Molecular mechanisms of amyloid formation in living systems.
Ontology highlight
ABSTRACT: Fibrillar protein aggregation is a hallmark of a variety of human diseases. Examples include the deposition of amyloid-β and tau in Alzheimer's disease, and that of α-synuclein in Parkinson's disease. The molecular mechanisms by which soluble proteins form amyloid fibrils have been extensively studied in the test tube. These investigations have revealed the microscopic steps underlying amyloid formation, and the role of factors such as chaperones that modulate these processes. This perspective explores the question to what extent the mechanisms of amyloid formation elucidated in vitro apply to human disease. The answer is not yet clear, and may differ depending on the protein and the associated disease. Nevertheless, there are striking qualitative similarities between the aggregatio
SUBMITTER: Sinnige T
PROVIDER: S-EPMC9214716 | biostudies-literature | 2022 Jun
REPOSITORIES: biostudies-literature
ACCESS DATA