Results 91 to 100 of about 1,549,882 (213)

Role of lipid rafts and GM1 in the segregation and processing of prion protein.

open access: yesPLoS ONE, 2014
The prion protein (PrPC) is highly expressed within the nervous system. Similar to other GPI-anchored proteins, PrPC is found in lipid rafts, membrane domains enriched in cholesterol and sphingolipids.
Laura Botto   +10 more
doaj   +1 more source

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining

open access: yesJournal of General Virology, 2016
We established abnormal isoform of prion protein (PrPSc)-specific double immunostaining using mAb 132, which recognizes aa 119-127 of the PrP molecule, and novel PrPSc-specific mAb 8D5, which recognizes the N-terminal region of the PrP molecule. Using the PrPSc-specific double immunostaining, we analysed PrPSc in immortalized neuronal cell lines and ...
Tanaka, Misaki   +6 more
openaire   +3 more sources

Aspects of prion protein dynamics in cell culture models. [PDF]

open access: yes, 2005
The cell biology of Prion formation and transfer is not well understood. In order to further elucidate the dynamics of PrPc and PrPsc in a cellular context, fusions between Green Fluorescent Protein (GFP) and PrP were constructed and infected/uninfected ...
Landy, Timothy Adam, Landy, T.A.
core  

Expression of selected genes isolated from whole blood, liver and obex in lambs with experimental classical scrapie and healthy controls, showing a systemic innate immune response at the clinical end-stage

open access: yesBMC Veterinary Research, 2018
Background Incubation period, disease progression, pathology and clinical presentation of classical scrapie in sheep are highly dependent on PRNP genotype, time and route of inoculation and prion strain.
Siv Meling   +4 more
doaj   +1 more source

Decontamination of surgical instruments from prion proteins: in vitro studies on the detachment, destabilization and degradation of PrPSc bound to steel surfaces

open access: yesJournal of General Virology, 2004
Effective reprocessing of surgical instruments ensuring elimination of inadvertent contamination with infectious agents causing transmissible spongiform encephalopathies (TSEs) is essential for the prevention of iatrogenic transmission of Creutzfeldt-Jakob disease (CJD) or its new variant (vCJD) from asymptomatic carriers. In a search for effective yet
Karin, Lemmer   +3 more
openaire   +2 more sources

The Structure of PrPSc Prions

open access: yes, 2018
PrPSc (scrapie isoform of the prion protein) prions are the infectious agent behind diseases such as Creutzfeldt–Jakob disease in humans, bovine spongiform encephalopathy in cattle, chronic wasting disease in cervids (deer, elk, moose, and reindeer), as ...
Holger Wille   +2 more
core   +1 more source

PrPCWD lymphoid cell targets in early and advanced chronic wasting disease of mule deer [PDF]

open access: yes, 2002
Up to 15% of free-ranging mule deer in northeastern Colorado and southeastern Wyoming, USA, are afflicted with a prion disease, or transmissible spongiform encephalopathy (TSE), known as chronic wasting disease (CWD).
Keulen, L.J.M., van   +7 more
core   +1 more source

Small-Molecule Theranostic Probes: A Promising Future in Neurodegenerative Diseases

open access: yesInternational Journal of Cell Biology, 2013
Prion diseases are fatal neurodegenerative illnesses, which include Creutzfeldt-Jakob disease in humans and scrapie, chronic wasting disease, and bovine spongiform encephalopathy in animals.
Suzana Aulić   +2 more
doaj   +1 more source

Assessing Proteinase K Resistance of Fish Prion Proteins in a Scrapie-Infected Mouse Neuroblastoma Cell Line

open access: yesViruses, 2014
The key event in prion pathogenesis is the structural conversion of the normal cellular protein, PrPC, into an aberrant and partially proteinase K resistant isoform, PrPSc.
Evgenia Salta   +5 more
doaj   +1 more source

Primary Myopathy and Accumulation of PrPSc-Like Molecules in Peripheral Tissues of Transgenic Mice Expressing a Prion Protein Insertional Mutation

open access: yesNeurobiology of Disease, 2001
A nine-octapeptide insertional mutation in the prion protein (PrP) gene is associated with an inherited variant of Creutzfeldt-Jakob disease in humans. Transgenic mice that express the mouse PrP homologue of this mutation (designated PG14) under control of a PrP promoter display a progressive neurological disorder characterized by ataxia, apoptosis of ...
Roberto Chiesa   +6 more
openaire   +3 more sources

Home - About - Disclaimer - Privacy