Results 31 to 40 of about 1,553,593 (211)
The pathological features of Alzheimer’s disease (AD) include senile plaques induced by amyloid-β (Aβ) protein deposits, neurofibrillary tangles formed by aggregates of hyperphosphorylated tau proteins and neuronal cell loss in specific position within ...
Yuan Zhang +5 more
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Intra- and interspecies interactions between prion proteins and effects of mutations and polymorphisms [PDF]
Recently, crystallization of the prion protein in a dimeric form was reported. Here we show that native soluble homogenous FLAG-tagged prion proteins from hamster, man and cattle expressed in the baculovirus system are predominantly dimeric.
Hundt, C. +4 more
core +1 more source
Role of the prion protein in copper turnover in astrocytes
The prion protein (PrPc) is a glycoprotein that is not only expressed predominantly by neurones but also by other cells, including astrocytes. The recent identification of PrPc as a Cu-binding protein has opened the way to investigating its function in a
David R Brown
doaj +1 more source
Dopamine induces the accumulation of insoluble prion protein and affects autophagic flux
Accumulation of protein aggregates is a histopathological hallmark of several neurodegenerative diseases, but in most cases the aggregation occurs without defined mutations or clinical histories, suggesting that certain endogenous metabolites can promote
Marcio Henrique Mello da Luz +6 more
doaj +1 more source
Transcriptomic Determinants of Scrapie Prion Propagation in Cultured Ovine Microglia. [PDF]
Susceptibility to infection by prions is highly dependent on the amino acid sequence and host expression of the cellular prion protein (PrPC); however, cellular expression of a genetically susceptible PrPC is insufficient.
Juan F Muñoz-Gutiérrez +4 more
doaj +1 more source
Glycosylphosphatidylinositols: More than just an anchor?
There is increasing interest in the role of glycosylphosphatidylinositol (GPI) anchors that attach some proteins to cell membranes. Far from being biologically inert, GPIs influence the targeting, intracellular trafficking and function of the attached ...
Clive Bate, William Nolan, Alun Williams
doaj +1 more source
Prions are misfolded proteins that accumulate within the brain in association with a rare group of fatal and infectious neurological disorders in humans and animals.
Jessy A. Slota +4 more
doaj +1 more source
Nanopore analysis of wild-type and mutant prion protein (PrPC): single molecule discrimination and PrPC kinetics [PDF]
Prion diseases are fatal neurodegenerative diseases associated with the conversion of cellular prion protein (PrPC) in the central nervous system into the infectious isoform (PrPSc).
Cashman, Neil R. +14 more
core +1 more source
A Monomer-Dimer Equilibrium of a Cellular Prion Protein (PrPC) Not Observed with Recombinant PrP [PDF]
Both the purified normal (protease-sensitive) isoform of the prion protein (PrP(C)) (Pergami, P., Jaffe, H., and Safar, J. (1996) Anal. Biochem. 236, 63-73) and recombinant prion protein (PrP) have been found to be in monomeric form (Mehlhorn, I., Groth, D., Stockel, J., Moffat, B., Reilly, D., Yansura, D., Willet, W.
Meyer RK +5 more
openaire +3 more sources
Background Glioblastoma (GBM), a highly aggressive brain tumor, contains a subpopulation of glioblastoma stem-like cells (GSCs) that play roles in tumor maintenance, invasion, and therapeutic resistance.
Rebeca Piatniczka Iglesia +5 more
doaj +1 more source

