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Showing 1 to 17 of 17 for “"Prion Proteins"”.
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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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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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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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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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The role of the 37-kDa/67-kDa laminin receptor in the cellular metabolism of the prion protein
Prionen Erkrankungen sind neurodegenerative Erkrankungen, bei denen die abnormale Form (PrPSc) des zellulären Prion Proteins (PrPC) eine entscheidente Rolle spielt. PrPSc lagert sich im Gehirn von Menschen und verschiedenen Säugetieren zu langen Ketten, sogenanntem Amyloid, zusammen und bildet …
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Prediction of parallel in-register amyloidogenic beta-structures In highly beta-rich protein sequences by pairwise propensity analysis
Amyloids and prion proteins are clinically and biologically important beta-structures, whose supersecondary structures are difficult to determine by standard experimental or computational means. In addition, significant conformational heterogeneity is known or suspected to exist in many amyloid …
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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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Assessing the role of Hsp70 in prion propagation in Saccharomyces cerevisiae
The term Prion (Proteinaceous infectious) was first described by Stanley Prusiner in 1982. Prions are infectious proteins and are responsible for many neurodegenerative diseases, collectively termed as transmissible spongioform encephalopathies, including; BSE, vBSE, scrapie and CJD. Prions are …
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Domain swapping as a molecular mechanism in amyloidosis
… to brain hemorrhage and death. Amyloidogenic proteins like cystatin C and prion proteins have been shown to form dimers by exchange of subdomains of the monomeric proteins. This process, called ?domain swapping?, has also been suggested to play a part in the generation of amyloid fibrils. In …
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Übertragung von BSE auf nicht humane Primaten als Modell für die variante Creutzfeldt-Jakob Erkrankung (vCJD) im Menschen
… infizierten Javaneraffen an einer Prionenerkrankung erkrankten. Im Vergleich mit verschiedenen humanen CJD-Subtypen konnte diese als vCJD identifiziert werden. Diese Ergebnisse bestätigen BSE-Material als Auslöser für vCJD. Zusätzlich wurden bei 2/6 Tieren Charakteristika …
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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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Mielių baltymo Sup35 GNNQQNY sekos mutantinių variantų kūrimas ir jų sintezė Saccharomyces cerevisiae ląstelėse /
Prions are proteinaceous particles that are able to replicate and spread as an infection. Prions cause transmissible spongiform encephalopathies (TSEs), a fatal neurodegenerative disease in mammals. Neurodegenerative diseases also include amyloidoses, better known as Alzheimer's, Parkinson's or …
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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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Discovery and characterization of prions in Saccharomyces cerevisiae
… reaction. These aggregates, or prions, are the infectious agents behind diseases like Kuru and mad-cow disease. In yeast, however, prions act as epigenetic elements that confer heritable alternative phenotypes. Prion-forming proteins create bistable molecular systems whose …
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Using yeast to study neurodegenerative diseases : amyloid formation as a protective mechanism and a new Alzheimer's disease model
… ranging from E. coli to human stem cells. Yeast prion proteins are another group of proteins capable of adapting an amyloid conformation. The self-templating amyloid fold allows yeast prions to act as non-Mendelian elements of inheritance. We have shown that yeast prion amyloid fibrils, …
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Microfluidic Approaches for Investigating Aggregated Forms of Disease-Related Proteins
The self-assembly of soluble proteins is a common phenomenon observed in nature. It ranges from the formation of functional biomaterials, such as actin filaments and tubulin microtubules that form the cytoeskeleton, to the abnormal deposition of aberrant aggregates that lead to disease. There are …