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Showing 1 to 20 of 69 for “"prion protein"”.

  1. 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 …

    mit Repository record for Prion protein in health and disease (opens in a new tab)

  2. 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 …

    utmb Repository record for Molecular Basis of Mammalian Prion Protein Misfolding (opens in a new tab)

  3. 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 …

    lmu-germany Repository record for Interaction studies of the cellular prion protein (opens in a new tab)

  4. Cell-free formation of protease-resistant prion protein

    Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1996.

    mit Repository record for Cell-free formation of protease-resistant prion protein (opens in a new tab)

  5. 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 …

    montana-tech Repository record for Probing Isoforms of the Prion Protein through Tyrosine Nitration (opens in a new tab)

  6. 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 …

    montana Repository record for Probing Isoforms of the Prion Protein through Tyrosine Nitration (opens in a new tab)

  7. Aggregation & Localization of a Disease-Associated Prion Protein (PrP) Mutant

    … & Localization of a Disease-Associated Prion Protein: PrP) Mutant by Andrea Rhonda Zaragoza Medrano Doctor of Philosophy in Biology and Biomedical Sciences: Genetics) Washington University in St. Louis, 2009 Professor David A. Harris, Chairperson Prion protein: PrP) is a GPI-anchored …

    wustl Repository record for Aggregation & Localization of a Disease-Associated Prion Protein (PrP) Mutant (opens in a new tab)

  8. Cellular Prion Protein (PrPC): Identification and Characterization of Novel Interacting Partners

    The cellular prion protein (PrPC) is highly conserved throughout the evolution of mammals. (What does this sentence mean? What do you mean by ``conserved´´? This protein was higly conserved during the evolution of mammals [pantera et al. 2009; Jiayu et al.2009] and the gene tree deduced from the …

    goettingen Repository record for Cellular Prion Protein (PrPC): Identification and Characterization of Novel Interacting Partners (opens in a new tab)

  9. Effects of glycosylation on the structure and fibrillization of prion protein fragments

    … to PrPSc conversion. Structural studies on glycoprotein fragments in the Imperiali group has previously shown that N-linked glycosylation can play a major role modulating polypeptide conformation. It has also been shown that glycosylation can alter the thermodynamics of disulfide bond formation, …

    mit Repository record for Effects of glycosylation on the structure and fibrillization of prion protein fragments (opens in a new tab)

  10. pH MODULATION OF FIBRIL DISSOCIATION AND COPPER BINDING PROPERTIES OF THE PRION PROTEIN

    <p>The cellular form of prion protein (PrP<sup>C</sup>) is a cell-surface glycoprotein attached to lipid rafts via its glycosylphosphatidylinositol anchor. Conversion of PrP<sup>C</sup> to its "scrapie" conformer (PrP<sup>Sc</sup>, the fibrillar form) constitutes the key event of the etiology of …

    montana-tech Repository record for pH MODULATION OF FIBRIL DISSOCIATION AND COPPER BINDING PROPERTIES OF THE PRION PROTEIN (opens in a new tab)

  11. pH MODULATION OF FIBRIL DISSOCIATION AND COPPER BINDING PROPERTIES OF THE PRION PROTEIN

    <p>The cellular form of prion protein (PrP<sup>C</sup>) is a cell-surface glycoprotein attached to lipid rafts via its glycosylphosphatidylinositol anchor. Conversion of PrP<sup>C</sup> to its "scrapie" conformer (PrP<sup>Sc</sup>, the fibrillar form) constitutes the key event of the etiology of …

    montana Repository record for pH MODULATION OF FIBRIL DISSOCIATION AND COPPER BINDING PROPERTIES OF THE PRION PROTEIN (opens in a new tab)

  12. ACUTE CELLULAR UPTAKE OF ABNORMAL PRION PROTEIN IS CELL TYPE AND SCRAPIE STRAIN INDEPENDENT

    … cellular level, the uptake of protease resistant prion protein (PrP-res), which strongly correlates with infectivity and is a valid marker for TSE infection, is one of the earliest events that must occur during TSE infection. Given the difficulty of clearly distinguishing input PrP-res from either …

    montana-tech Repository record for ACUTE CELLULAR UPTAKE OF ABNORMAL PRION PROTEIN IS CELL TYPE AND SCRAPIE STRAIN INDEPENDENT (opens in a new tab)

  13. ACUTE CELLULAR UPTAKE OF ABNORMAL PRION PROTEIN IS CELL TYPE AND SCRAPIE STRAIN INDEPENDENT

    … cellular level, the uptake of protease resistant prion protein (PrP-res), which strongly correlates with infectivity and is a valid marker for TSE infection, is one of the earliest events that must occur during TSE infection. Given the difficulty of clearly distinguishing input PrP-res from either …

    montana Repository record for ACUTE CELLULAR UPTAKE OF ABNORMAL PRION PROTEIN IS CELL TYPE AND SCRAPIE STRAIN INDEPENDENT (opens in a new tab)

  14. 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 …

    trento Repository record for Development and Application of a Novel Assay for Rapid Identification of Cellular Prion Protein Modulators (opens in a new tab)

  15. 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 …

    calgary Repository record for Timing recombinant prion protein conversion as a measure of prion activity in chronic wasting disease (opens in a new tab)

  16. The Role of Cellular Prion Protein in the Development of Schwannomas and other Merlin-Deficient Tumours

    … disease caused by loss of the tumour suppressor protein, Merlin. There are several tumours associated with NF2 including; ependymomas, meningiomas and schwannomas. Merlin loss can also occur sporadically in all of these tumours and is associated with upregulation of various growth factor …

    plymouth Repository record for The Role of Cellular Prion Protein in the Development of Schwannomas and other Merlin-Deficient Tumours (opens in a new tab)

  17. Influence of Prion Protein Expression on Function of Excitatory Amino Acid Transporters in Mouse Primary Astrocytes

    Prion protein (PrP) is expressed on a wide variety of cells and plays an important role in the pathogenesis of transmissible spongiform encephalopathies. However, its normal function remains unclear. Mice that do not express PrP exhibit deficits in spatial memory and abnormalities in excitatory …

    montana-tech Repository record for Influence of Prion Protein Expression on Function of Excitatory Amino Acid Transporters in Mouse Primary Astrocytes (opens in a new tab)

  18. Influence of Prion Protein Expression on Function of Excitatory Amino Acid Transporters in Mouse Primary Astrocytes

    Prion protein (PrP) is expressed on a wide variety of cells and plays an important role in the pathogenesis of transmissible spongiform encephalopathies. However, its normal function remains unclear. Mice that do not express PrP exhibit deficits in spatial memory and abnormalities in excitatory …

    montana Repository record for Influence of Prion Protein Expression on Function of Excitatory Amino Acid Transporters in Mouse Primary Astrocytes (opens in a new tab)

  19. The subcellular trafficking of the prion protein: Characterisation of the function of the PrPc N-terminus

    … alteration of the non-pathogenic cellular prion protein (PrPc) into a infectious isoform denoted PrPSc. The latter therefore represents a pathogenic agent (prion) which does not contain nucleic acids. During biogenesis, PrPc undergoes posttranslational modifications with the addition of two …

    lmu-germany Repository record for The subcellular trafficking of the prion protein: Characterisation of the function of the PrPc N-terminus (opens in a new tab)

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