Search for dissertations about: "Creutzfeldt Jakob disease"

Showing result 1 - 5 of 9 swedish dissertations containing the words Creutzfeldt Jakob disease.

  1. 1. Biochemical markers in dementia - Exploring Swedish registry data and the human proteome

    Author : Tobias Skillbäck; Göteborgs universitet; Göteborgs universitet; Gothenburg University; []
    Keywords : MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; Biomarkers; Dementia; Alzheimer s disease; Vascular dementia; Creutzfeldt Jakob disease; Lewy body dementia; Frontotemporal dementia; Parkinson s disease dementia;

    Abstract : Cerebrospinal fluid (CSF) biomarkers of neurodegenerative diseases have a wide scope of applications in diagnostics, prognosis assessment, disease staging, treatment evaluation and more. In this PhD project we aimed to expand the understanding of the properties of known CSF biomarkers of Alzheimer’s disease (AD) and other neurodegenerative diseases, including the most prevalent dementia disorders. READ MORE

  2. 2. Interactions of Prion Proteins and PrP-derived Peptides in Scrapie infection

    Author : Kajsa Löfgren Söderberg; Astrid Gräslund; Marcus Fändrich; Stockholms universitet; []
    Keywords : NATURAL SCIENCES; NATURVETENSKAP; NATURVETENSKAP; NATURAL SCIENCES; Spongiform encephalopathy; Creutzfeldt-Jakob disease; Amyloidosis; Neurodegeneration; Cell penetrating peptide; Protein Transduction Domain; Heparan sulfate; Proteoglycan; Glypican; Src family kinase; Fyn; Biochemistry; Biokemi; Biochemistry; biokemi;

    Abstract : Prion diseases are fatal and incurable spongiform encephalopathies that occur amongst mammals. The central pathological event is the misfolding of the cellular prion protein (PrPC) into an amyloid, neurotoxic isoform called scrapie (PrPSc). PrPSc is the main, or sole, constituent of infectious prions. READ MORE

  3. 3. Modeling Amyloid Disease in Drosophila melanogaster

    Author : Ina Berg; Per Hammarström; Stefan Thor; Damian Crowther; Linköpings universitet; []
    Keywords : NATURAL SCIENCES; NATURVETENSKAP;

    Abstract : Amyloid diseases are caused by protein misfolding and aggregation. To date there are 27 known proteins causing amyloid disorders involving brain and peripheral protein deposition. The proteins involved in this mechanism do not share sequence homology, but the amyloid fibrils share biophysical properties and possibly a common pathogenic mechanism. READ MORE

  4. 4. Early events in disease associated protein misfolding

    Author : Sofie Nyström; Per Hammarström; Marcus Fändrich; Linköpings universitet; []
    Keywords : MEDICAL AND HEALTH SCIENCES; MEDICIN OCH HÄLSOVETENSKAP; MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; Biochemistry; Biokemi;

    Abstract : The scope of this thesis is to unravel some of the mysteries concerning events takingplace early in the amyloid cascade. In vitro studies of early misfolded states ofamyloidogenic proteins are important since the use of recombinant proteins allow us to monitor slight changes in environmental conditions as well as in amino acid composition and thereby illuminate the problem at near atomic resolution. READ MORE

  5. 5. A Drosophila Disease-Model for Transthyretin-associated Amyloidosis

    Author : Malgorzata Pokrzywa; Erik Lundgren; Damian Crowther; Umeå universitet; []
    Keywords : NATURAL SCIENCES; NATURVETENSKAP; NATURVETENSKAP; NATURAL SCIENCES; transthyretin; amyloid; amyloidosis; Drosophila; transthyretin-associated amyloidosis; Familial amyloid polyneuropathy; neurodegeneration; serum amyloid P component; Non-steroidal Anti-Inflammatory Drugs; drug screens; Molecular biology; Molekylärbiologi;

    Abstract : Amyloidoses comprise a group of gain-of-toxic function protein misfolding diseases, in which normally soluble proteins in their functional state undergo conformational changes into highly organized and generally intractable thread-like aggregates, termed amyloid fibrils. These structures accumulate predominantly in the extracellular space but growing evidence suggests that amyloids may start to form intracellularly. READ MORE