Results 51 to 60 of about 5,869 (184)
Objective Traumatic brain injury (TBI) is an established risk factor for dementia, although the underlying mechanisms remain unclear. Our previous research demonstrated that a single severe TBI in wild‐type (WT) mice induces a prion‐like form of tau (tauTBI) that spreads throughout the brain, leading to memory deficits.
Gloria Vegliante +19 more
wiley +1 more source
Toxic mechanisms of amyloid oligomers and therapeutic strategies
Abstract Amyloid oligomers are increasingly recognized as the major toxic contributors across protein‐misfolding disorders. In this review, we cover mechanistic evidence showing how these transient and structurally heterogeneous oligomers disrupt cellular homeostasis by: (i) permeabilizing lipid membranes and forming ion‐conducting pores; (ii ...
Magdalena I. Ivanova +2 more
wiley +1 more source
Phenotyping of Protein-Prion (PrPsc)-accumulating Cells in Lymphoid and Neural Tissues of Naturally Scrapie-affected Sheep by Double-labeling Immunohistochemistry [PDF]
Transmissible spongiform encephalopathies are fatal neurodegenerative diseases characterized by amyloid deposition of protein-prion (PrPsc), the pathogenic isoform of the host cellular protein PrPc, in the immune and central nervous systems. In the absence of definitive data on the nature of the infectious agent, PrPsc immunohistochemistry (IHC ...
Andreoletti, Olivier +7 more
openaire +3 more sources
Plasmonics‐Enhanced Characterization of Cervid PrP (87–114) Fragment Aggregates in Solution
Multimodal nanophotonics platform combining plasmon‐enhanced imaging, label‐free SERS, and optical staining reveals new insights into the aggregation of the cervid PrP (87–114) fragment, an amyloidogenic sequence linked to chronic wasting disease susceptibility.ABSTRACTWe performed a multimodal characterisation of self‐assembled fibrillar aggregates ...
Shinki Midha +4 more
wiley +1 more source
Classical- (C-) and atypical L-type bovine spongiform encephalopathy (BSE) prions cause different pathological phenotypes in cattle brains, and the disease-associated forms of each prion protein (PrPSc) has a dissimilar biochemical signature.
Ken'ichi Hagiwara +9 more
doaj +1 more source
Prions are infectious proteins causing fatal, transmissible neurodegenerative diseases of animals and humans. Replication involves template-directed refolding of host encoded prion protein, PrPC, by its infectious conformation, PrPSc.
Jifeng Bian +24 more
doaj +1 more source
CpG oligodeoxynucleotide-enhanced humoral immune response and production of antibodies to prion protein PrPSc in mice immunized with 139A scrapie-associated fibrils [PDF]
AbstractPrion diseases are characterized by conversion of the cellular prion protein (PrPC) to a protease-resistant conformer, the srapie form of PrP (PrPSc). Humoral immune responses to nondenatured forms of PrPSc have never been fully characterized. We investigated whether production of antibodies to PrPSc could occur in PrP null (Prnp−/−) mice and ...
Daryl S, Spinner +11 more
openaire +2 more sources
Plasma biomarkers in CJD reveal multisystem involvement, with neuronal injury markers showing strong discriminative performance and vascular proteins indicating blood–brain barrier dysfunction. In asymptomatic PRNP mutation carriers, biomarker changes are minimal and emerge mainly near disease onset ABSTRACT Background Plasma markers of neuronal injury
Zhong‐Yun Chen +11 more
wiley +1 more source
The Prion Basis of Progressive Neurodegenerative Disorders
The discovery of proteinaceous infectious agents by Prusiner in 1982 was sensational. All previously known pathogens contained nucleic acids, the code of life, that enabled them to reproduce. In contrast, the proteinaceous agents of disease, called prion
Tvisha Joshi, Nidhi Ahuja
doaj +1 more source
Abstract In the coming decades, there is expected to be a sharply increased demand for dietary proteins for humans and animals. As a result, there is an increasing focus on reared insects as a new source of protein. According to the Ministry of Agriculture, Nature and Food Quality (LNV), the use of food chain residual flows such as former foodstuffs as
L.F.F. Kox, D.T.H.M. Sijm
wiley +1 more source

