Search for dissertations about: "Familial amyloid polyneuropathy"
Showing result 1 - 5 of 17 swedish dissertations containing the words Familial amyloid polyneuropathy.
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1. Familial amyloidosis with polyneuropathy : studies of genetic factors modifying the phenotype of the disease
Abstract : Background. Familial Amyloidosis with Polyneuropathy (FAP) is an autosomal dominantly inherited systemic amyloid disease. The disease is caused by mutations in the transthyretin (TTR) gene, where close to 100 different amyloidogenic mutations have been identified. READ MORE
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2. A Drosophila Disease-Model for Transthyretin-associated Amyloidosis
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
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3. Mechanisms involved in amyloid induced cytotoxicity
Abstract : Amyloidoses comprise a group of diseases where normal or mutated protein precipitates into amyloid fibrils. The deposition of fibrils causes dysfunction of organs and toxicity to nervous tissue. Up to date, 24 different proteins and peptides are known to be able to form amyloid fibrils. READ MORE
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4. Molecular Aspects of Transthyretin Amyloid Disease
Abstract : This thesis was made to get a deeper understanding of how chaperones interact with unstable, aggregation prone, misfolded proteins involved in human disease. Over the last two decades, there has been much focus on misfolding diseases within the fields of biochemistry and molecular biotechnology research. READ MORE
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5. Apolipoprotein A-IV and Transthyretin in Swedish Forms of Systemic Amyloidosis
Abstract : Over 20 different plasma proteins have been shown to have the capacity to undergo conformational changes and self-assemble into highly stable and insoluble amyloid fibrils. One, transthyretin (TTR), consists of 127 amino acid residues arranged in eight β-strands (named A to H) and is involved in two different clinical forms of amyloidosis. READ MORE