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Showing 1 to 7 of 7 for “"human islet amyloid polypeptide hIAPP"”.

  1. Role of aromatic pi-stacking on the aggregation of human islet amyloid polypeptide (hIAPP)

    <p>Human islet amyloid polypeptide (hIAPP) is secreted in the β-cells of the pancreas, which also secretes insulin. In type 2 diabetes mellitus, hIAPP undergoes self-aggregation, forming fibrils. This self-aggregation is cytotoxic and is thought to be linked to type 2 diabetes mellitus by causing …

    emich Repository record for Role of aromatic pi-stacking on the aggregation of human islet amyloid polypeptide (hIAPP) (opens in a new tab)

  2. Insulin based inhibitors of human islet amyloid polypeptide (hIAPP) and their effect on hIAPP- mediated membrane damage in type 2 diabetes mellitus

    <p>Amylin (Islet Amyloid Polypeptide, IAPP) is a 37 amino acid polypeptide, co-secreted with insulin from pancreatic beta cells, that plays a role in the damage of cell membranes by forming amyloid fibrils in Type 2 diabetes. Insulin has been found to inhibit hIAPP (Human Islet Amyloid Polypeptide) …

    emich Repository record for Insulin based inhibitors of human islet amyloid polypeptide (hIAPP) and their effect on hIAPP- mediated membrane damage in type 2 diabetes mellitus (opens in a new tab)

  3. Insulin based inhibitors of human islet amyloid polypeptide (hIAPP) and their effect on aggregation of hIAPP in the treatment of type II diabetes

    <p>Human islet amyloid polypeptide protein (hIAPP) is secreted by the pancreas along with insulin and is assumed to play a role in pathological development of type II diabetes. It has 37 amino acids in its sequence. Amyloid is formed due to misfolding of the protein, which is cytotoxic to beta …

    emich Repository record for Insulin based inhibitors of human islet amyloid polypeptide (hIAPP) and their effect on aggregation of hIAPP in the treatment of type II diabetes (opens in a new tab)

  4. Experimental simulation of human islet amyloid polypeptide (hIAPP)-pancreatic beta cell membrane interactions: Inferences and implications in the etiopathogenesis of diabetes mellitus type II

    … and maintains normal physiological activity in humans and animals. Diabetes mellitus type II is a consequence of the gradual destruction of these important cells, likely by human islet amyloid polypeptide (hIAPP) that is co-secreted with insulin. Increasing health care costs, coupled with the …

    emich Repository record for Experimental simulation of human islet amyloid polypeptide (hIAPP)-pancreatic beta cell membrane interactions: Inferences and implications in the etiopathogenesis of diabetes mellitus type II (opens in a new tab)

  5. Membrane fragmentation by a 20-29 fragment of human islet amyloid polypeptide and rat amyloid polypeptide

    … of insulin-producing pancreatic beta cells. The amyloidogenic human Islet Amyloid Polypeptide (hIAPP, also known as human amylin) is believed to play a crucial role in this biological process. Previous studies have shown that hIAPP forms small aggregates that kill β-cells by disrupting the …

    emich Repository record for Membrane fragmentation by a 20-29 fragment of human islet amyloid polypeptide and rat amyloid polypeptide (opens in a new tab)

  6. Unzipping Amyloid Fibrils: How a Novel Calcium-Binding Protein, NUCB1, Prevents the Formation of Amyloid Fibrils

    … we also established novel and unique anti-amyloidogenic functional ability of sNUCB1. We show that Ca<sup>2+</sup>-free sNUCB1 can inhibit fibril formation by highly amyloidogenic human Islet Amyloid PolyPeptide (hIAPP) and Amyloid-β 42 (Aβ42) peptides, as relevant to Type-2 Diabetes and …

    rockefeller Repository record for Unzipping Amyloid Fibrils: How a Novel Calcium-Binding Protein, NUCB1, Prevents the Formation of Amyloid Fibrils (opens in a new tab)

  7. Developing peptide-based inhibitors of amylin aggregation as a novel treatment for type 2 diabetes

    Human islet amyloid polypeptide (hIAPP), also known as amylin, is the main constituent of the amyloid deposits present in approximately 95% of people with type 2 diabetes. Amylin aggregates into oligo-/polymeric sheet structures which are considered to be cytotoxic to pancreatic -cells. Inhibiting …

    lancaster Repository record for Developing peptide-based inhibitors of amylin aggregation as a novel treatment for type 2 diabetes (opens in a new tab)