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Computer modeling of human islet amyloid polypeptide
2016It is believed that a variety of human diseases are related to the misfolding of proteins or peptides. Amyloid fibrils are highly organized aggregates with a cross-? structure and are generated by misfolding of proteins. These aggregates are also related to disease. For instance, human islet amyloid polypeptide (hIAPP), ?-synuclein, and amyloid-?
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Cross-Seeding Interaction between β-Amyloid and Human Islet Amyloid Polypeptide
ACS Chemical Neuroscience, 2015Alzheimer's disease (AD) and type 2 diabetes (T2D) are two common protein misfolding diseases. Increasing evidence suggests that these two diseases may be correlated with each other via cross-sequence interactions between β-amyloid peptide (Aβ) associated with AD and human islet amyloid polypeptide (hIAPP) associated with T2D.
Rundong, Hu +4 more
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2D amyloid aggregation of human islet amyloid polypeptide at the solid–liquid interface
Soft Matter, 2012Protein misfolding, aggregation, and amyloid deposits are the common hallmarks of amyloid diseases, such as Alzheimer's disease, type 2 diabetes mellitus (T2DM), Huntington disease, prion disease, and Parkinson's disease. In the case of T2DM, the aggregation of human islet amyloid polypeptide (hIAPP) accumulates in the pancreatic islets, which has the ...
Yu, Y.-P. +6 more
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Islet-amyloid polypeptide in human plasma
The Lancet, 1990Van Jaarsveld, B. C. +5 more
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Design of Peptide-based Inhibitors of Human Islet Amyloid Polypeptide Fibrillogenesis
Journal of Molecular Biology, 2002Joanne Mclaurin
exaly

