Results 101 to 110 of about 5,185,837 (206)
Prion degradation pathways: Potential for therapeutic intervention [PDF]
Prion diseases are fatal neurodegenerative disorders. Pathology is closely linked to the misfolding of native cellular PrP(C) into the disease-associated form PrP(Sc) that accumulates in the brain as disease progresses. Although treatments have yet to be
McKinnon, C, Tabrizi, SJ, Goold, R
core
Prion-like seeding and nucleation of intracellular amyloid-β
Alzheimer's disease (AD) brain tissue can act as a seed to accelerate aggregation of amyloid-β (Aβ) into plaques in AD transgenic mice. Aβ seeds have been hypothesized to accelerate plaque formation in a prion-like manner of templated seeding and ...
Tomas T. Olsson +2 more
doaj +1 more source
Conversion of cellular prion protein (PrPC) into the pathogenic isoform of prion protein (PrPSc) in neurons is one of the key pathophysiological events in prion diseases.
Misaki Tanaka +4 more
doaj +1 more source
This review focuses on the principles and signal mechanisms of four types of neurofluid biomarker sensors (electrochemical, optical, mechanical, and multimodal), summarizes the detection strategies for biomarkers such as ions, neurotransmitters, metabolites, and inflammatory proteins and their applications in the diagnosis and treatment of neurological
Ting Li +4 more
wiley +1 more source
Isolation of a novel human prion strain from a PRNP codon 129 heterozygous vCJD patient.
The epizootic prion disease of cattle, bovine spongiform encephalopathy (BSE), caused variant Creutzfeldt-Jakob disease (vCJD) in humans following dietary exposure. Codon 129 polymorphism of the human prion protein gene (PRNP), encoding either methionine
Fuquan Zhang +14 more
doaj +1 more source
SKALE 2.0 maps disease‐associated protein aggregation as a phase‐resolved structural process, linking mutation‐induced geometric perturbations to nucleation, elongation, and suppressor design. Across neurodegenerative proteins, the framework reveals cryptic aggregation vulnerabilities, separates phase‐concordant and phase‐switching mutations, and ...
Jia Shen Sio +6 more
wiley +1 more source
A novel, resistance-linked ovine PrP variant and its equivalent mouse variant modulate the in vitro cell-free conversion of rPrP to PrPres [PDF]
Prion diseases are associated with the conversion of the normal cellular prion protein, PrPC, to the abnormal, disease-associated form, PrPSc. This conversion can be mimicked in vitro by using a cell-free conversion assay. It has recently been shown that
Kirby, Louise +4 more
core +1 more source
Creutzfeldt-Jakob disease and mad cows: lessons learnt from yeast cells
Transmissible spongiform encephalopathies are fatal neurodegenerative diseases that affect mammals including humans. The proteinaceous nature of the infectious agent, the prion, and its propagation, challenge established dogmas in biology. It is now
Julia Hofmann +5 more
doaj +1 more source
Sup35p in Its Soluble and Prion States Is Packaged inside Extracellular Vesicles
The yeast Saccharomyces cerevisiae harbors several prions that constitute powerful models to investigate the mechanisms of epigenetic structural inheritance.
Mehdi Kabani, Ronald Melki
doaj +1 more source
Genetic variability of the prion protein gene (PRNP) in wild ruminants from Italy and Scotland [PDF]
The genetics of the prion protein gene (PRNP) play a crucial role in determining the relative susceptibility to transmissible spongiform encephalopathies (TSEs) in several mammalian species.
Acutis, Pier Luigi +33 more
core +1 more source

