Results 31 to 40 of about 57,548 (261)
Neural Stem Cell Differentiation and Prion Infection
Bio-Protocol, 2014 Prion diseases are transmissible, fatal, neurodegenerative diseases in human and animals. The molecular basis of neurodegeneration in prion diseases is largely unclear. Developing a cellular model capable of monitoring prion-induced cytotoxicity would be
Yoshi Iwamaru +2 more
doaj +1 more source
Differential Accumulation of Misfolded Prion Strains in Natural Hosts of Prion Diseases
Viruses, 2021 Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of neurodegenerative protein misfolding diseases that invariably cause death.
Zoe J. Lambert +3 more
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Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations [PDF]
, 2011 Computer simulation of protein dynamics offers unique high-resolution information that complements experiment. Using experimentally derived structures of the natively folded prion protein (PrP), physically realistic dynamics and conformational changes ...
Daggett, Valerie, van der Kamp, Marc W
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Intercellular Transfer of the Cellular Prion Protein [PDF]
Journal of Biological Chemistry, 2002 The cellular prion protein (PrP(C)) is a glycosylphosphatidylinositol (GPI)-anchored protein. We investigated whether PrP(C) can move from one cell to another cell in a cell model. Little PrP(C) transfer was detected when a PrP(C) expressing human neuroblastoma cell line was cultured with the human erythroleukemia cells IA lacking PrP(C).
Tong, Liu +7 more
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Soluble Aβ aggregates can inhibit prion propagation [PDF]
Open Biology, 2017 Mammalian prions cause lethal neurodegenerative diseases such as Creutzfeldt–Jakob disease (CJD) and consist of multi-chain assemblies of misfolded cellular prion protein (PrPC).
Claire J. Sarell +8 more
doaj +1 more source
The prion protein constitutively controls neuronal store-operated ca2+ entry through Fyn Kinase [PDF]
, 2015 The prion protein (PrPC) is a cell surface glycoprotein mainly expressed in neurons, whose misfolded isoforms generate the prion responsible for incurable neurodegenerative disorders.
Agnese eDe Mario +8 more
core +4 more sources
Therapeutic implications of prion diseases
Biosafety and Health, 2021 Prions are unconventional infectious agents that cause lethal transmissible neurodegenerative diseases in human and animals. Prions can be distinguished from other known pathogens by their lack of nucleic acids.
Cao Chen, Xiaoping Dong
doaj +1 more source
A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein [PDF]
, 2016 Prion diseases are rare neurodegenerative conditions associated with the conformational conversion of the cellular prion protein (PrPC) into PrPSc, a self-replicating isoform (prion) that accumulates in the central nervous system of affected individuals.
Biasini, Emiliano +16 more
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Inhibition of group-I metabotropic glutamate receptors protects against prion toxicity.
PLoS Pathogens, 2017 Prion infections cause inexorable, progressive neurological dysfunction and neurodegeneration. Expression of the cellular prion protein PrPC is required for toxicity, suggesting the existence of deleterious PrPC-dependent signaling cascades.
Despoina Goniotaki +10 more
doaj +1 more source
Dimerization of the cellular prion protein inhibits propagation of scrapie prions [PDF]
Journal of Biological Chemistry, 2018 A central step in the pathogenesis of prion diseases is the conformational transition of the cellular prion protein (PrPC) into the scrapie isoform, denoted PrPSc Studies in transgenic mice have indicated that this conversion requires a direct interaction between PrPC and PrPSc; however, insights into the underlying mechanisms are still missing ...
Anna D. Engelke +12 more
openaire +3 more sources