Mechanism of nucleated conformational conversion of Aβ42

Z Fu, D Aucoin, J Davis, WE Van Nostrand… - Biochemistry, 2015 - ACS Publications
Soluble oligomers and protofibrils of the Aβ42 peptide are neurotoxic intermediates in the
conversion of monomeric Aβ42 into the amyloid fibrils associated with Alzheimer's disease …

Assembly of Aβ amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease

JD Harper, SS Wong, CM Lieber, PT Lansbury - Biochemistry, 1999 - ACS Publications
Amyloid fibrils comprising primarily the peptides Aβ40 and Aβ42 are a defining feature of the
Alzheimer's disease (AD) brain, and convergent evidence suggests that the process of their …

Paired β-sheet structure of an Aβ (1-40) amyloid fibril revealed by electron microscopy

C Sachse, M Fändrich… - Proceedings of the …, 2008 - National Acad Sciences
Alzheimer's disease is a neurodegenerative disorder that is characterized by the cerebral
deposition of amyloid fibrils formed by Aβ peptide. Despite their prevalence in Alzheimer's …

Experimental evidence for the reorganization of β-strands within aggregates of the Aβ (16− 22) peptide

SA Petty, SM Decatur - Journal of the American Chemical Society, 2005 - ACS Publications
Amyloidogenic deposits that accumulate in brain tissue with the progression of Alzheimer's
disease contain large amounts of the amyloid β-peptide. A small fragment of this peptide …

Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation

W Hoyer, C Grönwall, A Jonsson… - Proceedings of the …, 2008 - National Acad Sciences
According to the amyloid hypothesis, the pathogenesis of Alzheimer's disease is triggered
by the oligomerization and aggregation of the amyloid-β (Aβ) peptide into protein plaques …

Recent progress in understanding Alzheimer's β-amyloid structures

M Fändrich, M Schmidt, N Grigorieff - Trends in biochemical sciences, 2011 - cell.com
The formation of amyloid fibrils, protofibrils and oligomers from the β-amyloid (Aβ) peptide
represents a hallmark of Alzheimer's disease. Aβ-peptide-derived assemblies might be …

Direct observations of amyloid β self-assembly in live cells provide insights into differences in the kinetics of Aβ (1–40) and Aβ (1–42) aggregation

EK Esbjörner, F Chan, E Rees, M Erdelyi, LM Luheshi… - Chemistry & biology, 2014 - cell.com
Insight into how amyloid β (Aβ) aggregation occurs in vivo is vital for understanding the
molecular pathways that underlie Alzheimer's disease and requires new techniques that …

Amyloid β-protein assembly: differential effects of the protective A2T mutation and recessive A2V familial Alzheimer's disease mutation

X Zheng, D Liu, R Roychaudhuri… - ACS chemical …, 2015 - ACS Publications
Oligomeric states of the amyloid β-protein (Aβ) appear to be causally related to Alzheimer's
disease (AD). Recently, two familial mutations in the amyloid precursor protein gene have …

Amino acid position-specific contributions to amyloid β-protein oligomerization

SK Maji, RRO Loo, M Inayathullah, SM Spring… - Journal of biological …, 2009 - ASBMB
Understanding the structural and assembly dynamics of the amyloid β-protein (Aβ) has
direct relevance to the development of therapeutic agents for Alzheimer disease. To …

Preparation of fluorescently‐labeled amyloid‐beta peptide assemblies: the effect of fluorophore conjugation on structure and function

LM Jungbauer, C Yu, KJ Laxton… - Journal of Molecular …, 2009 - Wiley Online Library
Recent research has focused on soluble oligomeric assemblies of the 42 amino acid isoform
of the amyloid‐beta peptide (Aβ42) as the proximal cause of neuronal injury, synaptic loss …