Sökning: "Polyneuropathy"
Visar resultat 11 - 15 av 41 avhandlingar innehållade ordet Polyneuropathy.
11. Cardiac arrhythmias and heart rate variability in familial amyloidotic polyneuropathy : A clinical study before and after liver transplantation
Sammanfattning : 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). LÄS MER
12. Methodological aspects and usefulness of Quantitative Sensory Testing in early small fiber polyneuropathy : a clinical study in Swedish hereditary transthyretin amyloidosis patients
Sammanfattning : Generalised polyneuropathy (PNP) is a common cause to neurological impairment, and may be an early symptom of a severe systemic disease. One such illness is hereditary transthyretin (TTR) amyloidosis (ATTR), a progressive fatal disorder caused by a mutation on the TTR gene. LÄS MER
13. Hypertrophic cardiomyopathy in Northern Sweden : with special emphasis on molecular genetics
Sammanfattning : Hypertrophic cardiomyopathy (HCM) is a heterogeneous, often familial disease, characterized by cardiac hypertrophy, predominantly affecting the interventricular septum. To date, no study has systematically analysed the genetic and phenotypic aspects of the disease in a Swedish population. LÄS MER
14. Apolipoprotein A-IV and Transthyretin in Swedish Forms of Systemic Amyloidosis
Sammanfattning : 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. LÄS MER
15. A Drosophila Disease-Model for Transthyretin-associated Amyloidosis
Sammanfattning : 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. LÄS MER
