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 …

In most cases, protein aggregation stems from the establishment of non-native
intermolecular contacts. The formation of insoluble protein aggregates is associated with …

The abnormal assembly of TAR DNA-binding protein 43 (TDP-43) in neuronal and glial cells
characterizes nearly all cases of amyotrophic lateral sclerosis (ALS) and around half of …

Alpha-synuclein (αSyn) is a protein involved in neurodegenerative disorders including
Parkinson's disease. Amyloid formation of αSyn can be modulated by the 'P1 …

Cryoelectron microscopy (cryo-EM) has provided unprecedented insights into amyloid fibril
structures, including those associated with disease. However, these structures represent the …

Protein aggregation and amyloid formation have historically been linked with various
diseases such as Alzheimer's and Parkinson's disease, but recently functional amyloids …

Amyloid fibrils are a pathologically and functionally relevant state of protein folding, which is
generally accessible to polypeptide chains and differs fundamentally from the globular state …

Deposition of amyloid plaques in the brains of Alzheimer's disease (AD) patients is a
hallmark of the disease. AD plaques consist primarily of the beta-amyloid (Aβ) peptide but …

Amyloid fibril formation of α-synuclein (αS) is associated with multiple neurodegenerative
diseases, including Parkinson's disease (PD). Growing evidence suggests that progression …

The β-sheet–rich amyloid core is the defining feature of protein aggregates associated with
neurodegenerative disorders. Recent investigations have revealed that there exist multiple …