[HTML][HTML] 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 …

Amyloid formation as a protein phase transition

TCT Michaels, D Qian, A Šarić, M Vendruscolo… - Nature Reviews …, 2023 - nature.com
The formation of amyloid fibrils is a general class of protein self-assembly behaviour, which
is associated with both functional biology and the development of a number of disorders …

Apolipoprotein E and Alzheimer disease: pathobiology and targeting strategies

Y Yamazaki, N Zhao, TR Caulfield, CC Liu… - Nature Reviews …, 2019 - nature.com
Polymorphism in the apolipoprotein E (APOE) gene is a major genetic risk determinant of
late-onset Alzheimer disease (AD), with the APOE* ε 4 allele conferring an increased risk …

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 …

Amyloid-type protein aggregation and prion-like properties of amyloids

D Willbold, B Strodel, GF Schröder, W Hoyer… - Chemical …, 2021 - ACS Publications
This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade

F Chiti, CM Dobson - Annual review of biochemistry, 2017 - annualreviews.org
Peptides and proteins have been found to possess an inherent tendency to convert from
their native functional states into intractable amyloid aggregates. This phenomenon is …

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 …

[HTML][HTML] 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 …

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 …

Biopolymer nanofibrils: Structure, modeling, preparation, and applications

S Ling, W Chen, Y Fan, K Zheng, K Jin, H Yu… - Progress in polymer …, 2018 - Elsevier
Biopolymer nanofibrils exhibit exceptional mechanical properties with a unique combination
of strength and toughness, while also presenting biological functions that interact with the …