Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid

S Chimon, MA Shaibat, CR Jones, DC Calero… - Nature structural & …, 2007 - nature.com
Diffusible subfibrillar aggregates of amyloid proteins are potent neurotoxins and primary
suspects in amyloid diseases including Alzheimer's disease. Despite widespread interest …

C-terminal turn stability determines assembly differences between Aβ40 and Aβ42

R Roychaudhuri, M Yang, A Deshpande… - Journal of molecular …, 2013 - Elsevier
Oligomerization of the amyloid β-protein (Aβ) is a seminal event in Alzheimer's disease.
Aβ42, which is only two amino acids longer than Aβ40, is particularly pathogenic. Why this is …

Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides

G Meisl, X Yang, E Hellstrand… - Proceedings of the …, 2014 - National Acad Sciences
The two major forms of the amyloid-beta (Aβ) peptide found in plaques in patients suffering
from Alzheimer's disease, Aβ40 and Aβ42, only differ by two amino acids in the C-terminal …

Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Aβ42 peptide

W Kim, MH Hecht - Proceedings of the National Academy of …, 2006 - National Acad Sciences
One hundred years ago, Alois Alzheimer observed a relationship between cognitive
impairment and the presence of plaque in the brains of patients suffering from the disease …

Supramolecular structural constraints on Alzheimer's β-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance

ON Antzutkin, RD Leapman, JJ Balbach, R Tycko - Biochemistry, 2002 - ACS Publications
We describe electron microscopy (EM), scanning transmission electron microscopy (STEM),
and solid-state nuclear magnetic resonance (NMR) measurements on amyloid fibrils formed …

Interprotofilament interactions between Alzheimer's Aβ1–42 peptides in amyloid fibrils revealed by cryoEM

R Zhang, X Hu, H Khant, SJ Ludtke… - Proceedings of the …, 2009 - National Acad Sciences
Alzheimer's disease is a neurodegenerative disorder characterized by the accumulation of
amyloid plaques in the brain. This amyloid primarily contains amyloid-β (Aβ), a 39-to 43-aa …

Unraveling the secrets of Alzheimer's β-amyloid fibrils

LK Thompson - Proceedings of the National Academy of …, 2003 - National Acad Sciences
Proteins adopt an amazing array of sequence-dependent struc-tures that enable them to
perform the many chemical functions critical to life. Over the past decade, however, it has …

Cross-strand pairing and amyloid assembly

Y Liang, SV Pingali, AS Jogalekar, JP Snyder… - Biochemistry, 2008 - ACS Publications
Amino acid cross-strand pairing interactions along a β-sheet surface have been implicated
in protein β-structural assembly and stability, yet the relative contributions have been difficult …

Antiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide

E Cerf, R Sarroukh, S Tamamizu-Kato… - Biochemical …, 2009 - portlandpress.com
AD (Alzheimer's disease) is linked to Aβ (amyloid β-peptide) misfolding. Studies
demonstrate that the level of soluble Aβ oligomeric forms correlates better with the …

Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly

DE Otzen, O Kristensen… - Proceedings of the …, 2000 - National Acad Sciences
Limited solubility and precipitation of amyloidogenic sequences such as the Alzheimer
peptide (β-AP) are major obstacles to a molecular understanding of protein fibrillation and …