2017/05/30 by Michel Goedert, Maria Grazia Spillantini · 1 citation
Medicine · Biochemistry, Genetics and Molecular Biology · Neuroscience · Chemistry · #Alzheimer's disease research and treatments #Prion Diseases and Protein Misfolding #Neurological diseases and metabolism #Fibril #Neurodegeneration #Prion protein #Protein aggregation #Biophysics #Chemistry #Tau protein #Neuroscience #Amyloid fibril #Amyloid β #Biology #Disease #Biochemistry #Alzheimer's disease #Medicine #Pathology
paper · pdf · doi:10.1186/s13041-017-0298-7
openalex publication_date 2017/05/30 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/29
Since 2009, evidence has accumulated to suggest that Tau aggregates form first in a small number of brain cells, from where they propagate to other regions, resulting in neurodegeneration and disease. Propagation of Tau aggregates is often called prion-like, which refers to the capacity of an assembled protein to induce the same abnormal conformation in a protein of the same kind, initiating a self-amplifying cascade. In addition, prion-like encompasses the release of protein aggregates from brain cells and their uptake by neighbouring cells. In mice, the intracerebral injection of Tau inclusions induced the ordered assembly of monomeric Tau, followed by its spreading to distant brain regions. Short fibrils constituted the major species of seed-competent Tau. The existence of several human Tauopathies with distinct fibril morphologies has led to the suggestion that different molecular conformers (or strains) of aggregated Tau exist.