Results 31 to 40 of about 50,704 (271)
Brain Pathology, 1996 The prion protein (PrP) plays an essential role in the pathogenesis of a group of sporadic, genetically determined and infectious fatal degenerative diseases, referred to as “prion diseases”, affecting the central nervous system of humans and other mammals. The cellular PrP is encoded by a single copy gene, highly conserved across mammalian species. In
B, Ghetti +9 more
openaire +2 more sources
Prion protein scrapie and the normal cellular prion protein [PDF]
Prion, 2015 Prions are infectious proteins and over the past few decades, some prions have become renowned for their causative role in several neurodegenerative diseases in animals and humans. Since their discovery, the mechanisms and mode of transmission and molecular structure of prions have begun to be established. There is, however, still much to be elucidated
Atkinson, Caroline J +4 more
openaire +3 more sources
Molecular Barriers to Zoonotic Transmission of Prions
Emerging Infectious Diseases, 2014 The risks posed to human health by individual animal prion diseases cannot be determined a priori and are difficult to address empirically. The fundamental event in prion disease pathogenesis is thought to be the seeded conversion of normal prion protein
Marcelo A. Barria +8 more
doaj +1 more source
Sequence features governing aggregation or degradation of prion-like proteins. [PDF]
PLoS Genetics, 2018 Enhanced protein aggregation and/or impaired clearance of aggregates can lead to neurodegenerative disorders such as Alzheimer's Disease, Huntington's Disease, and prion diseases.
Sean M Cascarina +3 more
doaj +1 more source
Prion protein—Semisynthetic prion protein (PrP) variants with posttranslational modifications [PDF]
Journal of Peptide Science, 2019 Deciphering the pathophysiologic events in prion diseases is challenging, and the role of posttranslational modifications (PTMs) such as glypidation and glycosylation remains elusive due to the lack of homogeneous protein preparations. So far, experimental studies have been limited in directly analyzing the earliest events of the conformational change ...
Stefanie Hackl, Christian F.W. Becker
openaire +4 more sources
PLoS Biology, 2016 Protein misfolding is common across many neurodegenerative diseases, with misfolded proteins acting as seeds for "prion-like" conversion of normally folded protein to abnormal conformations.
James Alibhai +7 more
doaj +1 more source
PLoS ONE, 2020 Conversion of cellular prion protein (PrPC) into the pathogenic isoform of prion protein (PrPSc) in neurons is one of the key pathophysiological events in prion diseases.
Misaki Tanaka +4 more
doaj +1 more source
Prion pathogenesis is unaltered in the absence of SIRPα-mediated "don't-eat-me" signaling. [PDF]
PLoS ONE, 2017 Prion diseases are neurodegenerative conditions caused by misfolding of the prion protein, leading to conspicuous neuronal loss and intense microgliosis.
Mario Nuvolone +6 more
doaj +1 more source
PLoS ONE, 2006 Prions are known to cause transmissible spongiform encephalopathies (TSE) after accumulation in the central nervous system. There is increasing evidence that prions are also present in body fluids and that prion infection by blood transmission is possible.
Franscini, Nicola +8 more
openaire +5 more sources
Journal of Integrative Neuroscience, 2019 The effects of cellular prion protein on rapid eye movement sleep deprivation-induced spatial memory impairment were investigated, and the related mechanisms explored.
Li Hu +5 more
doaj +1 more source