2008/10/10 by Robin Roychaudhuri, Mingfeng Yang, Minako Hoshi +1 · 1 citation
Medicine · Biochemistry, Genetics and Molecular Biology · Computer Science · Neuroscience · Chemistry · #Alzheimer's disease research and treatments #Prion Diseases and Protein Misfolding #Computational Drug Discovery Methods #Disease #Amyloid fibril #Protein folding #Amyloid (mycology) #Fibril #Biochemistry of Alzheimer's disease #P3 peptide #Neuroscience #Protein aggregation #Alzheimer's disease #Amyloid β #Chemistry #Medicine #Amyloid precursor protein #Biology #Pathology #Cell biology #Biochemistry
paper · pdf · doi:10.1074/jbc.r800036200
openalex publication_date 2008/10/10 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
The biochemistry of amyloid proteins has been a fascinating and important area of research because of its contribution to our understanding of protein folding dynamics and assembly and of the pathogenetic mechanisms of human disease. One such disease is AD,2 the most common neurodegenerative disorder of aging. In AD, Aβ (Fig. 1A), which is expressed normally and ubiquitously throughout life as a 40–42-residue peptide, forms fibrils that deposit in the brain as “amyloid plaques.” This pathologic deposition process led researchers to investigate fibril formation as a target for therapeutic intervention.