Results 11 to 20 of about 48,246 (290)
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
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 Protocols, 2017 Infectious proteins (prions) are usually self-templating filamentous protein polymers (amyloids). Yeast prions are genes composed of protein and, like the multiple alleles of DNA-based genes, can have an array of “variants,” each a distinct self-propagating amyloid conformation. Like the lethal mammalian prions and amyloid diseases, yeast prions may be
Dmitry, Kryndushkin +3 more
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
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
Prion protein and prion disease at a glance [PDF]
Journal of Cell Science, 2021 ABSTRACT Prion diseases are neurodegenerative disorders caused by conformational conversion of the cellular prion protein (PrPC) into scrapie prion protein (PrPSc). As the main component of prion, PrPSc acts as an infectious template that recruits and converts normal cellular PrPC into its pathogenic, misfolded isoform. Intriguingly, the
Zhu, Caihong, Aguzzi, Adriano
openaire +3 more sources
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
Reduction of Chronic Wasting Disease Prion Seeding Activity following Digestion by Mountain Lions
mSphere, 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
Viruses, 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