Pancreatic amyloid deposits, composed of the 37 amino acid residue peptide amylin,
represent an integral part of type 2 diabetes mellitus pathology. Human amylin (hA) forms …

Amyloiddeposits of fibrillar human amylin (hA) in the pancreas may be a causative factor in
type-2 diabetes. A detailed comparison of in vitro fibril formation by full-length hA (1–37) …

Human amylin is the primary component of amyloid deposits found in the pancreatic β-cells
of patients with type 2 diabetes mellitus. Recently, two fragments of amylin have been …

Amylin, also known as islet amyloid polypeptide (IAPP), is the major protein component of
the fibril deposits found in the pancreas of individuals with type II diabetes. The central …

Human amylin forms fibrillar amyloid between pancreatic islet cells in patients with non-
insulin-dependent (type 2) diabetes mellitus. Fibrillar assemblies also formin vitroin aqueous …

The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are
the main peptide or protein component of amyloid that develops in the pancreas of type 2 …

Pancreatic amyloid is found in more than 95% of type II diabetes patients. Pancreatic
amyloid is formed by the aggregation of islet amyloid polypeptide (hIAPP or amylin), which is …

Human amylin, or islet amyloid polypeptide, is a peptide cosecreted with insulin by the beta
cells of the pancreatic islets of Langerhans. The 37-residue, C-terminally amidated human …

Human amylin (hA), a 37-amino-acid polypeptide, is one of a number of peptides with the
ability to form amyloid fibrils and cause disease. It is the main constituent of the pancreatic …

Human amylin, a major constituent of pancreatic amyloid deposits, may be a pathogenetic
factor for noninsulin-dependent diabetes mellitus (NIDDM). We demonstrated that the …