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 …
How melittin inserts into cell membrane: conformational changes, inter-peptide cooperation, and disturbance on the membrane
J Hong, X Lu, Z Deng, S Xiao, B Yuan, K Yang - Molecules, 2019 - mdpi.com
Antimicrobial peptides (AMPs), as a key component of the immune defense systems of
organisms, are a promising solution to the serious threat of drug-resistant bacteria to public …
organisms, are a promising solution to the serious threat of drug-resistant bacteria to public …
Modulation of disordered proteins with a focus on neurodegenerative diseases and other pathologies
Intrinsically disordered proteins (IDPs) do not have rigid 3D structures, showing changes in
their folding depending on the environment or ligands. Intrinsically disordered proteins are …
their folding depending on the environment or ligands. Intrinsically disordered proteins are …
Molecular insights into the oligomerization dynamics and conformations of amyloidogenic and non-amyloidogenic amylin from discrete molecular dynamics …
The amyloid aggregation of human islet amyloid polypeptide (hIAPP) is associated with
pancreatic β-cell death in type 2 diabetes. The S20G substitution of hIAPP (hIAPP (S20G)) …
pancreatic β-cell death in type 2 diabetes. The S20G substitution of hIAPP (hIAPP (S20G)) …
Computer simulations of protein–membrane systems
The interactions between proteins and membranes play critical roles in signal transduction,
cell motility, and transport, and they are involved in many types of diseases. Molecular …
cell motility, and transport, and they are involved in many types of diseases. Molecular …
[HTML][HTML] Silybins inhibit human IAPP amyloid growth and toxicity through stereospecific interactions
S García-Viñuales, IM Ilie, AM Santoro… - … et Biophysica Acta (BBA …, 2022 - Elsevier
Type 2 Diabetes is a major public health threat, and its prevalence is increasing worldwide.
The abnormal accumulation of islet amyloid polypeptide (IAPP) in pancreatic β-cells is …
The abnormal accumulation of islet amyloid polypeptide (IAPP) in pancreatic β-cells is …
Molecular Dynamics Simulations of the Tau Amyloid Fibril Core Dimer at the Surface of a Lipid Bilayer Model: I. In Alzheimer's Disease
PH Nguyen, P Derreumaux - The Journal of Physical Chemistry B, 2022 - ACS Publications
A tau R3–R4 domain spanning residues 306–378 was shown to form an amyloid fibril core
of a full-length tau in the brain of patients with Alzheimer's disease. Recently, we studied the …
of a full-length tau in the brain of patients with Alzheimer's disease. Recently, we studied the …
Metastable intermediate during hIAPP aggregation catalyzed by membranes as detected with 2D IR spectroscopy
The aggregation of human islet amyloid polypeptide (hIAPP) into amyloid fibrils involves
formation of oligomeric intermediates that are thought to be the cytotoxic species …
formation of oligomeric intermediates that are thought to be the cytotoxic species …
Evidence of the different effect of mercury and cadmium on the hIAPP aggregation process
Abstract hIAPP is a hormone consisting of 37 aminoacids that shows a strong tendency to
self-assemble into β-sheet-rich aggregates, which evolve to form insoluble aggregates that …
self-assemble into β-sheet-rich aggregates, which evolve to form insoluble aggregates that …
Phytoconstituents of Ashwagandha as potential inhibitors of human islet amyloid polypeptide (hIAPP): an in silico investigation
Amylin or human islet amyloid polypeptide (hIAPP) is a small peptide co-secreted with
insulin. Its peripheral aggregation on the lipid bilayer leads to fibril formation. The formation …
insulin. Its peripheral aggregation on the lipid bilayer leads to fibril formation. The formation …