ThT 101: a primer on the use of thioflavin T to investigate amyloid formation

K Gade Malmos, LM Blancas-Mejia, B Weber… - Amyloid, 2017 - Taylor & Francis
Thioflavin T (ThT) has been widely used to investigate amyloid formation since 1989. While
concerns have recently been raised about its use as a probe specific for amyloid, ThT still …

Preparation of amyloid β‐protein for structural and functional studies

DB Teplow - Methods in enzymology, 2006 - Elsevier
Amyloid proteins cause a number of progressive, degenerative diseases. Among these is
Alzheimer's disease (AD), the etiology of which is linked to the formation of neurotoxic …

Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease

SL Bernstein, NF Dupuis, ND Lazo, T Wyttenbach… - Nature …, 2009 - nature.com
In recent years, small protein oligomers have been implicated in the aetiology of a number of
important amyloid diseases, such as type 2 diabetes, Parkinson's disease and Alzheimer's …

A partially folded structure of amyloid-beta (1–40) in an aqueous environment

S Vivekanandan, JR Brender, SY Lee… - Biochemical and …, 2011 - Elsevier
Aggregation of the Aβ1–40 peptide is linked to the development of extracellular plaques
characteristic of Alzheimer's disease. While previous studies commonly show the Aβ1–40 is …

Hydrophobic, aromatic, and electrostatic interactions play a central role in amyloid fibril formation and stability

KE Marshall, KL Morris, D Charlton, N O'Reilly… - Biochemistry, 2011 - ACS Publications
Amyloid-like fibrous crystals formed by the peptide KFFEAAAKKFFE have been previously
characterized and provide an ideal model system to examine the importance of specific …

Amyloid β-protein monomer folding: free-energy surfaces reveal alloform-specific differences

M Yang, DB Teplow - Journal of molecular biology, 2008 - Elsevier
Alloform-specific differences in structural dynamics between amyloid β-protein (Aβ) 40 and
Aβ42 appear to underlie the pathogenesis of Alzheimer's disease. To elucidate these …

Differences in the free energies between the excited states of Aβ40 and Aβ42 monomers encode their aggregation propensities

D Chakraborty, JE Straub… - Proceedings of the …, 2020 - National Acad Sciences
The early events in the aggregation of the intrinsically disordered peptide, amyloid-β (A β),
involve transitions from the disordered free energy ground state to assembly-competent …

[HTML][HTML] Aβ–ganglioside interactions in the pathogenesis of Alzheimer's disease

K Matsuzaki - Biochimica et Biophysica Acta (BBA)-Biomembranes, 2020 - Elsevier
It is widely accepted that the abnormal self-association of amyloid β-protein (Aβ) is central to
the pathogenesis of Alzheimer's disease, the most common form of dementia. Accumulating …

[HTML][HTML] Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid β-protein assembly and toxicity

K Ono, MM Condron, DB Teplow - Journal of Biological Chemistry, 2010 - ASBMB
Mutations in the amyloid β-protein (Aβ) precursor gene cause autosomal dominant
Alzheimer disease in a number of kindreds. In two such kindreds, the English and the Tottori …

A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity

S Sinha, DHJ Lopes, G Bitan - ACS Chemical Neuroscience, 2012 - ACS Publications
A combination of hydrophobic and electrostatic interactions is important in initiating the
aberrant self-assembly process that leads to formation of toxic oligomers and aggregates by …