Results 1 to 10 of about 5,830 (147)

Novel anti-prion compounds screening in prion-infected cell culture model combined with surface plasmon resonance analysis [PDF]

Scientific Reports
Prions 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, Daisuke Ishibashi, Andrea Altieri, Evgeniy A. Spiridonov, Nikolai A. Dmitriev, Evgeny R. Lukyanenko, Emiliano Biasini, Alexander V. Kurkin   +7 more
doaj   +2 more sources

Bridging prion biology and Alzheimer’s disease: from pathogenic seeds to precision therapeutics [PDF]

Frontiers in Molecular Neuroscience
Alzheimer’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, Zhanhui Feng, Lingfeng Shu, Yongmei Hu, Yuting Chen, Baihui Zhang, Hua Huang   +6 more
doaj   +2 more sources

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.
Joanna E. Pankiewicz, Sandrine Sanchez, Kent Kirshenbaum, Regina B. Kascsak, Richard J. Kascsak, Martin J. Sadowski   +5 more
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Plasminogen [PDF]

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

Prion-induced photoreceptor degeneration begins with misfolded prion protein accumulation in cones at two distinct sites: cilia and ribbon synapses

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, Brent Race, Jacqueline M. Leung, Cindi Schwartz, Bruce Chesebro   +4 more
doaj   +1 more source

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, Andy Bailey, Tiffany Avory, Junji Tanimoto, Thierry Burnouf   +4 more
doaj   +1 more source

Role of donor genotype in RT-QuIC seeding activity of chronic wasting disease prions using human and bank vole substrates.

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, Justin J Greenlee, Eric M Nicholson   +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, Justin J Greenlee, Eric M Nicholson   +2 more
doaj   +1 more source

Proteostasis unbalance in prion diseases: Mechanisms of neurodegeneration and therapeutic targets

Frontiers in Neuroscience, 2022
Transmissible spongiform encephalopathies (TSEs), or prion diseases, are progressive neurodegenerative disorders of the central nervous system that affect humans and animals as sporadic, inherited, and infectious forms.
Stefano Thellung, Alessandro Corsaro, Irene Dellacasagrande, Mario Nizzari, Martina Zambito, Tullio Florio, Tullio Florio   +6 more
doaj   +1 more source

Trapping Prion Protein in the Endoplasmic Reticulum Impairs PrPC Maturation and Prevents PrPSc Accumulation [PDF]

Journal of Biological Chemistry, 2005
The conversion of the normal cellular prion protein (PrP(C)) into the abnormal scrapie isoform (PrP(Sc)) is a key feature of prion diseases. The pathogenic mechanisms and the subcellular sites of the conversion are complex and not completely understood.
Cardinale, A, Filesi, I, Vetrugno, V, Pocchiari, M, Sy, MS, BIOCCA, SILVIA   +5 more
openaire   +4 more sources