Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways

G Bitan, MD Kirkitadze, A Lomakin… - Proceedings of the …, 2003 - National Acad Sciences
Amyloid β-protein (Aβ) is linked to neuronal injury and death in Alzheimer's disease (AD). Of
particular relevance for elucidating the role of Aβ in AD is new evidence that oligomeric …

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 …

Elucidation of primary structure elements controlling early amyloid β-protein oligomerization

G Bitan, SS Vollers, DB Teplow - Journal of Biological Chemistry, 2003 - ASBMB
Assembly of monomeric amyloid β-protein (Aβ) into oligomeric structures is an important
pathogenetic feature of Alzheimer's disease. The oligomer size distributions of aggregate …

Amyloid β-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins

G Bitan, A Lomakin, DB Teplow - Journal of Biological Chemistry, 2001 - ASBMB
Assembly of the amyloid β-protein (Aβ) into neurotoxic oligomers and fibrils is a seminal
event in Alzheimer's disease. Understanding the earliest phases of Aβ assembly, including …

The Alzheimer's amyloid-β (1–42) peptide forms off-pathway oligomers and fibrils that are distinguished structurally by intermolecular organization

WM Tay, D Huang, TL Rosenberry… - Journal of Molecular …, 2013 - Elsevier
Increasing evidence suggests that soluble aggregates of amyloid-β (Aβ) initiate the
neurotoxicity that eventually leads to dementia in Alzheimer's disease. Knowledge on …

Residues 17–20 and 30–35 of beta‐amyloid play critical roles in aggregation

R Liu, C McAllister, Y Lyubchenko… - Journal of …, 2004 - Wiley Online Library
We examined the effects of co‐incubating nine different Aβ peptide fragments with full‐
length Aβ1–40 (Aβ40) on protein aggregation. Six fragments enhanced aggregation of Aβ40 …

Amyloid β-protein assembly and Alzheimer's disease: dodecamers of Aβ42, but not of Aβ40, seed fibril formation

NJ Economou, MJ Giammona, TD Do… - Journal of the …, 2016 - ACS Publications
Evidence suggests that oligomers of the 42-residue form of the amyloid β-protein (Aβ), Aβ42,
play a critical role in the etiology of Alzheimer's disease (AD). Here we use high resolution …

The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation

R Cukalevski, X Yang, G Meisl, U Weininger… - Chemical …, 2015 - pubs.rsc.org
The assembly of proteins into amyloid fibrils, a phenomenon central to several currently
incurable human diseases, is a process of high specificity that commonly tolerates only a …

Distinct early folding and aggregation properties of Alzheimer amyloid-β peptides Aβ40 and Aβ42: stable trimer or tetramer formation by Aβ42

YR Chen, CG Glabe - Journal of Biological Chemistry, 2006 - ASBMB
The amyloid β peptide (Aβ), composed of 40 or 42 amino acids, is a critical component in the
etiology of the neurodegenerative Alzheimer disease. Aβ is prone to aggregate and forms …

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 …