Results 41 to 50 of about 5,604,422 (355)
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
The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules
Frontiers in Molecular Neuroscience, 2017 The prion glycoprotein (PrPC) is mostly located at the cell surface, tethered to the plasma membrane through a glycosyl-phosphatydil inositol (GPI) anchor.
R. Linden
semanticscholar +1 more source
, 2016 Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements.
Aguzzi +122 more
core +2 more sources
Exosomes and the Prion Protein: More than One Truth
Frontiers in Neuroscience, 2017 Exosomes are involved in the progression of neurodegenerative diseases. The cellular prion protein (PrPC) is highly expressed on exosomes. In neurodegenerative diseases, PrPC has at least two functions: It is the substrate for the generation of ...
A. Hartmann +4 more
semanticscholar +1 more source
Prion, 2023 Misfolding of the prion protein is central to prion disease aetiology. Although understanding the dynamics of the native fold helps to decipher the conformational conversion mechanism, a complete depiction of distal but coupled prion protein sites common
Patricia Soto +5 more
doaj +1 more source
Neural regeneration research, 2013 Transmissible spongiform encephalopathy or prion disease is triggered by the conversion from cellular prion protein to pathogenic prion protein. Growing evidence has concentrated on prion protein configuration changes and their correlation with prion disease transmissibility and pathogenicity.
Deming Zhao, Zhiqi Song, Lifeng Yang
openaire +3 more sources
Molecular Dynamics Studies on 3D Structures of the Hydrophobic Region PrP(109-136) [PDF]
, 2013 Prion diseases caused by the conversion from a soluble normal cellular prion protein into insoluble abnormally folded infectious prions, are invariably fatal and highly infectious degenerative diseases that affect a wide variety of mammalian species. The
Zhang, Jiapu, Zhang, Yuanli
core +4 more sources
Nature Communications, 2017 One of the most puzzling aspects of the prion diseases is the intricate relationship between prion strains and interspecies transmissibility barriers. Previously we have shown that certain fundamental aspects of mammalian prion propagation, including the
Theint Theint +7 more
semanticscholar +1 more source
Prion protein and cancers [PDF]
Acta Biochimica et Biophysica Sinica, 2014 The normal cellular prion protein, PrP(C) is a highly conserved and widely expressed cell surface glycoprotein in all mammals. The expression of PrP is pivotal in the pathogenesis of prion diseases; however, the normal physiological functions of PrP(C) remain incompletely understood.
Lihua Zhang +5 more
openaire +3 more sources
Shortest known prion protein allele in highly BSE-susceptible lemurs [PDF]
, 2000 We describe the shortest prion protein allele known to date. Surprisingly, it is found as a polymorphism exactly in a species (prosimian lemurs) which seems highly susceptible to oral infection with BSE-derived prions. The truncation of the prion protein
Gilch, S. +2 more
core +1 more source