Sökning: "Transthyretin"

Visar resultat 6 - 10 av 50 avhandlingar innehållade ordet Transthyretin.

  1. 6. Structural and functional properties of transthyretin

    Författare :Anders Karlsson; A. Elisabeth Sauer-Eriksson; Salam Al-Karadaghi; Umeå universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Transthyretin; Amyloidosis; X-ray crystallography; Protein structure; Protein; Structural biology; Strukturbiologi;

    Sammanfattning : The hereditary transthyretin (TTR) amyloidoses are rare, and in severe cases, fatal disorders caused by mutations in the TTR gene. The clinical picture is diverse, involving neuropathies and myopathies, and mainly depends on the causative mutation and the sites and rates of amyloid deposition. LÄS MER

  3. 7. The heart in hereditary transthyretin amyloidosis : clinical studies on the impact of amyloid fibril composition

    Författare :Björn Pilebro; Ole Suhr; Henning Mölgaard; Umeå universitet; []
    Nyckelord :MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; Amyloidosis; Transthyretin; Cardiomyopathy; Echocardiography; Scintigraphy; Positron emission tomography; cardiovascular disease; hjärt- och kärlforskning; kardiologi; Cardiology; Clinical Physiology; klinisk fysiologi;

    Sammanfattning : Background Hereditary transthyretin amyloid (ATTRm) amyloidosis is a systemic disease mainly affecting the peripheral nervous system and the heart. The disease is inherited in an autosomal dominant manner with a varying penetrance. It is caused by mutations in the transthyretin (TTR) gene. Today more than 100 disease causing mutations are known. LÄS MER

  4. 8. Molecular Aspects of Transthyretin Amyloid Disease

    Författare :Karin Sörgjerd; Per Hammarström; Joel Buxbaum; Linköpings universitet; []
    Nyckelord :MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; Amyloid; apoptosis; BiP; chaperone; misfolding; oligomer; transthyretin; Biochemistry; Biokemi;

    Sammanfattning : 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. LÄS MER

  5. 9. 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

  7. 10. Kinetic stabilization of transthyretin and its role as an inhibitor of Aβ amyloid formation

    Författare :Lina Nilsson; Anders Olofsson; Elisabeth Sauer-Eriksson; Gunilla Westermark; Umeå universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Amyloid; transthyretin; amyloid beta; kinetic stabilizer; biokemi; Biochemistry;

    Sammanfattning : Amyloid formation occurs when normally soluble proteins and peptides misfold and aggregate into intractable threadlike structures called fibrils. There are currently more than 30 proteins associated with this aberrant structure, including the Aβ peptide in Alzheimer’s disease (AD) and transthyretin (TTR) in TTR amyloidosis. LÄS MER