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Computer modeling of human islet amyloid polypeptide

2016
It 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, 2015
Alzheimer'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, 2012
Protein 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, 1990
Van Jaarsveld, B. C.   +5 more
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