Recent advances in the histo‐molecular pathology of human prion disease

S Baiardi, M Rossi, S Capellari, P Parchi - Brain Pathology, 2019 - Wiley Online Library
Prion diseases are progressive neurodegenerative disorders affecting humans and other
mammalian species. The term prion, originally put forward to propose the concept that a …

Distinct types of amyloid‐β oligomers displaying diverse neurotoxicity mechanisms in Alzheimer's disease

P Madhu, S Mukhopadhyay - Journal of cellular biochemistry, 2021 - Wiley Online Library
Soluble oligomers of amyloid‐β (Aβ) are recognized as key pernicious species in
Alzheimer's disease (AD) that cause synaptic dysfunction and memory impairments …

The cellular prion protein increases the uptake and toxicity of TDP-43 fibrils

C Scialò, L Celauro, M Zattoni, TH Tran, E Bistaffa… - Viruses, 2021 - mdpi.com
Cytoplasmic aggregation of the primarily nuclear TAR DNA-binding protein 43 (TDP-43)
affects neurons in most amyotrophic lateral sclerosis (ALS) and approximately half of …

Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy

AS König, NS Rösener, L Gremer, M Tusche… - Journal of Biological …, 2021 - ASBMB
Human PrP (huPrP) is a high-affinity receptor for oligomeric amyloid β (Aβ) protein
aggregates. Binding of Aβ oligomers to membrane-anchored huPrP has been suggested to …

Prion protein stabilizes amyloid-β (Aβ) oligomers and enhances Aβ neurotoxicity in a Drosophila model of Alzheimer's disease

ND Younan, KF Chen, RS Rose, DC Crowther… - Journal of Biological …, 2018 - ASBMB
The cellular prion protein (PrP C) can act as a cell-surface receptor for β-amyloid (Aβ)
peptide; however, a role for PrP C in the pathogenesis of Alzheimer's disease (AD) is …

Proteopathic seed amplification assays for neurodegenerative disorders

N do Carmo Ferreira… - Clinics in laboratory …, 2020 - labmed.theclinics.com
In order to function properly, proteins typically must fold and assume defined native three-
dimensional structures. However, disruption of native protein folding may allow abnormal …

Production of seedable Amyloid-β peptides in model of prion diseases upon PrPSc-induced PDK1 overactivation

J Ezpeleta, V Baudouin, ZE Arellano-Anaya… - Nature …, 2019 - nature.com
The presence of amyloid beta (Aβ) plaques in the brain of some individuals with Creutzfeldt-
Jakob or Gertsmann-Straussler-Scheinker diseases suggests that pathogenic prions …

The characterization of AD/PART co-pathology in CJD suggests independent pathogenic mechanisms and no cross-seeding between misfolded Aβ and prion proteins

M Rossi, H Kai, S Baiardi, A Bartoletti-Stella… - Acta neuropathologica …, 2019 - Springer
Current evidence indicating a role of the human prion protein (PrP) in amyloid-beta (Aβ)
formation or a synergistic effect between Aβ and prion pathology remains controversial …

Infectious prions do not induce Aβ deposition in an in vivo seeding model

J Rasmussen, S Krasemann, H Altmeppen… - Acta …, 2018 - Springer
An increasing number of studies have suggested that certain cases of iatrogenic Creutzfeldt–
Jakob disease (iCJD) that harbor significant β-amyloid (Aβ) pathology are the result of …

Adaptación de un sistema de propagación de priones in vitro para el cribado masivo de compuestos específicos frente a las encefalopatías espongiformes …

E González Miranda - 2020 - ekoizpen-zientifikoa.ehu.eus
Las Encefalopatías Espongiformes Transmisibles (EET) son un conjunto de desórdenes
neurodegenerativos mortales que afectan a varios mamíferos incluidos los humanos, cuyo …