Results 111 to 120 of about 78,455 (315)
The prion protein regulates glutamate-mediated Ca2+ entry and mitochondrial Ca2+ accumulation in neurons [PDF]
, 2017 The cellular prion protein (PrPC) whose conformational misfolding leads to the production of deadly prions, has a still-unclarified cellular function despite decades of intensive research.
Bertoli, Alessandro +8 more
core +1 more source
Current Opinion in Genetics & Development, 2011 Prion diseases or transmissible spongiform encephalopathies (TSEs) are neurodegenerative disorders of humans and animals for which there are no effective treatments or cure. They include Creutzfeldt-Jakob disease (CJD) in humans and sheep scrapie, bovine spongiform encephalopathy (BSE) and chronic wasting disease (CWD) in cervids.
Lloyd, Sarah E +2 more
openaire +3 more sources
Microbiology and Immunology, EarlyView.ABSTRACT Among the three prion strains of bovine spongiform encephalopathy (BSE), classical BSE (C‐BSE) prions are known causative agents of variant Creutzfeldt–Jakob disease. By contrast, human infections with L‐type (L‐) or H‐type (H‐) BSE prions have not been reported.
Ken'ichi Hagiwara +8 more
wiley +1 more source
Evolutionary descent of prion genes from a ZIP metal ion transport ancestor [PDF]
, 2009 In the more than 20 years since its discovery, both the phylogenetic origin and cellular function of the prion protein (PrP) have remained enigmatic.
David Westaway +4 more
core +1 more source
Scientific American, 1995 The human prion diseases are fatal neurodegenerative maladies that may present as sporadic, genetic, or infectious illnesses. The sporadic form is called Creutzfeldt-Jakob disease (CJD) while the inherited disorders are called familial (f) CJD, Gerstmann-Straussler-Scheinker (GSS) disease and fatal familial insomnia (FFI).
openaire +3 more sources
Brain Pathology, EarlyView.The study analyzed the seeding activity of misfolded tau protein in Alzheimer's disease and rapidly progressive Alzheimer's disease patients and provides evidence for the existence of different tau assemblies supported by differences in cellular toxicity and morphology of thioflavin T‐positive real‐time quaking‐induced conversion products.
Matthias Schmitz +13 more
wiley +1 more source
Dogs Never Gets Prion Diseases. The Entropic Landscape Analysis of Prion Proteins Answers Why. [PDF]
, 2009 The Entropic Landscape Analysis was applied to the prion protein sequences of various mammals in order to detect potential sites of variants that would be responsible for the susceptibility of prion disease infection.
Kentaro Onizuka
core +1 more source
Brain Pathology, EarlyView.The efficacy of the novel anti‐tau active immunotherapy, p5555kb, was tested using two mouse models of tau pathology. p5555kb inoculation increased the survival rate and reduced tau pathology in tau‐overexpressing P301L mice and decreased tau seeding in the brains of C57BL/6 mice injected with human‐purified Alzheimer's disease tau.
Christopher M. Brown +7 more
wiley +1 more source
Cystatin F is a biomarker of prion pathogenesis in mice.
PLoS ONE, 2017 Misfolding of the cellular prion protein (PrPC) into the scrapie prion protein (PrPSc) results in progressive, fatal, transmissible neurodegenerative conditions termed prion diseases.
Mario Nuvolone +17 more
doaj +1 more source