Results 11 to 20 of about 71,281 (314)
Human stem cell-derived astrocytes replicate human prions in a PRNP genotype-dependent manner. [PDF]
Journal of Experimental Medicine, 2017 Prions are infectious agents that cause neurodegenerative diseases such as Creutzfeldt-Jakob disease (CJD). The absence of a human cell culture model that replicates human prions has hampered prion disease research for decades.
Alibhai, James +9 more
core +2 more sources
Artificial strain of human prions created in vitro
Nature Communications, 2018 Synthetic prions have previously been generated from recombinant rodent PrP. Here the authors generate synthetic human prions, by seeding human PrP with CJD prions, and characterize its infectivity in mice.
Chae Kim +11 more
doaj +2 more sources
Ex vivomammalian prions are formed of paired double helical prion protein fibrils [PDF]
Open Biology, 2016 Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively correlated with infectivity and the three-dimensional structure of infectious prions has remained ...
Clare, Daniel +11 more
core +3 more sources
High-resolution structure and strain comparison of infectious mammalian prions.
Molecules and Cells, 2021 Within the extensive range of self-propagating pathologic protein aggregates of mammals, prions are the most clearly infectious (e.g., ∼109 lethal doses per milligram). The structures of such lethal assemblies of PrP molecules have been poorly understood.
Allison Kraus +9 more
semanticscholar +1 more source
Proceedings of the National Academy of Sciences of the United States of America, 2020 Significance Chronic wasting disease (CWD) is a highly contagious disease caused by prions that affects several cervid species and is relentlessly spreading across North America. Very recently, CWD was detected for the first time in Europe. In this study,
R. Nonno +15 more
semanticscholar +1 more source
Cold 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
Biomolecules, 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]
Current 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]
PLoS 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
Scientific 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