Results 51 to 60 of about 7,097 (179)

Alteration of Prion Strain Emergence by Nonhost Factors

open access: yesmSphere, 2019
Prions can persist in the environment for extended periods of time after adsorption to surfaces, including soils, feeding troughs, or fences. Prion strain- and soil-specific differences in prion adsorption, infectivity, and response to inactivation may ...
Sara A. M. Holec   +2 more
doaj   +1 more source

Lack of prion accumulation in lymphoid tissues of PRNP ARQ/ARR sheep intracranially inoculated with the agent of scrapie. [PDF]

open access: yesPLoS ONE, 2014
Sheep scrapie is a transmissible spongiform encephalopathy that can be transmitted horizontally. The prion protein gene (PRNP) profoundly influences the susceptibility of sheep to the scrapie agent and the tissue levels and distribution of PrPSc in ...
Justin J Greenlee   +4 more
doaj   +1 more source

Exploring and Targeting the Connection of Iron and Copper Homeostasis to Neurodegenerative Diseases

open access: yesMedComm, Volume 7, Issue 6, June 2026.
Iron and copper dyshomeostasis, along with their interactions with key intrinsically disordered proteins (e.g., Aβ, tau, α‐synuclein) have a strong implication in the onset and progression of neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), Prion diseases (PrDs), Huntington's disease (HD), Wilson's disease (WD),
Xin Liu   +9 more
wiley   +1 more source

Glycosylphosphatidylinositols: More than just an anchor?

open access: yesCommunicative & Integrative Biology, 2016
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

Biochemical Characterization of Prion Strains in Bank Voles

open access: yesPathogens, 2013
Prions exist as different strains exhibiting distinct disease phenotypes. Currently, the identification of prion strains is still based on biological strain typing in rodents.
Romolo Nonno   +5 more
doaj   +1 more source

Enhanced Sensitivity of a Modified Quaking‐Induced Conversion Diagnostic Test for the Broad Detection of Sporadic and Inherited Prion Diseases: A Retrospective Study

open access: yesAnnals of Neurology, Volume 99, Issue 5, Page 1303-1314, May 2026.
Objective Quaking‐induced conversion (QuIC) tests, which detect prion‐seeding activity in cerebrospinal fluid (CSF), have markedly advanced the antemortem diagnosis of prion diseases such as Creutzfeldt‐Jakob disease (CJD). These tests provide high diagnostic accuracy and enable timely differentiation from other rapidly progressive neurodegenerative ...
Jennifer Myskiw   +13 more
wiley   +1 more source

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

open access: yesPLoS 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   +2 more
doaj   +1 more source

Prion Protein Misfolding, Strains, and Neurotoxicity: An Update from Studies on Mammalian Prions

open access: yesInternational Journal of Cell Biology, 2013
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders affecting humans and other mammalian species.
Ilaria Poggiolini   +2 more
doaj   +1 more source

The first non-prion pathogen identified: neurotropic influenza virus

open access: yesPrion, 2022
The cellular isoform of prion protein, designated PrPC, is a membrane glycoprotein expressed most abundantly in the brain, particularly by neurons, and its conformational conversion into the abnormally folded, amyloidogenic isoform, PrPSc, is an ...
Suehiro Sakaguchi, Hideyuki Hara
doaj   +1 more source

PrPSc AS A PRODUCT OF MEMBRANE FOLDING

open access: yesGrail of Science
The features of the course of transmissible spongiform encephalopathies have been correlated with the regularities of protein structure formation and their interaction with cell membranes. Evidence is given about the mechanism of formation of the pathogenic isoform of the prion protein as a consequence of membrane folding of the protein with incomplete
Nataliya Obernikhina   +2 more
openaire   +1 more source

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