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Showing 1 to 5 of 5 for “"Protein misfolding disorders"”.

  1. Structural Elucidation of [RNQ+] prions Transmissible Infectivity

    <p>Protein conformational disorders are a hallmark of protein aggregation and understanding these diseases requires a large degree of knowledge pertaining to protein folding and misfolding. Neurodegenerative diseases associated with humans are commonly found to be the result of aggregated proteins …

    wustl Repository record for Structural Elucidation of [RNQ+] prions Transmissible Infectivity (opens in a new tab)

  2. The Effect of Traumatic Brain Injury On Tau Pathology By A Potential Seeding Mechanism

    <p>The misfolding, aggregation and accumulation of specific proteins is the overarching concept in protein misfolding disorders (PMDs). The microtubule associated protein tau is known to form insoluble filaments known as neurofibrillary tangles (NFTs) composed of hyperphosphorylated tau (pTau) …

    uthsc Repository record for The Effect of Traumatic Brain Injury On Tau Pathology By A Potential Seeding Mechanism (opens in a new tab)

  3. The Molecular Interaction Between Type Ii Diabetes and Alzheimer’S Disease Through Cross-Seeding of Protein Misfolding

    … other complications. T2D and AD are considered protein misfolding disorders (PMDs). PMDs are characterized by the presence of misfolded protein aggregates, such as in T2D pancreas (islet amyloid polypeptide - IAPP) and in AD brain (amyloid– Aβ) of affected individuals. The misfolding and …

    uthsc Repository record for The Molecular Interaction Between Type Ii Diabetes and Alzheimer’S Disease Through Cross-Seeding of Protein Misfolding (opens in a new tab)

  4. Investigating the effects of extracellular biomolecules on Aß1-42 oligomer uptake and trafficking by microglia cells

    Arguably, the most prominent of the protein-misfolding disorders is Alzheimer’s disease (AD), a de- bilitating neurodegenerative disorder pathologically characterised by the deposition of tau fibrillary tangles and Ab1-42 amyloid plaques in the brain. To date, the cause of AD is unknown and rising …

    cambridge Repository record for Investigating the effects of extracellular biomolecules on Aß1-42 oligomer uptake and trafficking by microglia cells (opens in a new tab)

  5. An interdisciplinary approach to studying mechanistic, structural and toxic features of protein aggregates associated with neurodegenerative disorders.

    The misfolding and aggregation of proteins is closely associated with more than fifty human disorders, including Alzheimer's and Parkinson's diseases, all of which are currently incurable and many represent a major threat to human life. The mechanism of protein aggregation is subject to extensive …

    cambridge Repository record for An interdisciplinary approach to studying mechanistic, structural and toxic features of protein aggregates associated with neurodegenerative disorders. (opens in a new tab)