A review of the current state of magnetic force microscopy to unravel the magnetic properties of nanomaterials applied in biological systems and future directions for …

R Winkler, M Ciria, M Ahmad, H Plank, C Marcuello - Nanomaterials, 2023 - mdpi.com
Magnetism plays a pivotal role in many biological systems. However, the intensity of the
magnetic forces exerted between magnetic bodies is usually low, which demands the …

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

DJ Rinauro, F Chiti, M Vendruscolo… - Molecular …, 2024 - Springer
The conversion of native peptides and proteins into amyloid aggregates is a hallmark of over
50 human disorders, including Alzheimer's and Parkinson's diseases. Increasing evidence …

[HTML][HTML] Morphological and Biophysical Study of S100A9 protein fibrils by atomic force microscopy imaging and nanomechanical analysis

AP Carapeto, C Marcuello, PFN Faísca, MS Rodrigues - Biomolecules, 2024 - mdpi.com
Atomic force microscopy (AFM) imaging enables the visualization of protein molecules with
high resolution, providing insights into their shape, size, and surface topography. Here, we …

Inhibition of Tau seeding by targeting Tau nucleation core within neurons with a single domain antibody fragment

C Danis, E Dupré, O Zejneli, R Caillierez, A Arrial… - Molecular Therapy, 2022 - cell.com
Tau proteins aggregate into filaments in brain cells in Alzheimer's disease and related
disorders referred to as tauopathies. Here, we used fragments of camelid heavy-chain-only …

[HTML][HTML] Liquid− liquid phase separation of tau: driving forces, regulation, and biological implications

P Li, J Chen, X Wang, Z Su, M Gao, Y Huang - Neurobiology of Disease, 2023 - Elsevier
The past 15 years have witnessed an explosion in the studies of biomolecular condensates
that are implicated in numerous biological processes and play vital roles in human health …

Tau liquid–liquid phase separation is modulated by the Ca2+‐switched chaperone activity of the S100B protein

GG Moreira, CM Gomes - Journal of Neurochemistry, 2023 - Wiley Online Library
Aggregation of the microtubule‐associated protein tau is implicated in several
neurodegenerative tauopathies including Alzheimer's disease (AD). Recent studies …

S100B chaperone multimers suppress the formation of oligomers during Aβ42 aggregation

AJ Figueira, J Saavedra, I Cardoso… - Frontiers in …, 2023 - frontiersin.org
Extracellular aggregation of the amyloid-β 1–42 (Aβ42) peptide is a major hallmark of
Alzheimer's disease (AD), with recent data suggesting that Aβ intermediate oligomers (AβO) …

Deciphering the structure and formation of amyloids in neurodegenerative diseases with chemical biology tools

I Landrieu, E Dupré, D Sinnaeve, L El Hajjar… - Frontiers in …, 2022 - frontiersin.org
Protein aggregation into highly ordered, regularly repeated cross-β sheet structures called
amyloid fibrils is closely associated to human disorders such as neurodegenerative …

Traumatic brain injury derived pathological tau polymorphs induce the distinct propagation pattern and neuroinflammatory response in wild type mice

N Puangmalai, N Bhatt, A Bittar, C Jerez… - Progress in …, 2024 - Elsevier
The misfolding and aggregation of the tau protein into neurofibrillary tangles constitutes a
central feature of tauopathies. Traumatic brain injury (TBI) has emerged as a potential risk …

[HTML][HTML] Tetramerization of the S100B chaperone spawns a Ca2+ independent regulatory surface that enhances anti-aggregation activity and client specificity

AJ Figueira, GG Moreira, J Saavedra, I Cardoso… - Journal of Molecular …, 2022 - Elsevier
Alzheimer's disease (AD) hallmarks include the aggregation of amyloid-β (Aβ), tau and
neuroinflammation promoted by several alarmins. Among these is S100B, a small astrocytic …