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 …

Metal binding sites in amyloid oligomers: Complexes and mechanisms

Y Miller, B Ma, R Nussinov - Coordination Chemistry Reviews, 2012 - Elsevier
Neurodegenerative diseases constitute a worldwide health problem. Metal ions are
essential for life, but they are also involved in several neurodegenerative mechanisms such …

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 …

Dynamic α-helix structure of micelle-bound human amylin

SM Patil, S Xu, SR Sheftic, AT Alexandrescu - Journal of Biological …, 2009 - ASBMB
Amylin is an endocrine hormone that regulates metabolism. In patients afflicted with type 2
diabetes, amylin is found in fibrillar deposits in the pancreas. Membranes are thought to …

A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity

JR Brender, K Hartman, KR Reid, RT Kennedy… - Biochemistry, 2008 - ACS Publications
Islet amyloid polypeptide (IAPP or amylin) is a 37-residue peptide secreted with insulin by β-
cells in the islets of Langerhans. The aggregation of the peptide into either amyloid fibers or …

Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy

RPR Nanga, JR Brender, J Xu, K Hartman… - Journal of the …, 2009 - ACS Publications
Islet amyloid polypeptide (IAPP or amylin) is a 37-residue peptide hormone associated with
glucose metabolism that is cosecreted with insulin by β-cells in the pancreas. Since human …

[HTML][HTML] Interaction of amylin species with transition metals and membranes

M Alghrably, I Czaban, Ł Jaremko… - Journal of inorganic …, 2019 - Elsevier
Abstract Islet Amyloid Polypeptide (IAPP), also known as amylin, is a 37-amino-acid peptide
hormone that is secreted by pancreatic islet β-cells. Amylin is complementary to insulin in …

Amyloidogenic intrinsically disordered proteins: new insights into their self-assembly and their interaction with membranes

F Scollo, C La Rosa - Life, 2020 - mdpi.com
Aβ, IAPP, α-synuclein, and prion proteins belong to the amyloidogenic intrinsically
disordered proteins' family; indeed, they lack well defined secondary and tertiary structures …

[HTML][HTML] Extracellular truncated tau causes early presynaptic dysfunction associated with Alzheimer's disease and other tauopathies

F Florenzano, C Veronica, G Ciasca, MT Ciotti… - Oncotarget, 2017 - ncbi.nlm.nih.gov
The largest part of tau secreted from AD nerve terminals and released in cerebral spinal fluid
(CSF) is C-terminally truncated, soluble and unaggregated supporting potential extracellular …

The role of copper(ii) in the aggregation of human amylin

A Sinopoli, A Magrì, D Milardi, M Pappalardo… - Metallomics, 2014 - academic.oup.com
Amylin is a 37-residue peptide hormone produced by the islet β-cells of pancreas and the
formation of amylin aggregates is strongly associated with β-cell degeneration in type 2 …