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Showing 1 to 20 of 34 for “"Prion Diseases"”.
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Models for protein assembly in the prion diseases
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1994.
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Identification of gene expression changes in Drosophila models of mammalian prion diseases
Prion diseases are fatal transmissible neurodegenerative diseases of humans and other animals. These include acquired prion diseases, such as scrapie in sheep, bovine spongiform encephalopathy in cattle and variant Creutzfeldt-Jakob disease in humans. Genetic prion diseases also occur in humans, …
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High-resolution characterization of structural changes involved in prion diseases and dialysis-related amyloidosis
… strukturelle Veränderungen untersucht, die an Prionenerkrankungen und Dialyse-assoziierter Amyloidose beteiligt sind.Die Ursache von Prionenerkrankungen liegt in der Aggregation des nativen α-helikalen Prionproteins PrPC in seine pathologische β-faltblattreiche Isoform PrPSc. Obwohl der …
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Dilations of the Endoplasmic Reticulum Contribute to Spongiform Degeneration and Unlock a Door to a Unified Model of Neuropathological Features in Prion Diseases
Prion diseases are fatal neurodegenerative disorders characterized by spongiform degeneration, neuronal loss, and misfolded prion protein (PrPSc) deposition. The mechanistic origins of spongiform degeneration, which manifests as intracellular vacuolation in neurons, have remained unclear. We …
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Prion protein in health and disease
The prion protein (PrP) is a conserved glycoprotein tethered to cell membranes by a glycosylphosphatidylinositol anchor. In mammals, PrP is expressed in many tissues, most abundantly in brain, heart, and muscle. Importantly, PrP is required for prion diseases, which are neurodegenerative diseases …
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H4:1 and H4:2 monoclonal antibodies discriminate between the normal and misfolded conformers of recombinant prion protein
Prion diseases are infectious diseases and the causative agent of this disease is a misfolded conformer of prion protein which lack nucleic acids. For the last two decades prion diseases are still standing tall in front of science, neither a cure nor a proper diagnosis method are available until …
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Investigation of preferential binding properties of monoclonal antibodies M1:1D2 and H4:4 towards the conformers of recombinant prion protein
… and viruses which contain nucleic acids, prions are proteinaceous infectious agents. Prion diseases are clinically diagnosed by post-mortem histopathological examination of brain tissue and western blotting to detect proteinase K resistant prion protein. At present, no diagnostic test …
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Molecular Basis of Prion Pathogenesis and Development of a Novel Therapeutic Strategy
Prion diseases are fatal neurodegenerative disorders characterized by a long pre-symptomatic phase followed by rapid and progressive clinical phase. Although rare in humans, the unconventional infectious nature of the disease raises the potential for an epidemic. Unfortunately, no treatment is …
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Development and Application of a Novel Assay for Rapid Identification of Cellular Prion Protein Modulators
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are fatal neurodegenerative disorders caused by the misfolding and accumulation of proteins known as prions. Despite decades of research, no effective treatment is available, and the main therapeutic strategy being pursued is to …
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Use of the Protein Misfolding Cyclic Amplification for food safety and drug discovery
<p>Prion diseases are fatal neurodegenerative disorders caused by the misfolding of the normal prion protein (PrP<sup>C</sup>) into its infectious form (PrP<sup>Sc</sup>). While the zoonotic potential of chronic wasting disease (CWD) remains uncertain, the presence of prions in food products raises …
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Modelling prion-induced neurodegeneration in PrP transgenic Drosophila
… of various genotypes to study the process of prion-induced neurodegeneration in this model. Prion diseases are caused by the occurrence of an abnormally-folded form of PrP (PrPSc) protein that arises either from the environment as an acquired disease, from mutation in the PrP-coding gene as a …
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Characterization of the 37-kDa/67-kDa laminin receptor as the cell surface receptor for the cellular prion protein
Prions have been extensively studied since they represent a new class of infectious agents in which a protein, PrPSc (prion scrapie), appears to be the sole component of the infectious particle. They are responsible for transmissible spongiform encephalopathies (TSEs), which affect both, humans and …
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Yeast Prion Variants as Models of the Phenotypic and Pathological Consequences of Amyloid Polymorphism
… disorders such as Alzheimer's disease and prion diseases. Prions are infectious proteins that propagate a self- templating amyloid structure, and have become a model for studying these diseases. Interestingly, a single protein can form a variety of distinct amyloid structures, a phenomenon …
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Exploring Novel Immunodiagnostics for Prion Disease
Prion Diseases, or Transmissible Spongiform Encephalopathies (TSEs), are rapidly progressive and fatal neurodegenerative diseases of mammals. TSEs of global importance include Creutzfeldt-Jakob Disease (CJD) in humans, Chronic Wasting Disease (CWD) in cervids, and Bovine Spongiform Encephalopathy …
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Biochemical, computer, and spectroscopic techniques applied to the study of prions and of combinations of antineoplastic drugs
… associations (Part I); · Studies on the prion structure and the pathogenesis of prion diseases (Part II). Studies referring to the Part I have been carried out at the University of Cagliari and were focalized on the evaluation and experimental validation of the method known as Artificial …
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Probing Structural Differences of Recombinant Prion Isoforms Using Fluorescence Spectroscopy
Conversion of prion protein (PrP) from its normal, cellular isoform, PrPC, to an infectious, misfolded, fibrillar isoform, PrPSc, is responsible for various neurodegenerative diseases in a variety of mammalian hosts. Although the structure of PrPC is well studied, the structure of PrPSc is not …
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Probing Structural Differences of Recombinant Prion Isoforms Using Fluorescence Spectroscopy
Conversion of prion protein (PrP) from its normal, cellular isoform, PrPC, to an infectious, misfolded, fibrillar isoform, PrPSc, is responsible for various neurodegenerative diseases in a variety of mammalian hosts. Although the structure of PrPC is well studied, the structure of PrPSc is not …
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Vergleichende Analyse der Gerstmann-Straeussler-Scheinker-Syndrom-assoziierten Mutation A117V mit der neuen pathogenen Mutation G114V des humanen Prion-Proteins in vivo und in vitro
Besides its fully translocated form, the prion protein (PrP) can exist in two transmembrane forms (NtmPrP and CtmPrP), which span the lipid bilayer in either direction. Certain mutations in the membrane-spanning segment of PrP have been shown to increase synthesis of CtmPrP and result in …
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Development of the new yeast-based assays for prion properties
Prion is an infectious isoform of a normal cellular protein which is capable of converting the non-prion form of the same protein into the alternative prion form. Mammalian prion protein PrP is responsible for prion formation in mammals, causing a series of fatal and incurable prion diseases. (1) …
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Molecular Basis of Mammalian Prion Protein Misfolding
Prions are aberrantly folded proteins that are able to self-propagate their abnormal conformation using the normally folded protein as substrate. In mammals, the only known prion protein is PrP. The misfolding of PrP is a key event underlying Transmissible Spongiform Encephalopaties (TSEs), fatal …
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