Results 11 to 20 of about 5,646 (167)
Electrochemical Assay of Human Islet Amyloid Polypeptide and Its Aggregation [PDF]
Sensors, 2008 Square wave voltammetry is used in this work to detect human islet amyloid polypeptide (hIAPP) by using the oxidized signal of the tyrosine residue in hIAPP. A detection limit of 1×10-6 M for hIAPP has been obtained. A kinetic study of the aggregation
Genxi Li +3 more
doaj +3 more sources
Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide. [PDF]
Nano Lett, 2019 Human amyloids and plaques uncovered post mortem are highly heterogeneous in structure and composition, yet literature concerning the heteroaggregation of amyloid proteins is extremely scarce. This knowledge deficiency is further exacerbated by the fact that peptide delivery is a major therapeutic strategy for targeting their full-length counterparts ...
Kakinen A +12 more
europepmc +7 more sources
Membrane-mediated amyloid deposition of human islet amyloid polypeptide. [PDF]
Biophys Rev, 2018 Amyloid deposition of human islet amyloid polypeptide (hIAPP) within the islet of Langerhans is closely associated with type II diabetes mellitus. Accumulating evidence indicates that the membrane-mediated aggregation and subsequent deposition of hIAPP are linked to the dysfunction and death of insulin-producing pancreatic β-cells, but the molecular ...
Sasahara K.
europepmc +4 more sources
Lysophosphatidylcholine modulates the aggregation of human islet amyloid polypeptide. [PDF]
Phys Chem Chem Phys, 2017 Micellar lysophosphatidylcholine inhibits the aggregation of human islet amyloid polypeptide (IAPP).
Xing Y +9 more
europepmc +8 more sources
Idealized Models of Protofilaments of Human Islet Amyloid Polypeptide [PDF]
Journal of Chemical Information and Modeling, 2012 Fibrils formed by assembly of human islet amyloid polypeptide (hIAPP) are found in most patients with type II diabetes. Structurally, these fibrils are composed of multiple protofilaments and are characterized by extended beta sheets, variable helical twists, and different morphologies.
Yiyu Li +3 more
openaire +2 more sources
Frontiers in Molecular Biosciences, 2023 Insulin resistance is the major risk factor for Type 2 diabetes (T2D). In vulnerable individuals, insulin resistance induces a progressive loss of insulin secretion with islet pathology revealing a partial deficit of beta cells and islet amyloid derived ...
Tatyana Gurlo +8 more
doaj +1 more source
Aspects of structural landscape of human islet amyloid polypeptide [PDF]
The Journal of Chemical Physics, 2015 The human islet amyloid polypeptide (hIAPP) co-operates with insulin to maintain glycemic balance. It also constitutes the amyloid plaques that aggregate in the pancreas of type-II diabetic patients. We have performed extensive in silico investigations to analyse the structural landscape of monomeric hIAPP, which is presumed to be intrinsically ...
He, Jianfeng +4 more
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Molecular Mechanisms of Amylin Turnover, Misfolding and Toxicity in the Pancreas
Molecules, 2022 Amyloidosis is a common pathological event in which proteins self-assemble into misfolded soluble and insoluble molecular forms, oligomers and fibrils that are often toxic to cells.
Diti Chatterjee Bhowmick +3 more
doaj +1 more source
Micelle Formation by a Fragment of Human Islet Amyloid Polypeptide [PDF]
Biophysical Journal, 2003 Human islet amyloid polypeptide (hIAPP) is the major component of amyloid plaques found in the pancreatic islets of persons with type 2 diabetes mellitus. HIAPP belongs to the group of amyloidogenic proteins, characterized by their aggregation and deposition as fibrillar amyloid in various body tissues.
Rhoades, Elizabeth, Gafni, Ari
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Role of Zinc in Human Islet Amyloid Polypeptide Aggregation [PDF]
Journal of the American Chemical Society, 2010 Human Islet Amyloid Polypeptide (hIAPP) is a highly amyloidogenic protein found in islet cells of patients with type II diabetes. Because hIAPP is highly toxic to beta-cells under certain conditions, it has been proposed that hIAPP is linked to the loss of beta-cells and insulin secretion in type II diabetics.
Jeffrey R, Brender +7 more
openaire +2 more sources