[HTML][HTML] Amyloid polymorphism: structural basis and neurobiological relevance

R Tycko - Neuron, 2015 - cell.com
Our understanding of the molecular structures of amyloid fibrils that are associated with
neurodegenerative diseases, of mechanisms by which disease-associated peptides and …

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

M Biancalana, S Koide - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2010 - Elsevier
Intense efforts to detect, diagnose, and analyze the kinetic and structural properties of
amyloid fibrils have generated a powerful toolkit of amyloid-specific molecular probes. Since …

Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils

M Ahmed, J Davis, D Aucoin, T Sato, S Ahuja… - Nature structural & …, 2010 - nature.com
Abstract The amyloid-β1–42 (Aβ42) peptide rapidly aggregates to form oligomers, protofibils
and fibrils en route to the deposition of amyloid plaques associated with Alzheimer's …

Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

SA Sievers, J Karanicolas, HW Chang, A Zhao, L Jiang… - Nature, 2011 - nature.com
Many globular and natively disordered proteins can convert into amyloid fibrils. These fibrils
are associated with numerous pathologies as well as with normal cellular functions,, and …

Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils

J Bieschke, M Herbst, T Wiglenda, RP Friedrich… - Nature chemical …, 2012 - nature.com
Several lines of evidence indicate that prefibrillar assemblies of amyloid-β (Aβ)
polypeptides, such as soluble oligomers or protofibrils, rather than mature, end-stage …

Exploring pathological link between antimicrobial and amyloid peptides

Y Tang, Y Zhang, D Zhang, Y Liu, R Nussinov… - Chemical Society …, 2024 - pubs.rsc.org
Amyloid peptides (AMYs) and antimicrobial peptides (AMPs) are considered as the two
distinct families of peptides, characterized by their unique sequences, structures, biological …

Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process

E Hellstrand, B Boland, DM Walsh… - ACS chemical …, 2010 - ACS Publications
Protein aggregation can lead to major disturbances of cellular processes and is associated
with several diseases. We report kinetic and equilibrium data by ThT fluorescence and …

The chemistry of Alzheimer's disease

A Rauk - Chemical Society Reviews, 2009 - pubs.rsc.org
The chemistry of Alzheimer’s disease - Chemical Society Reviews (RSC Publishing) DOI:10.1039/B807980N
Royal Society of Chemistry View PDF VersionPrevious ArticleNext Article DOI: 10.1039/B807980N …

A New Structural Model of Aβ40 Fibrils

I Bertini, L Gonnelli, C Luchinat, J Mao… - Journal of the American …, 2011 - ACS Publications
The amyloid fibrils of beta-amyloid (Aβ) peptides play important roles in the pathology of
Alzheimer's disease. Comprehensive solid-state NMR (SSNMR) structural studies on …

Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies

M Biancalana, K Makabe, A Koide, S Koide - Journal of molecular biology, 2009 - Elsevier
A number of small organic molecules have been developed that bind to amyloid fibrils, a
subset of which also inhibit fibrillization. Among these, the benzothiol dye Thioflavin-T (ThT) …