Results 11 to 20 of about 14,159 (251)
Prion-Prion Interactions [PDF]
Prion, 2007 The term prion has been used to describe self-replicating protein conformations that can convert other protein molecules of the same primary structure into its prion conformation. Several different proteins have now been found to exist as prions in Saccharomyces cerevisiae. Surprisingly, these heterologous prion proteins have a strong influence on each
Irina L, Derkatch, Susan W, Liebman
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Arquivos de Neuro-Psiquiatria, 1991 Os autores se propõem a revisar alguns aspectos básicos sobre os prions, alertando sobre a possível participação destes na etiologia de algumas enfermidades degenerativas do sistema nervoso.
Godoy, J. M. +2 more
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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
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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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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
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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
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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
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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
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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
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The Standard Scrapie Cell Assay: Development, Utility and Prospects
Viruses, 2015 Prion diseases are a family of fatal neurodegenerative diseases that involve the misfolding of a host protein, PrPC. Measuring prion infectivity is necessary for determining efficacy of a treatment or infectivity of a prion purification procedure; animal
Jacques van der Merwe +3 more
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