[HTML][HTML] Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide

R Azriel, E Gazit - Journal of Biological Chemistry, 2001 - ASBMB
The development of type II diabetes was shown to be associated with the formation of
amyloid fibrils consisted of the islet amyloid polypeptide (IAPP or amylin). Recently, a short …

Structure of cat islet amyloid polypeptide and identification of amino acid residues of potential significance for islet amyloid formation

C Betsholtz, L Christmanson, U Engström… - Diabetes, 1990 - Am Diabetes Assoc
Cats and humans, unlike most rodent species, develop amyloid in the islets of Langerhans
in conjunction with non-insulin-dependent diabetes mellitus. The amyloid consists of a 37 …

The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid …

P Cao, F Meng, A Abedini, DP Raleigh - Biochemistry, 2010 - ACS Publications
Islet amyloid polypeptide (IAPP) is a 37-residue polypeptide hormone that is responsible for
islet amyloid formation in type II diabetes. Human IAPP is extremely amyloidogenic, while rat …

Amyloidogenicity of naturally occurring full‐length animal IAPP variants

LM Palato, S Pilcher, A Oakes, A Lamba… - Journal of Peptide …, 2019 - Wiley Online Library
The aggregation of the 37‐amino acid polypeptide human islet amyloid polypeptide (hIAPP),
as either insoluble amyloid or as small oligomers, appears to play a direct role in the death …

Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.

P Westermark, U Engström… - Proceedings of the …, 1990 - National Acad Sciences
Islet amyloid polypeptide (IAPP), a putative polypeptide hormone, is a product of pancreatic
beta-cells and the major constituent of the amyloid deposits seen mainly in islets of type 2 …

Aggregation of an amyloidogenic fragment of human islet amyloid polypeptide

E Rhoades, J Agarwal, A Gafni - … et Biophysica Acta (BBA)-Protein Structure …, 2000 - Elsevier
Native human islet amyloid polypeptide (hIAPP) has been identified as the major component
of amyloid plaques found in the pancreatic islets of Langerhans of persons affected by type …

The role of His-18 in amyloid formation by human islet amyloid polypeptide

A Abedini, DP Raleigh - Biochemistry, 2005 - ACS Publications
The 37-residue islet amyloid polypeptide (IAPP) is the major protein component of the
amyloid deposits found in type-II diabetes. IAPP is stored in a relatively low pH environment …

Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human …

A Abedini, DP Raleigh - Journal of molecular biology, 2006 - Elsevier
Islet amyloid polypeptide (IAPP; amylin) is responsible for amyloid formation in type-2
diabetes. Not all organisms form islet amyloid, and amyloid formation correlates strongly …

Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology

P Marek, A Abedini, BB Song, M Kanungo… - Biochemistry, 2007 - ACS Publications
Amyloid formation has been implicated in a wide range of human diseases, and a diverse
set of proteins is involved. There is considerable interest in elucidating the interactions …

Role of aromatic interactions in amyloid formation by islet amyloid polypeptide

LH Tu, DP Raleigh - Biochemistry, 2013 - ACS Publications
Aromatic–aromatic and aromatic–hydrophobic interactions have been proposed to play a
role in amyloid formation by a range of polypeptides, including islet amyloid polypeptide …