Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

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 …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

The use of transgenic mice displaying amyloid-β (Aβ) brain pathology has been essential for
the preclinical assessment of new treatment strategies for Alzheimer's disease. However, the …

Most neurodegenerative diseases such as Alzheimer's disease, type 2 diabetes, Parkinson's
disease, etc. are caused by inclusions and plaques containing misfolded protein …

Neurodegenerative diseases are an increasingly common group of diseases that occur late
in life with a significant impact on personal, family, and economic life. Among these …

The prediction of highly ordered three-dimensional structures of amyloid protein fibrils from
the amino acid sequences of their monomeric self-assembly precursors constitutes a …

Two distinct diseases are associated with the deposition of fibrillar amyloid-β (Aβ) peptides
in the human brain in an age-dependent fashion. Alzheimer's disease is primarily …

Amyloid fibrils are supramolecular systems showing distinct chirality at different levels of
their complex multilayered architectures. Due to the regular long‐range chiral organization …

The misfolding and aggregation of amyloid-β (Aβ) peptides play a pivotal role in the
pathogenesis of Alzheimer's disease (AD). Aβ40 and Aβ42, the two primary isoforms of Aβ …