Anti-prion Protein Antibody 6D11 Restores Cellular Proteostasis of Prion Protein Through Disrupting Recycling Propagation of PrPSc and Targeting PrPSc for Lysosomal Degradation [PDF]
Molecular Neurobiology, 2018 PrPSc is an infectious and disease-specific conformer of the prion protein, which accumulation in the CNS underlies the pathology of prion diseases. PrPSc replicates by binding to the cellular conformer of the prion protein (PrPC) expressed by host cells and rendering its secondary structure a likeness of itself.
Martin Sadowski +2 more
exaly +3 more sources
CpG oligodeoxynucleotide reduces PrPSc accumulation and prolongs survival in prion-infected mice [PDF]
Molecules and Cells: Prion diseases, also known as transmissible spongiform encephalopathies, are characterized by the accumulation of misfolded prion proteins (PrPSc), which resists clearance due to impaired removal mechanisms and immune tolerance.
Mohd Najib Mostafa +7 more
doaj +2 more sources
Experimental Transmission of Abnormal Prion Protein (PrPsc) in the Small Intestinal Epithelial Cells of Neonatal Mice [PDF]
Veterinary Pathology, 2003 Using an immunohistochemical method, we attempted to detect the transmission of abnormal prion protein (PrPsc) to the enterocytes of the small intestine of neonatal mice by oral exposure with sheep brain affected by scrapie. Five 1-day-old neonatal mice were exposed by oral inoculation to the homogenized brain of a scrapie-affected sheep. In the small
H Taniyama
exaly +3 more sources
Novel anti-prion compounds screening in prion-infected cell culture model combined with surface plasmon resonance analysis [PDF]
Scientific ReportsPrions are misfolded proteins (PrPSc) capable of inducing the same conformational change in normal prion proteins (PrPC). These aberrant proteins are responsible for neurodegenerative diseases in animals and humans, for which no effective treatments ...
Mai Hazekawa +7 more
doaj +2 more sources
Bridging prion biology and Alzheimer’s disease: from pathogenic seeds to precision therapeutics [PDF]
Frontiers in Molecular NeuroscienceAlzheimer’s disease (AD) is characterized by the pathological aggregation of amyloid-beta (Aβ) and tau proteins, which display self-templating propagation reminiscent of the prion protein (PrPSc).
Wenjin Wang +6 more
doaj +2 more sources
Acta Neuropathologica Communications, 2021 Accumulation of misfolded host proteins is central to neuropathogenesis of numerous human brain diseases including prion and prion-like diseases. Neurons of retina are also affected by these diseases.
James F. Striebel +4 more
doaj +1 more source
Prion, 2011 The biochemical essence of prion replication is the molecular multiplication of the disease-associated misfolded isoform of prion protein (PrP), termed PrPSc, in a nucleic acid-free manner. PrP(Sc) is generated by the protein misfolding process facilitated by conformational conversion of the host-encoded cellular PrP to PrP(Sc).
Charles E, Mays, Chongsuk, Ryou
openaire +2 more sources
Removal of transmissible spongiform encephalopathy prion from large volumes of cell culture media supplemented with fetal bovine serum by using hollow fiber anion-exchange membrane chromatography. [PDF]
PLoS ONE, 2015 Cases of variant Creutzfeldt-Jakob disease in people who had consumed contaminated meat products from cattle with bovine spongiform encephalopathy emphasize the need for measures aimed at preventing the transmission of the pathogenic prion protein (PrPSc)
Ming Li Chou +4 more
doaj +1 more source
PLoS ONE, 2020 Chronic wasting disease is a transmissible spongiform encephalopathy of cervids. This fatal neurodegenerative disease is caused by misfolding of the cellular prion protein (PrPC) to pathogenic conformers (PrPSc), and the pathogenic forms accumulate in ...
Soyoun Hwang +2 more
doaj +1 more source
Use of bovine recombinant prion protein and real-time quaking-induced conversion to detect cattle transmissible mink encephalopathy prions and discriminate classical and atypical L- and H-Type bovine spongiform encephalopathy. [PDF]
PLoS ONE, 2017 Prions are amyloid-forming proteins that cause transmissible spongiform encephalopathies through a process involving conversion from the normal cellular prion protein to the pathogenic misfolded conformation (PrPSc).
Soyoun Hwang +2 more
doaj +1 more source