Amyloid formation as a protein phase transition

TCT Michaels, D Qian, A Šarić, M Vendruscolo… - Nature Reviews …, 2023 - nature.com
The formation of amyloid fibrils is a general class of protein self-assembly behaviour, which
is associated with both functional biology and the development of a number of disorders …

Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils

M Muschol, W Hoyer - Frontiers in molecular biosciences, 2023 - frontiersin.org
Amyloid Diseases involve the growth of disease specific proteins into amyloid fibrils and
their deposition in protein plaques. Amyloid fibril formation is typically preceded by …

Pathways of amyloid-β aggregation depend on oligomer shape

B Barz, Q Liao, B Strodel - Journal of the American Chemical …, 2018 - ACS Publications
One of the main research topics related to Alzheimer's disease is the aggregation of the
amyloid-β peptide, which was shown to follow different pathways for the two major alloforms …

[HTML][HTML] Amyloid β interaction with model cell membranes–What are the toxicity-defining properties of amyloid β?

D Mrdenovic, IS Pieta, R Nowakowski, W Kutner… - International Journal of …, 2022 - Elsevier
Disruption of the neuronal membrane by toxic amyloid β oligomers is hypothesized to be the
major event associated with Alzheimer's disease's neurotoxicity. Misfolding of amyloid β is …

Fundamentals and exploration of aggregation-induced emission molecules for amyloid protein aggregation

Y Tang, D Zhang, Y Zhang, Y Liu, L Cai… - Journal of Materials …, 2022 - pubs.rsc.org
The past decade has witnessed the growing interest and advances in aggregation-induced
emission (AIE) molecules as driven by their unique fluorescence/optical properties in …

Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy

PCA van der Wel - Solid state nuclear magnetic resonance, 2017 - Elsevier
The aggregation of proteins and peptides into a variety of insoluble, and often non-native,
aggregated states plays a central role in many devastating diseases. Analogous processes …

Lipidic folding pathway of α-Synuclein via a toxic oligomer

V Sant, D Matthes, H Mazal, L Antonschmidt… - Nature …, 2025 - nature.com
Aggregation intermediates play a pivotal role in the assembly of amyloid fibrils, which are
central to the pathogenesis of neurodegenerative diseases. The structures of filamentous …

Amyloid β-peptides 1–40 and 1–42 form oligomers with mixed β-sheets

M Baldassarre, CM Baronio, LA Morozova-Roche… - Chemical …, 2017 - pubs.rsc.org
Two main amyloid-β peptides of different length (Aβ40 and Aβ42) are involved in
Alzheimer's disease. Their relative abundance is decisive for the severity of the disease and …

Structure and physicochemical properties of the Aβ42 tetramer: multiscale molecular dynamics simulations

HL Nguyen, P Krupa, NM Hai, HQ Linh… - The Journal of Physical …, 2019 - ACS Publications
Despite years of intensive research, little is known about oligomeric structures present
during Alzheimer's disease (AD). Excess of amyloid beta (Aβ) peptides and their …

Measuring Dipolar Order Parameters in Nondeuterated Proteins Using Solid-State NMR at the Magic-Angle-Spinning Frequency of 100 kHz

PP Taware, MG Jain, S Raran-Kurussi… - The Journal of …, 2023 - ACS Publications
Proteins are dynamic molecules, relying on conformational changes to carry out function.
Measurement of these conformational changes can provide insight into how function is …