Results 91 to 100 of about 75,780 (211)
Dissection and design of yeast prions. [PDF]
Many proteins can misfold into beta-sheet-rich, self-seeding polymers (amyloids). Prions are exceptional among such aggregates in that they are also infectious.
Cox Brian S +15 more
core +2 more sources
Genetic Variation and Strain Dynamics in Chronic Wasting Disease
Chronic wasting disease (CWD) is a prion disease of cervids marked by growing strain diversity and variation in host susceptibility. Central to this complexity are prion protein gene (Prnp) polymorphisms, which can modulate pathogenesis by altering the ...
Irina Zemlyankina +5 more
doaj +1 more source
Objective The goal of the research presented here is to determine if methods previously developed for the aqueous extraction of PrPSc from formalin-fixed paraffin-embedded tissue (FFPET) are applicable to the detection PrPSc by real-time quaking induced ...
Eric M. Nicholson +2 more
doaj +1 more source
Prion diseases are characterized by accumulation of misfolded protein, gliosis, synaptic dysfunction, and ultimately neuronal loss. This sequence, mirroring key features of Alzheimer disease, is modeled well in ME7 prion disease.
Asuni, Ayodeji A +5 more
core +1 more source
Update on human prion disease [PDF]
The recognition that variant Creutzfeldt–Jakob disease (vCJD) is caused by the same prion strain as bovine spongiform encephalopathy in cattle has dramatically highlighted the need for a precise understanding of the molecular biology of human prion ...
Wadsworth, Jonathan D.F., Collinge, John
core +1 more source
Identifying molecular determinants of prion conversion [PDF]
Prion diseases have been widely studied, but despite many great leaps in our knowledge of prion and protein misfolding diseases in general, many gaps remain. One example is the structural triggers or provocators of prion conversion found within the prion
Pischke, Kate Elizabeth
core
Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]
During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Hicks, M R +13 more
core +1 more source
Understanding why certain neurons are more sensitive to dysfunction and death caused by misfolded proteins could provide therapeutically relevant insights into neurodegenerative disorders.
Jessy A. Slota +4 more
doaj +1 more source
The physicochemical nature of the infectious agent in prion diseases creates asignificant challenge for decontamination services. It has been shown to be both resistant tostandard methods of decontamination, used to inactivate viruses and bacteria, and ...
Howlin, Robert
core +1 more source

