The proteostasis network and its decline in ageing

MS Hipp, P Kasturi, FU Hartl - Nature reviews Molecular cell biology, 2019 - nature.com
Ageing is a major risk factor for the development of many diseases, prominently including
neurodegenerative disorders such as Alzheimer disease and Parkinson disease. A hallmark …

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

G Wei, Z Su, NP Reynolds, P Arosio… - Chemical Society …, 2017 - pubs.rsc.org
Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

The amyloid state and its association with protein misfolding diseases

TPJ Knowles, M Vendruscolo… - Nature reviews Molecular …, 2014 - nature.com
The phenomenon of protein aggregation and amyloid formation has become the subject of
rapidly increasing research activities across a wide range of scientific disciplines. Such …

Molecular mechanisms of protein aggregation from global fitting of kinetic models

G Meisl, JB Kirkegaard, P Arosio, TCT Michaels… - Nature protocols, 2016 - nature.com
The elucidation of the molecular mechanisms by which soluble proteins convert into their
amyloid forms is a fundamental prerequisite for understanding and controlling disorders that …

On the lag phase in amyloid fibril formation

P Arosio, TPJ Knowles, S Linse - Physical Chemistry Chemical Physics, 2015 - pubs.rsc.org
The formation of nanoscale amyloid fibrils from normally soluble peptides and proteins is a
common form of self-assembly phenomenon that has fundamental connections with …

Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes

J Habchi, S Chia, C Galvagnion, TCT Michaels… - Nature …, 2018 - nature.com
Alzheimer's disease is a neurodegenerative disorder associated with the aberrant
aggregation of the amyloid-β peptide. Although increasing evidence implicates cholesterol …

The role of lipids interacting with α-synuclein in the pathogenesis of Parkinson's disease

C Galvagnion - Journal of Parkinson's disease, 2017 - content.iospress.com
Abstract α-synuclein is a small protein abundantly expressed in the brain and mainly located
in synaptic terminals. The conversion of α-synuclein into oligomers and fibrils is the hallmark …

Chemical kinetics for bridging molecular mechanisms and macroscopic measurements of amyloid fibril formation

TCT Michaels, A Šarić, J Habchi, S Chia… - Annual review of …, 2018 - annualreviews.org
Understanding how normally soluble peptides and proteins aggregate to form amyloid fibrils
is central to many areas of modern biomolecular science, ranging from the development of …

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

P Arosio, TCT Michaels, S Linse, C Månsson… - Nature …, 2016 - nature.com
It is increasingly recognized that molecular chaperones play a key role in modulating the
formation of amyloid fibrils, a process associated with a wide range of human disorders …

Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease

J Habchi, S Chia, R Limbocker… - Proceedings of the …, 2017 - National Acad Sciences
The aggregation of the 42-residue form of the amyloid-β peptide (Aβ42) is a pivotal event in
Alzheimer's disease (AD). The use of chemical kinetics has recently enabled highly accurate …