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 …

Review of the current state of protein aggregation inhibition from a materials chemistry perspective: Special focus on polymeric materials

R Rajan, S Ahmed, N Sharma, N Kumar, A Debas… - Materials …, 2021 - pubs.rsc.org
Protein instability caused by exposure to external additives or severe stress may result in
different diseases. Of these diseases, many are triggered by protein misfolding and …

TREM2 haplodeficiency in mice and humans impairs the microglia barrier function leading to decreased amyloid compaction and severe axonal dystrophy

P Yuan, C Condello, CD Keene, Y Wang, TD Bird… - Neuron, 2016 - cell.com
Haplodeficiency of the microglia gene TREM2 increases risk for late-onset Alzheimer's
disease (AD) but the mechanisms remain uncertain. To investigate this, we used high …

Implications of peptide assemblies in amyloid diseases

PC Ke, MA Sani, F Ding, A Kakinen, I Javed… - Chemical Society …, 2017 - pubs.rsc.org
Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …

Diffusible, nonfibrillar ligands derived from Aβ1–42 are potent central nervous system neurotoxins

MP Lambert, AK Barlow, BA Chromy… - Proceedings of the …, 1998 - National Acad Sciences
Aβ1–42 is a self-associating peptide whose neurotoxic derivatives are thought to play a role
in Alzheimer's pathogenesis. Neurotoxicity of amyloid β protein (Aβ) has been attributed to …

[HTML][HTML] ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins

R Sarroukh, E Goormaghtigh, JM Ruysschaert… - … et Biophysica Acta (BBA …, 2013 - Elsevier
Amyloid refers to insoluble protein aggregates that are responsible for amyloid diseases but
are also implicated in important physiological functions (functional amyloids). The …

Protein aggregation: pathways, induction factors and analysis

HC Mahler, W Friess, U Grauschopf, S Kiese - Journal of pharmaceutical …, 2009 - Elsevier
Control and analysis of protein aggregation is an increasing challenge to pharmaceutical
research and development. Due to the nature of protein interactions, protein aggregation …

Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid …

JD Harper, PT Lansbury Jr - Annual review of biochemistry, 1997 - annualreviews.org
Ordered protein aggregation in the brain is a hallmark of Alzheimer's disease and scrapie.
The disease-specific amyloid fibrils comprise primarily a single protein, amyloid β, in …

[HTML][HTML] Alzheimer's amyloid fibrils: structure and assembly

LC Serpell - Biochimica et Biophysica Acta (BBA)-Molecular Basis …, 2000 - Elsevier
Structural studies of Alzheimer's amyloid fibrils have revealed information about the structure
at different levels. The amyloid-β peptide has been examined in various solvents and …

In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis

WB Stine, KN Dahlgren, GA Krafft, MJ LaDu - Journal of Biological …, 2003 - ASBMB
Extensive research causally links amyloid-β peptide (Aβ) to Alzheimer's disease, although
the pathologically relevant Aβ conformation remains unclear. Aβ spontaneously aggregates …