Results 11 to 20 of about 56,806 (329)

Unconjugated PLGA nanoparticles attenuate temperature-dependent β-amyloid aggregation and protect neurons against toxicity: implications for Alzheimer’s disease pathology

open access: yesJournal of Nanobiotechnology, 2022
Conversion of β-amyloid (Aβ) peptides from soluble random-coil to aggregated protein enriched with β-sheet-rich intermediates has been suggested to play a role in the degeneration of neurons and development of Alzheimer’s disease (AD) pathology ...
Pallabi Sil Paul   +7 more
doaj   +1 more source

Susceptibility of Beavers to Chronic Wasting Disease

open access: yesBiology, 2022
Chronic wasting disease (CWD) is a contagious, fatal, neurodegenerative prion disease of cervids. The expanding geographical range and rising prevalence of CWD are increasing the risk of pathogen transfer and spillover of CWD to non-cervid sympatric ...
Allen Herbst   +8 more
doaj   +1 more source

Prions [PDF]

open access: yesCold Spring Harbor Perspectives in Biology, 2011
The discovery of infectious proteins, denoted prions, was unexpected. After much debate over the chemical basis of heredity, resolution of this issue began with the discovery that DNA, not protein, from pneumococcus was capable of genetically transforming bacteria (Avery et al. 1944).
David W, Colby, Stanley B, Prusiner
openaire   +2 more sources

Prion-Like Propagation Mechanisms in Tauopathies and Traumatic Brain Injury: Challenges and Prospects

open access: yesBiomolecules, 2020
The accumulation of tau protein in the form of filamentous aggregates is a hallmark of many neurodegenerative diseases such as Alzheimer’s disease (AD) and chronic traumatic encephalopathy (CTE).
Hadeel Alyenbaawi   +2 more
doaj   +1 more source

Prions: Portable prion domains [PDF]

open access: yesCurrent Biology, 2000
Self-propagating abnormal proteins, prions, have been identified in yeast; asparagine/glutamine-rich 'prion domains' within these proteins can inactivate the linked functional domains; new prion domains and reporters have been used to make 'synthetic prions', leading to discoveries of new natural prions.
Wickner, R.B.   +3 more
openaire   +2 more sources

Resistance of bovine spongiform encephalopathy (BSE) prions to inactivation. [PDF]

open access: yesPLoS Pathogens, 2008
Distinct prion strains often exhibit different incubation periods and patterns of neuropathological lesions. Strain characteristics are generally retained upon intraspecies transmission, but may change on transmission to another species.
Kurt Giles   +6 more
doaj   +1 more source

RETRACTED ARTICLE: Neurotropic influenza A virus infection causes prion protein misfolding into infectious prions in neuroblastoma cells

open access: yesScientific Reports, 2021
Misfolding of the cellular prion protein, PrPC, into the amyloidogenic isoform, PrPSc, which forms infectious protein aggregates, the so-called prions, is a key pathogenic event in prion diseases.
Hideyuki Hara   +6 more
doaj   +1 more source

Reduction of Chronic Wasting Disease Prion Seeding Activity following Digestion by Mountain Lions

open access: yesmSphere, 2021
Chronic wasting disease (CWD) is a transmissible prion disease first observed in the 1960s in North America. This invariably fatal disease affects multiple cervid species in the wild and in captivity.
Chase Baune   +6 more
doaj   +1 more source

Hsp40/JDP Requirements for the Propagation of Synthetic Yeast Prions

open access: yesViruses, 2022
Yeast prions are protein-based transmissible elements, most of which are amyloids. The chaperone protein network in yeast is inexorably linked to the spreading of prions during cell division by fragmentation of amyloid prion aggregates. Specifically, the
Sarah C. Miller   +5 more
doaj   +1 more source

Amyloid prions in fungi [PDF]

open access: yes, 2016
Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements.
Aguzzi   +122 more
core   +2 more sources

Home - About - Disclaimer - Privacy