Polymeric materials produced from fossil fuels have been intimately linked to the
development of industrial activities in the 20th century and, consequently, to the …

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 …

The gut microbiota is indispensable for maintaining host health by enhancing the host's
digestive capacity, safeguarding the intestinal epithelial barrier, and preventing pathogen …

Protein misfolding and aggregation, a key contributor to the progression of numerous
neurodegenerative diseases, results in functional deficiencies and the creation of harmful …

Fibrillar protein aggregates are characteristic of neurodegenerative diseases but represent
difficult targets for ligand design, because limited structural information about the binding …

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 …

Systemic ATTR amyloidosis is an increasingly important protein misfolding disease that is
provoked by the formation of amyloid fibrils from transthyretin protein. The pathological and …

Imaging of both the positions and orientations of single fluorophores, termed single-
molecule orientation-localization microscopy, is a powerful tool for the study of biochemical …

Amyloid formation is a hallmark of many medical diseases including diabetes type 2,
Alzheimer's and Parkinson diseases. Under these pathological conditions, misfolded …

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