Islet amyloid polypeptide, islet amyloid, and diabetes mellitus

P Westermark, A Andersson… - Physiological …, 2011 - journals.physiology.org
Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of
the pancreatic islets of Langerhans. It is a regulatory peptide with putative function both …

Islet amyloid polypeptide: structure, function, and pathophysiology

R Akter, P Cao, H Noor, Z Ridgway… - Journal of diabetes …, 2016 - Wiley Online Library
The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose
homeostasis but aggregates to form islet amyloid in type‐2 diabetes. Islet amyloid formation …

Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR

S Luca, WM Yau, R Leapman, R Tycko - Biochemistry, 2007 - ACS Publications
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 …

Protein misfolding and aggregation in Alzheimer's disease and type 2 diabetes mellitus

G M. Ashraf, N H. Greig, T A. Khan… - CNS & Neurological …, 2014 - benthamdirect.com
In general, proteins can only execute their various biological functions when they are
appropriately folded. Their amino acid sequence encodes the relevant information required …

[HTML][HTML] Mechanisms of islet amyloidosis toxicity in type 2 diabetes

A Abedini, AM Schmidt - FEBS letters, 2013 - Elsevier
Amyloid formation by the neuropancreatic hormone, islet amyloid polypeptide (IAPP or
amylin), one of the most amyloidogenic sequences known, leads to islet amyloidosis in type …

Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution

SH Shim, R Gupta, YL Ling… - Proceedings of the …, 2009 - National Acad Sciences
There is considerable interest in uncovering the pathway of amyloid formation because the
toxic properties of amyloid likely stems from prefibril intermediates and not the fully formed …

The β-cell assassin: IAPP cytotoxicity

D Raleigh, X Zhang, B Hastoy… - Journal of molecular …, 2017 - jme.bioscientifica.com
Islet amyloid polypeptide (IAPP) forms cytotoxic oligomers and amyloid fibrils in islets in type
2 diabetes (T2DM). The causal factors for amyloid formation are largely unknown …

Understanding the role of protein glycation in the amyloid aggregation process

I Sirangelo, C Iannuzzi - International Journal of Molecular Sciences, 2021 - mdpi.com
Protein function and flexibility is directly related to the native distribution of its structural
elements and any alteration in protein architecture leads to several abnormalities and …

Uncovering the mechanism of aggregation of human transthyretin

L Saelices, LM Johnson, WY Liang, MR Sawaya… - Journal of Biological …, 2015 - ASBMB
The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon
dissociation and monomer unfolding. The aggregation of transthyretin has been reported as …

Human islet amyloid polypeptide monomers form ordered β-hairpins: a possible direct amyloidogenic precursor

NF Dupuis, C Wu, JE Shea… - Journal of the American …, 2009 - ACS Publications
Oligomerization of human islet amyloid polypeptide (IAPP) has been increasingly
considered a pathogenic process in type II diabetes. Here structural features of the IAPP …