Proteostasis of islet amyloid polypeptide: a molecular perspective of risk factors and protective strategies for type II diabetes
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 …
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …
Amyloidogenic protein–membrane interactions: mechanistic insight from model systems
SM Butterfield, HA Lashuel - Angewandte Chemie International …, 2010 - Wiley Online Library
The toxicity of amyloid‐forming proteins is correlated with their interactions with cell
membranes. Binding events between amyloidogenic proteins and membranes result in …
membranes. Binding events between amyloidogenic proteins and membranes result in …
Simulation studies of amyloidogenic polypeptides and their aggregates
Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …
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 …
homeostasis but aggregates to form islet amyloid in type‐2 diabetes. Islet amyloid formation …
Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective
JR Brender, S Salamekh… - Accounts of chemical …, 2012 - ACS Publications
The aggregation of proteins is tightly controlled in living systems, and misfolded proteins are
normally removed before aggregation of the misfolded protein can occur. But for reasons not …
normally removed before aggregation of the misfolded protein can occur. But for reasons not …
[HTML][HTML] Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment
Human islet amyloid polypeptide is a hormone coexpressed with insulin by pancreatic beta-
cells. For reasons not clearly understood, hIAPP aggregates in type II diabetics to form …
cells. For reasons not clearly understood, hIAPP aggregates in type II diabetics to form …
Looking beyond the core: the role of flanking regions in the aggregation of amyloidogenic peptides and proteins
Amyloid proteins are involved in many neurodegenerative disorders such as Alzheimer's
disease [Tau, Amyloid β (Aβ)], Parkinson's disease [alpha-synuclein (αSyn)], and …
disease [Tau, Amyloid β (Aβ)], Parkinson's disease [alpha-synuclein (αSyn)], and …
Role of zinc in human islet amyloid polypeptide aggregation
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 …
cells of patients with type II diabetes. Because hIAPP is highly toxic to β-cells under certain …
Truncated β-amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndrome
H Jang, FT Arce, S Ramachandran… - Proceedings of the …, 2010 - National Acad Sciences
Full-length amyloid beta peptides (Aβ1–40/42) form neuritic amyloid plaques in Alzheimer's
disease (AD) patients and are implicated in AD pathology. However, recent transgenic …
disease (AD) patients and are implicated in AD pathology. However, recent transgenic …
The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes
JA Hebda, AD Miranker - Annual review of biophysics, 2009 - annualreviews.org
The dynamics, energies, and structures governing protein folding are critical to biological
function. Amyloidoses are a class of disease defined, in part, by the misfolding and …
function. Amyloidoses are a class of disease defined, in part, by the misfolding and …