A unifying framework for amyloid-mediated membrane damage: The lipid-chaperone hypothesis

C Tempra, F Scollo, M Pannuzzo, F Lolicato… - … et Biophysica Acta (BBA …, 2022 - Elsevier
Over the past thirty years, researchers have highlighted the role played by a class of proteins
or polypeptides that forms pathogenic amyloid aggregates in vivo, including i) the amyloid …

The human islet amyloid polypeptide in protein misfolding disorders: Mechanisms of aggregation and interaction with biomembranes

A El Saghir, G Farrugia, N Vassallo - Chemistry and Physics of Lipids, 2021 - Elsevier
Human islet amyloid polypeptide (hIAPP), otherwise known as amylin, is a 37-residue
peptide hormone which is reported to be a common factor in protein misfolding disorders …

The mechanistic basis of the membrane‐permeabilizing activities of the virulence‐associated protein A (VapA) from Rhodococcus equi

C Nehls, M Schröder, T Haubenthal… - Molecular …, 2024 - Wiley Online Library
Pathogenic Rhodococcus equi release the virulence‐associated protein A (VapA) within
macrophage phagosomes. VapA permeabilizes phagosome and lysosome membranes and …

The hazardous effects of the environmental toxic gases on amyloid beta-peptide aggregation: A theoretical perspective

V Saranya, PV Mary, S Vijayakumar, R Shankar - Biophysical Chemistry, 2020 - Elsevier
Alzheimer's disease (AD) is one of the leading causes of dementia in elderly people. It has
been well documented that the exposure to environmental toxins such as CO, CO 2, SO 2 …

Dmpc phospholipid bilayer as a potential interface for human cystatin c oligomerization: analysis of protein-liposome interactions using NMR spectroscopy

P Jurczak, K Szutkowski, S Lach, S Jurga… - Membranes, 2020 - mdpi.com
Studies revolving around mechanisms responsible for the development of amyloid-based
diseases lay the foundations for the recognition of molecular targets of future to-be …

[HTML][HTML] Development of a novel fluorescence assay for studying lipid bilayer perturbation induced by amyloidogenic peptides using cell plasma membrane vesicles

M Sebastiao, M Babych, N Quittot, K Kumar… - … et Biophysica Acta (BBA …, 2023 - Elsevier
Numerous pathophysiological conditions are associated with the misfolding and
aggregation of proteins into insoluble amyloid fibrils. The mechanisms by which this process …

Unpacking the aggregation-oligomerization-fibrillization process of naturally-occurring hIAPP amyloid oligomers isolated directly from sera of children with obesity or …

MM Altamirano-Bustamante… - Scientific Reports, 2019 - nature.com
The formation of amyloid oligomers and fibrils of the human islet amyloid polypeptide
(hIAPP) has been linked with β-cell failure and death which causes the onset, progression …

Protein-conformational diseases in childhood: Naturally-occurring hIAPP amyloid-oligomers and early β-cell damage in obesity and diabetes

NF Altamirano-Bustamante, E Garrido-Magaña… - Plos one, 2020 - journals.plos.org
Background and aims This is the first time that obesity and diabetes mellitus (DM) as protein
conformational diseases (PCD) are reported in children and they are typically diagnosed too …

Exploring interactions between lipids and amyloid-forming proteins: a review on applying fluorescence and NMR techniques

Z Chang, J Deng, W Zhao, J Yang - Chemistry and Physics of Lipids, 2021 - Elsevier
A hallmark of Alzheimer's, Parkinson's, and other amyloid diseases is the assembly of
amyloid proteins into amyloid aggregates or fibrils. In many cases, the formation and …

Combining molecular dynamics simulations and experimental analyses in protein misfolding

H Wille, L Dorosh, S Amidian, G Schmitt-Ulms… - Advances in Protein …, 2019 - Elsevier
The fold of a protein determines its function and its misfolding can result in loss-of-function
defects. In addition, for certain proteins their misfolding can lead to gain-of-function toxicities …