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-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 …

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

MD Tuttle, G Comellas, AJ Nieuwkoop… - Nature structural & …, 2016 - nature.com
Misfolded α-synuclein amyloid fibrils are the principal components of Lewy bodies and
neurites, hallmarks of Parkinson's disease (PD). We present a high-resolution structure of an …

Solid-state NMR: Methods for biological solids

S Ahlawat, KR Mote, NA Lakomek… - Chemical Reviews, 2022 - ACS Publications
In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology

MI Ivanova, Y Lin, YH Lee, J Zheng… - Biophysical chemistry, 2021 - Elsevier
Abnormal aggregation of proteins into filamentous aggregates commonly associates with
many diseases, such as Alzheimer's disease, Parkinson's disease and type-2 diabetes …

AGGRESCAN: a server for the prediction and evaluation of" hot spots" of aggregation in polypeptides

O Conchillo-Solé, NS de Groot, FX Avilés, J Vendrell… - BMC …, 2007 - Springer
Background Protein aggregation correlates with the development of several debilitating
human disorders of growing incidence, such as Alzheimer's and Parkinson's diseases. On …

Functional amyloid–from bacteria to humans

DM Fowler, AV Koulov, WE Balch, JW Kelly - Trends in biochemical …, 2007 - cell.com
Amyloid–a fibrillar, cross β-sheet quaternary structure–was first discovered in the context of
human disease and tissue damage, and was thought to always be detrimental to the host …

Solid-state NMR studies of amyloid fibril structure

R Tycko - Annual review of physical chemistry, 2011 - annualreviews.org
Current interest in amyloid fibrils stems from their involvement in neurodegenerative and
other diseases and from their role as an alternative structural state for many peptides and …

The fold of α-synuclein fibrils

M Vilar, HT Chou, T Lührs, SK Maji… - Proceedings of the …, 2008 - National Acad Sciences
The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative
diseases. In Parkinson's disease it is believed that the aggregation of α-synuclein (α-syn) …

Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR

S Luca, WM Yau, R Leapman, R Tycko - Biochemistry, 2007 - ACS Publications
The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are
the main peptide or protein component of amyloid that develops in the pancreas of type 2 …