Results 11 to 20 of about 69,500 (311)
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
openaire +3 more sources
Prion protein conversion at two distinct cellular sites precedes fibrillisation
Nature Communications, 2023 The self-templating nature of prions plays a central role in prion pathogenesis and is associated with infectivity and transmissibility. Since propagation of proteopathic seeds has now been acknowledged a principal pathogenic process in many types of ...
Juan Manuel Ribes +5 more
doaj +1 more source
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
openaire +5 more sources
Case report of homozygous E200D mutation of PRNP in apparently sporadic Creutzfeldt-Jakob disease
BMC Neurology, 2021 Background Inherited prion diseases are rare autosomal dominant disorders associated with diverse clinical presentations. All are associated with mutation of the gene that encodes prion protein (PRNP).
Ahamad Hassan +6 more
doaj +1 more source
The Future of Seed Amplification Assays and Clinical Trials
Frontiers in Aging Neuroscience, 2022 Prion-like seeded misfolding of host proteins is the leading hypothesised cause of neurodegenerative diseases. The exploitation of the mechanism in the protein misfolding cyclic amplification (PMCA) and real-time quaking-induced conversion (RT-QuIC ...
Thomas Coysh +3 more
doaj +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
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
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
Gene-Edited Cell Models to Study Chronic Wasting Disease
Viruses, 2022 Prion diseases are fatal infectious neurodegenerative disorders affecting both humans and animals. They are caused by the misfolded isoform of the cellular prion protein (PrPC), PrPSc, and currently no options exist to prevent or cure prion diseases ...
Simrika Thapa +5 more
doaj +1 more source
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
openaire +2 more sources