Search for dissertations about: "Familial amyloidotic polyneuropathy"
Showing result 1 - 5 of 8 swedish dissertations containing the words Familial amyloidotic polyneuropathy.
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1. Transthyretin in senile systemic amyloidosis and familial amyloidotic polyneuropathy
Abstract : The amyloidoses comprise a heterogeneous group of disorders characterized by the deposition of fibrillar, proteinaceous amyloid deposits in various organs and tissues. To date, 17 different proteins of various sizes have been identified as amyloid proteins. READ MORE
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2. Cardiac arrhythmias and heart rate variability in familial amyloidotic polyneuropathy : A clinical study before and after liver transplantation
Abstract : Familial amyloidotic polyneuropathy (FAP), found in the northernmost counties in Sweden, is a rare, lethal and inherited amyloidosis. The disease is caused by mutated transthyretin (TTR). The mutation is characterized by an exchange of valine for methionine at position 30 (ATTRVal30Met). READ MORE
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3. 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
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4. Two Types of Fibrils in ATTR Amyloidosis : Implications for Clinical Phenotype and Treatment Outcome
Abstract : Systemic amyloidoses are a group of lethal diseases where proteins aggregate into fibrillar structures, called amyloid fibrils, that deposits throughout the body. Transthyretin (TTR) causes one type of amyloidosis, in which the aggregates mainly infiltrate nervous and cardiac tissue. READ MORE
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5. Modeling Amyloid Disease in Drosophila melanogaster
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