Proteostasis of islet amyloid polypeptide: a molecular perspective of risk factors and protective strategies for type II diabetes

D Milardi, E Gazit, SE Radford, Y Xu… - Chemical …, 2021 - ACS Publications
The possible link between hIAPP accumulation and β-cell death in diabetic patients has
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …

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 …

Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils

Q Cao, DR Boyer, MR Sawaya, P Ge… - Nature structural & …, 2020 - nature.com
Human islet amyloid polypeptide (hIAPP) functions as a glucose-regulating hormone but
deposits as amyloid fibrils in more than 90% of patients with type II diabetes (T2D). Here we …

Ion mobility spectrometry–mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors

LM Young, P Cao, DP Raleigh… - Journal of the …, 2014 - ACS Publications
The molecular mechanisms by which different proteins assemble into highly ordered fibrillar
deposits and cause disease remain topics of debate. Human amylin (also known as islet …

Role of zinc in human islet amyloid polypeptide aggregation

JR Brender, K Hartman, RPR Nanga… - Journal of the …, 2010 - ACS Publications
Human Islet Amyloid Polypeptide (hIAPP) is a highly amyloidogenic protein found in islet
cells of patients with type II diabetes. Because hIAPP is highly toxic to β-cells under certain …

[HTML][HTML] Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity

P Cao, P Marek, H Noor, V Patsalo, LH Tu, H Wang… - FEBS letters, 2013 - Elsevier
Pancreatic islet amyloid is a characteristic feature of type 2 diabetes. The major protein
component of islet amyloid is the polypeptide hormone known as islet amyloid polypeptide …

Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence

R Wetzel - Journal of molecular biology, 2012 - Elsevier
Polyglutamine (polyQ) sequences of unknown normal function are present in a significant
number of proteins, and their repeat expansion is associated with a number of genetic …

Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor

CT Middleton, P Marek, P Cao, C Chiu, S Singh… - Nature …, 2012 - nature.com
Amyloid formation has been implicated in the pathology of over 20 human diseases, but the
rational design of amyloid inhibitors is hampered by a lack of structural information about …

Induction of de novo α-synuclein fibrillization in a neuronal model for Parkinson's disease

MB Fares, B Maco, A Oueslati… - Proceedings of the …, 2016 - National Acad Sciences
Lewy bodies (LBs) are intraneuronal inclusions consisting primarily of fibrillized human α-
synuclein (hα-Syn) protein, which represent the major pathological hallmark of Parkinson's …

Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols

P Cao, DP Raleigh - Biochemistry, 2012 - ACS Publications
Islet amyloid polypeptide (IAPP, amylin) is responsible for amyloid formation in type 2
diabetes and in transplanted islets. The flavanol (−)-epigallocatechin-3-gallate [EGCG;(2 R …