Results 11 to 20 of about 1,598,142 (264)

Prion protein scrapie and the normal cellular prion protein [PDF]

Prion, 2015
Prions are infectious proteins and over the past few decades, some prions have become renowned for their causative role in several neurodegenerative diseases in animals and humans. Since their discovery, the mechanisms and mode of transmission and molecular structure of prions have begun to be established. There is, however, still much to be elucidated
Atkinson, Caroline J, Zhang, Kai, Munn, Alan L, Wiegmans, Adrian, Wei, Ming Q   +4 more
openaire   +4 more sources

Dissection and design of yeast prions. [PDF]

PLoS Biology, 2004
Many proteins can misfold into beta-sheet-rich, self-seeding polymers (amyloids). Prions are exceptional among such aggregates in that they are also infectious.
Lev Z Osherovich, Brian S Cox, Mick F Tuite, Jonathan S Weissman   +3 more
doaj   +3 more sources

AI-designed prion-capping proteins provide evidence that prion fibril ends are replication-competent surfaces that contribute to prion seeding activity and infectivity [PDF]

mBio
End-elongation of amyloid fibrils is a prevailing theory to explain prion replication, but direct experimental evidence for this phenomenon is limited by the lack of research tools. To serve as molecular probes for prion fibril termini, here, we designed
Jessy A. Slota, Matthew Kirby, Aidan Van Den Driessche, Dominic M. S. Kielich, Lise Lamoureux, Daniel R. Beniac, Christine Layne, Melissa Poirier, Jörg Stetefeld, Stephanie A. Booth, Ben A. Bailey-Elkin   +10 more
doaj   +2 more sources

A self-complementary recombinant adeno-associated virus vector coding for an anchorless prion protein carrying the G127V mutation extends survival in a rodent prion disease model. [PDF]

PLoS Pathogens
The replacement of a single codon in the human prion gene, causing the substitution of glycine with valine at position 127 (G127V) of the prion protein (PrP), prevents development of prion disease.
Thomas Zerbes, Claire Verkuyl, Cunjie Zhang, Sophie Grunnesjoe, Shehab Eid, Hamza Arshad, Wenda Zhao, Zahra Nasser, Teaghan O'Shea, Ari Bel, Lise Lamoureux, Kathy L Frost, Jennifer Myskiw, Le Yao Li, Erica Stuart, Holger Wille, Stephanie Booth, Joel C Watts, Gerold Schmitt-Ulms   +18 more
doaj   +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

Prion protein and aging [PDF]

Frontiers in Cell and Developmental Biology, 2014
The cellular prion protein (PrP(C)) has been widely investigated ever since its conformational isoform, the prion (or PrP(Sc)), was identified as the etiological agent of prion disorders. The high homology shared by the PrP(C)-encoding gene among mammals, its high turnover rate and expression in every tissue strongly suggest that PrP(C) may possess key
Gasperini, Lisa, Legname, Giuseppe
openaire   +4 more sources

Intra- and interspecies interactions between prion proteins and effects of mutations and polymorphisms [PDF]

, 2003
Recently, crystallization of the prion protein in a dimeric form was reported. Here we show that native soluble homogenous FLAG-tagged prion proteins from hamster, man and cattle expressed in the baculovirus system are predominantly dimeric.
Hundt, C., Weiss, S., Riley, M. L., Gauczynski, S., Leucht, C.   +4 more
core   +1 more source

Prions and Prion-like Proteins [PDF]

Journal of Biological Chemistry, 2014
Prions are self-replicating protein aggregates and are the primary causative factor in a number of neurological diseases in mammals. The prion protein (PrP) undergoes a conformational transformation leading to aggregation into an infectious cellular pathogen.
openaire   +2 more sources

Conformational conversion of prion protein in prion diseases [PDF]

Acta Biochimica et Biophysica Sinica, 2013
Prion diseases are a group of infectious fatal neurodegenerative diseases. The conformational conversion of a cellular prion protein (PrP(C)) into an abnormal misfolded isoform (PrP(Sc)) is the key event in prion diseases pathology. Under normal conditions, the high-energy barrier separates PrP(C) from PrP(Sc) isoform.
Zheng, Zhou, Gengfu, Xiao
openaire   +2 more sources

Conservation of Prion-Like Composition and Sequence in Prion-Formers and Prion-Like Proteins of Saccharomyces cerevisiae

Frontiers in Molecular Biosciences, 2019
Prions in eukaryotes have been linked to diseases, evolutionary capacitance, large-scale genetic control, and long-term memory formation. Prion formation and propagation have been studied extensively in the budding yeast Saccharomyces cerevisiae.
Ting-Yi Su, Paul M. Harrison
doaj   +1 more source