Sökning: "transthyretin"

Visar resultat 1 - 5 av 46 avhandlingar innehållade ordet transthyretin.

  1. 1. Transthyretin and the transthyretin-related protein: A structural study

    Författare :Erik Lundberg; A. Elisabeth Sauer-Eriksson; Lennart Sjölin; Umeå universitet; []
    Nyckelord :NATURAL SCIENCES; NATURVETENSKAP; NATURVETENSKAP; NATURAL SCIENCES; Transthyretin; Transthyretin-related protein; X-ray crystallography; Protein structure; Amyloidosis; Structural biology; Strukturbiologi;

    Sammanfattning : Transthyretin (TTR) is one of several proteins involved in amyloid disease in humans. Unknown conformational changes of the native state of TTR result in aggregation of TTR molecules into amyloid fibrils, which accumulate in extracellular tissues. This may result in different clinical symptoms, e.g. LÄS MER

  2. 2. Hereditary transthyretin amyloidosis (ATTR V30M) : from genes to genealogy

    Författare :Nina Norgren; Ole Suhr; Alda Sousa; Umeå universitet; []
    Nyckelord :MEDICAL AND HEALTH SCIENCES; MEDICIN OCH HÄLSOVETENSKAP; MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; Hereditary transthyretin amyloidosis; Familial amyloid polyneuropathy; transthyretin; genealogy; founder effect; miRNA; allele-specific expression; gene expression; liver; medicin; Medicine;

    Sammanfattning : Background: Hereditary transthyretin amyloidosis is an autosomal dominant disease with a reduced penetrance. The most common mutation in Sweden is the V30M mutation in the transthyretin gene. Clustering areas of the disease can be found in Northern Sweden, Portugal, Brazil and Japan, although sporadic cases exist worldwide. LÄS MER

  3. 3. Transthyretin from a structural perspective

    Författare :Andreas Hörnberg; Elisabeth Sauer-Eriksson; Hugo Monaco; Umeå universitet; []
    Nyckelord :NATURAL SCIENCES; NATURVETENSKAP; NATURVETENSKAP; NATURAL SCIENCES; Cell and molecular biology; X-ray crystallography; amyloidosis; structural comparison; anomalous diffraction; Cell- och molekylärbiologi; Cell and molecular biology; Cell- och molekylärbiologi; molekylärbiologi; Molecular Biology;

    Sammanfattning : Conformational changes in human proteins can induce several types of diseases. The nature of the conformational changes is largely unknown, but some lead to amyloid fibril formation. Amyloid fibrils accumulate in the extra-cellular space of tissues resulting in disruption of organ function. LÄS MER

  4. 4. Selection of transthyretin amyloid inhibitors

    Författare :Irina Iakovleva; Anders Olofsson; Göran Larsson; Bente Westergaard; Umeå universitet; []
    Nyckelord :MEDICAL AND HEALTH SCIENCES; MEDICIN OCH HÄLSOVETENSKAP; MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; Transthyretin; TTR; ATTR; TTR-stabilizing drugs; selectivity; medicinsk biokemi; Medical Biochemistry;

    Sammanfattning : Amyloidosis is a group of clinical disorders caused by the aggregation of specific proteins into abnormal extracellular deposits. Today, 31 different proteins have been linked to amyloid diseases including transthyretin-related amyloidosis (ATTR). LÄS MER

  5. 5. A Drosophila Disease-Model for Transthyretin-associated Amyloidosis

    Författare :Malgorzata Pokrzywa; Erik Lundgren; Damian Crowther; Umeå universitet; []
    Nyckelord :NATURAL SCIENCES; NATURVETENSKAP; NATURVETENSKAP; NATURAL SCIENCES; transthyretin; amyloid; amyloidosis; Drosophila; transthyretin-associated amyloidosis; Familial amyloid polyneuropathy; neurodegeneration; serum amyloid P component; Non-steroidal Anti-Inflammatory Drugs; drug screens; Molecular biology; Molekylärbiologi;

    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