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 …

Functional amyloids

D Otzen, R Riek - Cold Spring Harbor perspectives in …, 2019 - cshperspectives.cshlp.org
When protein/peptides aggregate, they usually form the amyloid state consisting of cross β-
sheet structure built by repetitively stacked β-strands forming long fibrils. Amyloids are …

Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2

TR Alderson, I Pritišanac, Đ Kolarić, AM Moses… - Proceedings of the …, 2023 - pnas.org
The AlphaFold Protein Structure Database contains predicted structures for millions of
proteins. For the majority of human proteins that contain intrinsically disordered regions …

Protein structure determination using metagenome sequence data

S Ovchinnikov, H Park, N Varghese, PS Huang… - Science, 2017 - science.org
Despite decades of work by structural biologists, there are still~ 5200 protein families with
unknown structure outside the range of comparative modeling. We show that Rosetta …

Simulation studies of amyloidogenic polypeptides and their aggregates

IM Ilie, A Caflisch - Chemical reviews, 2019 - ACS Publications
Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …

Structural analysis and architectural principles of the bacterial amyloid curli

M Sleutel, B Pradhan, AN Volkov, H Remaut - Nature Communications, 2023 - nature.com
Two decades have passed since the initial proposition that amyloids are not only (toxic)
byproducts of an unintended aggregation cascade, but that they can also be produced by an …

Large-scale determination of previously unsolved protein structures using evolutionary information

S Ovchinnikov, L Kinch, H Park, Y Liao, J Pei, DE Kim… - elife, 2015 - elifesciences.org
The prediction of the structures of proteins without detectable sequence similarity to any
protein of known structure remains an outstanding scientific challenge. Here we report …

Uncovering the universality of self-replication in protein aggregation and its link to disease

G Meisl, CK Xu, JD Taylor, TCT Michaels, A Levin… - Science …, 2022 - science.org
Fibrillar protein aggregates are a hallmark of a range of human disorders, from prion
diseases to dementias, but are also encountered in several functional contexts. Yet, the …

[HTML][HTML] On the potential of machine learning to examine the relationship between sequence, structure, dynamics and function of intrinsically disordered proteins

K Lindorff-Larsen, BB Kragelund - Journal of Molecular Biology, 2021 - Elsevier
Intrinsically disordered proteins (IDPs) constitute a broad set of proteins with few uniting and
many diverging properties. IDPs—and intrinsically disordered regions (IDRs) interspersed …

Functional amyloids from bacterial biofilms–structural properties and interaction partners

Ü Akbey, M Andreasen - Chemical Science, 2022 - pubs.rsc.org
Protein aggregation and amyloid formation have historically been linked with various
diseases such as Alzheimer's and Parkinson's disease, but recently functional amyloids …