Half a century of amyloids: past, present and future

PC Ke, R Zhou, LC Serpell, R Riek… - Chemical Society …, 2020 - pubs.rsc.org
Amyloid diseases are global epidemics with profound health, social and economic
implications and yet remain without a cure. This dire situation calls for research into the …

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 …

In vivo aspects of protein folding and quality control

D Balchin, M Hayer-Hartl, FU Hartl - Science, 2016 - science.org
BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …

Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide

TCT Michaels, A Šarić, S Curk, K Bernfur, P Arosio… - Nature …, 2020 - nature.com
Oligomeric species populated during the aggregation of the Aβ42 peptide have been
identified as potent cytotoxins linked to Alzheimer's disease, but the fundamental molecular …

Secondary nucleation in amyloid formation

M Törnquist, TCT Michaels, K Sanagavarapu… - Chemical …, 2018 - pubs.rsc.org
Nucleation of new peptide and protein aggregates on the surfaces of amyloid fibrils of the
same peptide or protein has emerged in the past two decades as a major pathway for both …

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

MT Colvin, R Silvers, QZ Ni, TV Can… - Journal of the …, 2016 - ACS Publications
Amyloid-β (Aβ) is a 39–42 residue protein produced by the cleavage of the amyloid
precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that …

Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies

S Linse, T Scheidt, K Bernfur, M Vendruscolo… - Nature structural & …, 2020 - nature.com
The amyloid cascade hypothesis, according to which the self-assembly of amyloid-β peptide
(Aβ) is a causative process in Alzheimer's disease, has driven many therapeutic efforts for …

Towards an understanding of amyloid-β oligomers: characterization, toxicity mechanisms, and inhibitors

SJC Lee, E Nam, HJ Lee, MG Savelieff… - Chemical Society …, 2017 - pubs.rsc.org
Alzheimer's disease (AD) is characterized by an imbalance between production and
clearance of amyloid-β (Aβ) species. Aβ peptides can transform structurally from monomers …

The activities of amyloids from a structural perspective

R Riek, DS Eisenberg - Nature, 2016 - nature.com
The aggregation of proteins into structures known as amyloids is observed in many
neurodegenerative diseases, including Alzheimer's disease. Amyloids are composed of …