Search for dissertations about: "amyloid β-protein"

Found 3 swedish dissertations containing the words amyloid β-protein.

  1. 1. Membrane mediated aggregation of amyloid-β protein : a potential key event in Alzheimer's disease

    Author : Marcus Bokvist; Gerhard Gröbner; Göran Lindblom; Lena Mäler; Umeå universitet; []
    Keywords : NATURVETENSKAP; NATURAL SCIENCES; Alzheimer’s Disease; Aβ40; Circular Dichroism; NMR; Amyloids; Crowding; Peptide-Lipid Interaction; Biophysical chemistry; Biofysikalisk kemi;

    Abstract : The pathogenesis of Alzheimer’s disease (AD), the most common senile dementia, is a complex process. A crucial event in AD is the aggregation of amyloid-β protein (Aβ), a cleavage product from the Amyloid Precursor Protein (APP). READ MORE

  2. 2. Amyloid β-protein, Cystatin C and Cathepsin B as Biomarkers of Alzheimer's Disease

    Author : Johan Sundelöf; Lars Lannfelt; Lena Kilander; Hans Basun; Johan Sundstrom; Laura Fratiglioni; Uppsala universitet; []
    Keywords : MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; Alzheimer´s disease; amyloid β-protein; cystatin C; cathepsin B; biomarkers; risk factors; epidemiology; Geriatrics and medical gerontology; Geriatrik och medicinsk gerontologi; Medicin; Medicine;

    Abstract : It is suggested that Alzheimer’s disease (AD) is caused by an imbalance between production, degradation and clearance of the amyloid-β (Aβ) protein. This imbalance leads to aggregation of Aβ and tau proteins and neurodegeneration in the brain. READ MORE

  3. 3. Understanding the dual nature of lysozyme: part villain – part hero : A Drosophila melanogaster model of lysozyme amyloidosis

    Author : Linda Helmfors; Ann-Christin Brorsson; Bengt-Harald (Nalle) Jonsson; R. Luke Wiseman; Linköpings universitet; []
    Keywords : ;

    Abstract : Amyloid proteins are a distinct class of proteins that can misfold into β-sheet rich structures that later mature to form the characteristic species known as amyloid fibrils, and accumulate in tissues in the human body. The misfolding event is often caused by mutations (or outer factors such as changes in pH) that destabilize the native protein structure. READ MORE