Results 11 to 20 of about 56,657 (298)
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 +4 more
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Efficient transmission and characterization of creutzfeldt-jakob disease strains in bank voles.
PLoS Pathogens, 2006 Transmission of prions between species is limited by the "species barrier," which hampers a full characterization of human prion strains in the mouse model.
Romolo Nonno +14 more
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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
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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
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Prion protein self-peptides modulate prion interactions and conversion [PDF]
, 2009 Background: Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood.
Bossers, A. +12 more
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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.
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BMC Genomics, 2017 Background The function of the prion protein, involved in the so-called prion diseases, remains a subject of intense debate and the possibility that it works as a pleiotropic protein through the interaction with multiple membrane proteins is somehow ...
J. A. Macedo +7 more
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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
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Intraperitoneal Infection of Wild-Type Mice with Synthetically Generated Mammalian Prion. [PDF]
PLoS Pathogens, 2015 The prion hypothesis postulates that the infectious agent in transmissible spongiform encephalopathies (TSEs) is an unorthodox protein conformation based agent.
Xinhe Wang +6 more
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Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [PDF]
, 2010 Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. These diseases can be hereditary in humans and four of the many disease-associated missense mutants of PrP are in the ...
Valerie Daggett +3 more
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