Glucosylceramide associated with Gaucher Disease forms amyloid-like twisted ribbon fibrils that induce α-synuclein Aggregation

A Paul, G Jacoby, D Laor Bar-Yosef, R Beck, E Gazit… - ACS …, 2021 - ACS Publications
A major risk factor for Gaucher's disease is loss of function mutations in the GBA1 gene that
encodes lysosomal β-glucocerebrosidase, resulting in accumulation of glucosylceramide …

[HTML][HTML] Evidence of small fungal cysteine-rich proteins acting as biosurfactants and self-assembling into large fibers

R Pitocchi, I Stanzione, A Illiano, A Amoresano… - International Journal of …, 2023 - mdpi.com
Fungi produce surface-active proteins, among which hydrophobins are the most
characterized and attractive also for their ability to form functional amyloids. Our most recent …

Inhibition of tau amyloid formation and disruption of its preformed fibrils by Naphthoquinone–Dopamine hybrid

A Paul, GKK Viswanathan, A Huber, E Arad… - The FEBS …, 2021 - Wiley Online Library
Misfolding and aggregation of tau protein, into pathological amyloids, are hallmarks of a
group of neurodegenerative diseases collectively termed tauopathies and their modulation …

Self‐Assembly and Neurotoxicity of β‐Amyloid (21–40) Peptide Fragment: The Regulatory Role of GxxxG Motifs

D Sarkar, I Chakraborty, M Condorelli… - …, 2020 - Wiley Online Library
The three GxxxG repeating motifs from the C‐terminal region of β‐amyloid (Aβ) peptide play
a significant role in regulating the aggregation kinetics of the peptide. Mutation of these …

Morphology of a Transmembrane Aβ42 Tetramer via REMD Simulations

ST Ngo, TH Nguyen, VV Vu - Journal of Chemical Information and …, 2023 - ACS Publications
The folding/misfolding of membrane-permiable Amyloid beta (Aβ) peptides is likely
associated with the advancing stage of Alzheimer's disease (AD) by disrupting Ca2+ …

[HTML][HTML] Copper (I) or (II) replacement of the structural zinc ion in the prokaryotic zinc finger Ros does not result in a functional domain

M Dragone, R Grazioso, G D'Abrosca, I Baglivo… - International Journal of …, 2022 - mdpi.com
A strict interplay is known to involve copper and zinc in many cellular processes. For this
reason, the results of copper's interaction with zinc binding proteins are of great interest. For …

[HTML][HTML] Folding mechanism and aggregation propensity of the KH0 domain of FMRP and its R138Q pathological variant

D Santorelli, F Troilo, F Fata, F Angelucci… - International Journal of …, 2022 - mdpi.com
The K-homology (KH) domains are small, structurally conserved domains found in proteins
of different origins characterized by a central conserved βααβ “core” and a GxxG motif in the …

[HTML][HTML] Structural and dynamical determinants of a β-sheet-enriched intermediate involved in amyloid fibrillar assembly of human prion protein

L Russo, G Salzano, A Corvino, E Bistaffa, F Moda… - Chemical …, 2022 - pubs.rsc.org
The conformational conversion of the cellular prion protein (PrPC) into a misfolded,
aggregated and infectious scrapie isoform is associated with prion disease pathology and …

[HTML][HTML] Substitution of the native Zn (II) with Cd (II), Co (II) and Ni (II) changes the downhill unfolding mechanism of Ros87 to a completely different scenario

R Grazioso, S García-Viñuales, L Russo… - International Journal of …, 2020 - mdpi.com
The structural effects of zinc replacement by xenobiotic metal ions have been widely studied
in several eukaryotic and prokaryotic zinc-finger-containing proteins. The prokaryotic zinc …

[HTML][HTML] Different Impacts of MucR Binding to the babR and virB Promoters on Gene Expression in Brucella abortus 2308

G Borriello, V Russo, R Paradiso, MG Riccardi… - Biomolecules, 2020 - mdpi.com
The protein MucR from Brucella abortus has been described as a transcriptional regulator of
many virulence genes. It is a member of the Ros/MucR family comprising proteins that …