Sökning: "familial amyloidotic polyneuropathy"

Visar resultat 1 - 5 av 8 avhandlingar innehållade orden familial amyloidotic polyneuropathy.

  1. 1. Transthyretin in senile systemic amyloidosis and familial amyloidotic polyneuropathy

    Författare :Åsa Gustavsson; Maria João Mascharenhas Saraiva; Linköpings universitet; []
    Nyckelord :MEDICINE; MEDICIN;

    Sammanfattning : 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. LÄS MER

  3. 2. Cardiac arrhythmias and heart rate variability in familial amyloidotic polyneuropathy : A clinical study before and after liver transplantation

    Författare :Rolf Hörnsten; Urban Wiklund; Staffan Andersson; Umeå universitet; []
    Nyckelord :MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; Clinical physiology; Klinisk fysiologi;

    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

  4. 3. Apolipoprotein A-IV and Transthyretin in Swedish Forms of Systemic Amyloidosis

    Författare :Joakim Bergström; Per Westermark; Giampaolo Merlini; Uppsala universitet; []
    Nyckelord :MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; Pathology; Amyloid; Fibril; Aggregation; Apolipoprotein A-IV; Transthyretin; Seeding; Senile systemic amyloidosis; Familial amyloidotic polyneuropathy; Patologi; Pathology; Patologi;

    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

  5. 4. Two Types of Fibrils in ATTR Amyloidosis : Implications for Clinical Phenotype and Treatment Outcome

    Författare :Elisabet Ihse; Per Westermark; Per Hammarström; Uppsala universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; amyloid; transthyretin; familial amyloidotic polyneuropathy; TTRV30M; non-TTRV30M; wild-type; liver transplantation; cardiomyopathy; fibril composition; Biokemi; Biochemistry; Biology with specialization in Molecular Biology; Biologi med inriktning mot molekylärbiologi; Experimentell patologi; Experimental Pathology; Medical Biochemistry; Medicinsk biokemi; Molecular Biology; Molekylärbiologi; Pathology; Patologi;

    Sammanfattning : 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. LÄS MER

  7. 5. Modeling Amyloid Disease in Drosophila melanogaster

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

    Sammanfattning : 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. LÄS MER