegenerative diseases caused by misfolding of the Prion protein. ...
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are neurodegenerative and infec...
Cellular (also termed 'natural') prion protein has been extensively studied for many years for its p...
Prion diseases are neurodegenerative disorders caused by conformational conversion of the cellular p...
Specific protein misfolding and aggregation are mechanisms underlying various neurodegenerative dise...
The role for cellular prion protein PrP(c) in beta-amyloid (Abeta) oligomer-induced synaptic impairm...
Thesis (Ph.D.)--Boston UniversityAlzheimer's disease (AD) is characterized by progressive dementia a...
High molecular mass assemblies of amyloid-b oligomers bind prion protein in patients with Alzheimer’...
Prion diseases are fatal neurodegenerative disorders caused by protein misfolding and aggregation, a...
A pathological hallmark of Alzheimer’s disease (AD) is an accumulation of insoluble plaque containin...
The misfolding and aggregation of proteins is the neuropathological hallmark for numerous diseases i...
Proteinopathies represent a group of diseases characterized by the unregulated misfolding and aggreg...
The prion paradigm is increasingly invoked to explain the molecular pathogenesis of neurodegenerativ...
Neurodegenerative disorders are associated with intra- or extra-cellular deposition of aggregates of...
The misfolding and aggregation of proteins is the neuropathological hallmark for numerous diseases i...
Prion diseases are very rare, neurodegenerative diseases caused by misfolding of the Prion protein. ...
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are neurodegenerative and infec...
Cellular (also termed 'natural') prion protein has been extensively studied for many years for its p...
Prion diseases are neurodegenerative disorders caused by conformational conversion of the cellular p...
Specific protein misfolding and aggregation are mechanisms underlying various neurodegenerative dise...
The role for cellular prion protein PrP(c) in beta-amyloid (Abeta) oligomer-induced synaptic impairm...
Thesis (Ph.D.)--Boston UniversityAlzheimer's disease (AD) is characterized by progressive dementia a...
High molecular mass assemblies of amyloid-b oligomers bind prion protein in patients with Alzheimer’...
Prion diseases are fatal neurodegenerative disorders caused by protein misfolding and aggregation, a...
A pathological hallmark of Alzheimer’s disease (AD) is an accumulation of insoluble plaque containin...
The misfolding and aggregation of proteins is the neuropathological hallmark for numerous diseases i...
Proteinopathies represent a group of diseases characterized by the unregulated misfolding and aggreg...
The prion paradigm is increasingly invoked to explain the molecular pathogenesis of neurodegenerativ...
Neurodegenerative disorders are associated with intra- or extra-cellular deposition of aggregates of...
The misfolding and aggregation of proteins is the neuropathological hallmark for numerous diseases i...
Prion diseases are very rare, neurodegenerative diseases caused by misfolding of the Prion protein. ...
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are neurodegenerative and infec...
Cellular (also termed 'natural') prion protein has been extensively studied for many years for its p...