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 …

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 …

Structural properties of Aβ protofibrils stabilized by a small molecule

AD Williams, M Sega, M Chen… - Proceedings of the …, 2005 - National Acad Sciences
Metastable oligomeric and protofibrillar forms of amyloidogenic proteins have been
implicated as on-pathway assembly intermediates in amyloid formation and as the major …

Amyloid β-Protein:  Monomer Structure and Early Aggregation States of Aβ42 and Its Pro19 Alloform

SL Bernstein, T Wyttenbach… - Journal of the …, 2005 - ACS Publications
The amyloid β-protein (Aβ) is a seminal neuropathic agent in Alzheimer's disease (AD).
Recent evidence points to soluble Aβ oligomers as the probable neurotoxic species. Among …

Nanoscale Characterization of Parallel and Antiparallel β-Sheet Amyloid Beta 1–42 Aggregates

K Zhaliazka, D Kurouski - ACS chemical neuroscience, 2022 - ACS Publications
Abrupt aggregation of amyloid beta (Aβ) peptide is strongly associated with Alzheimer's
disease. In this study, we used atomic force microscopy–infrared (AFM-IR) spectroscopy to …

Amyloid β-protein assembly and Alzheimer disease

R Roychaudhuri, M Yang, MM Hoshi… - Journal of Biological …, 2009 - ASBMB
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 …

High-resolution atomic force microscopy of soluble Aβ42 oligomers

IA Mastrangelo, M Ahmed, T Sato, W Liu… - Journal of molecular …, 2006 - Elsevier
Soluble oligomers and protofibrils are widely thought to be the toxic forms of the Aβ42
peptide associated with Alzheimer's disease. We have investigated the structure and …

Studies on the in vitro assembly of Aβ 1–40: implications for the search for Aβ fibril formation inhibitors

CS Goldsbury, S Wirtz, SA Müller, S Sunderji… - Journal of structural …, 2000 - Elsevier
The progressive deposition of the amyloid β peptide (Aβ) in fibrillar form is a key feature in
the development of the pathology in Alzheimer's disease (AD). We have characterized the …

On the nucleation of amyloid β‐protein monomer folding

ND Lazo, MA Grant, MC Condron, AC Rigby… - Protein …, 2005 - Wiley Online Library
Neurotoxic assemblies of the amyloid β‐protein (Aβ) have been linked strongly to the
pathogenesis of Alzheimer's disease (AD). Here, we sought to monitor the earliest step in Aβ …

High-speed atomic force microscopy reveals structural dynamics of amyloid β1–42 aggregates

T Watanabe-Nakayama, K Ono… - Proceedings of the …, 2016 - National Acad Sciences
Aggregation of amyloidogenic proteins into insoluble amyloid fibrils is implicated in various
neurodegenerative diseases. This process involves protein assembly into oligomeric …