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Showing 1 to 20 of 160 for “"prion"”.
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Mechanisms of Prion Strain Interference
Prion diseases are infectious neurodegenerative disorders that affect humans and other mammals and are inevitably fatal. The infectious agent in prion disease (PrPSc) is an abnormal isoform of an endogenous host protein (PrPC). Prion conversion involves a conformational change of PrPC into PrPSc, …
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Timing recombinant prion protein conversion as a measure of prion activity in chronic wasting disease
… neurological disease affecting cervids caused by prions. Infected cervids shed the CWD prion in bodily fluids and excrement, contaminating the environment and creating an agricultural and ecological calamity. Preclinical antemortem CWD testing method is demanded by CWD risk management programs. In …
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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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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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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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Interaction studies of the cellular prion protein
Prion diseases are rare but fatal neurodegenerative diseases which occur both in humans and mammals caused by the prion protein (PrP) which is well conserved among the species. In this thesis the biochemical properties and the function of prion protein were investiagted using different methods. The …
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„Ex vivo” Replikation des pathogenen Prion Proteins
Das Prion Protein (PrP) ist ein ubiquitär vorkommendes Protein. Prion steht dabei für "proteinaceous infections particle" und ist laut der "protein-only hypothesis" das infektiöse Agens der Transmissiblen Spongiformen Enzephalopathien (TSE). Die TSE-Erkrankungen werden durch eine …
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Prion biology in the context of bacteria
Prions are infectious amyloid aggregates first described in the context of mammalian neurodegenerative diseases collectively known as the transmissible spongiform encephalopathies. Prions have also been uncovered in yeast, where they function as protein-based units of heredity that confer unique …
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Synthesis and structural studies of prion peptides
Thesis (M.S.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1995.
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The Life of Prion: an investigation into the physiological role of a prion-like protein in the nematode Caenorhabditis elegans
For centuries, the threat of prion disease has plagued populations – whether it be in the form of scrapie ravaging through the sheep populations of Spain in the eighteenth century, fatal familial insomnia afflicting families in Italy, or an outbreak of Creutzfeldt-Jakob disease in the UK triggered …
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Komplexe des Prion Proteins mit antiprional wirksamen Substanzen
Prionerkrankungen gehören zur Klasse der neurodegenerativen Erkrankungen, in deren Verlauf sich das Prion Protein (PrP) von einer zellulären in eine pathogene Konformation umwandelt. Sie verlaufen letal und eine Therapie ist trotz intensiver Forschung bisher nicht verfügbar. Ziel der vorliegenden …
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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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Models for protein assembly in the prion diseases
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1994.
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Cell-free formation of protease-resistant prion protein
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1996.
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Mechanism of yeast prion portein aggregation and strain formation
Misfolding and aggregation of the prion protein: PrP) causes fatal neurodegenerative diseases in many mammalian species, including humans. Mutations in the gene encoding PrP are associated with ~15% of the incidences, while, the vast majority of the cases are sporadic. Interestingly, prion diseases …
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Probing Isoforms of the Prion Protein through Tyrosine Nitration
The prion protein (PrP) has multiple stable isoforms. When PrP misfolds, it aggregates and causes neurological disease and death in mammals. The structure of the non-pathogenic isoform has been determined while the structures of the disease related isoforms are unknown. The nitration labeling …
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Probing Isoforms of the Prion Protein through Tyrosine Nitration
The prion protein (PrP) has multiple stable isoforms. When PrP misfolds, it aggregates and causes neurological disease and death in mammals. The structure of the non-pathogenic isoform has been determined while the structures of the disease related isoforms are unknown. The nitration labeling …
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Identifizierung und Charakterisierung von Interaktoren des zellulären Prion-Proteins
Das Prion-Protein ist in seiner infektiösen Form für das Auftreten und die Übertragung von transmissiblen spongiformen Enzephalopathien verantwortlich. Diese Erkrankungen können bei Mensch und Tier auftreten, wobei die bekannteste tierische Form der „Rinderwahn“ bzw. BSE ist. Die häufigste …
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The prion-like properties of assembled human alpha-synuclein
… suggested that some misfolded proteins resemble prions. Thus, aggregated alpha-synuclein shares features of PrPSc, the scrapie form of the prion protein. The aim of this thesis was to further characterize the prion-like properties of aggregated alpha-synuclein by studying the pathways of seeded …
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