Results 11 to 20 of about 97,377 (307)
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
Caihong Zhu, Adriano Aguzzi
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Prion protein glycosylation [PDF]
Journal of Neurochemistry, 2005 AbstractThe transmissible spongiform encephalopathies (TSE), or prion diseases are a group of transmissible neurodegenerative disorders of humans and animals. Although the infectious agent (the ‘prion’) has not yet been formally defined at the molecular level, much evidence exists to suggest that the major or sole component is an abnormal isoform of ...
Lawson, Victoria A +3 more
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Prion Protein Misfolding [PDF]
Current Molecular Medicine, 2009 The crucial event in the development of transmissible spongiform encephalopathies (TSEs) is the conformational change of a host-encoded membrane protein - the cellular PrP(C) - into a disease associated, fibril-forming isoform PrP(Sc). This conformational transition from the alpha-helix-rich cellular form into the mainly beta-sheet containing ...
Kupfer, L, Hinrichs, W, Groschup, M.H
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Cell, 1998 We thank G. Carlson, N. Nathanson, and J. Safar for carefully reviewing sections of this manuscript. This research was supported by grants from the National Institute of Aging and the National Institute of Neurologic Diseases and Stroke of the National Institutes of Health, International Human Frontiers of Science Program, and American Health ...
Prusiner, Stanley B +3 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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Scientific Reports, 2022 Transgenic mice over-expressing human PRNP or murine Prnp transgenes on a mouse prion protein knockout background have made key contributions to the understanding of human prion diseases and have provided the basis for many of the fundamental advances in
Graham S. Jackson +5 more
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Distinct amino acid compositional requirements for formation and maintenance of the [PSI+] prion in yeast [PDF]
, 2015 Multiple yeast prions have been identified that result from the structural conversion of proteins into a self-propagating amyloid form. Amyloid-based prion activity in yeast requires a series of discrete steps.
Ben-Musa, Zobaida +6 more
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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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, 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
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