Aug 2026· Nature Structural & Molecular Biology· Vol 33, pp. 1194 - 1203· 0 citations· 80 references
Medicine
TL;DR
Cryo-electron microscopy structures of amyloid filaments extracted from the postmortem parietal lobes of two individuals representing the only two known Flemish pedigrees worldwide provide insight into the molecular basis of Flemish-type dementia and cerebral hemorrhage.
It is established that low-twist filaments, which include over 75% of disease-associated Lewy aSyn amyloids, share a common structural core with high-twist forms and are the predominant aSyn species in samples that engage in templated infection.
Nicholas L. Yan, Mylan Mayer, Arthur A. Melo et al.· bioRxiv· 0 citations
ATTR amyloidosis is caused by transthyretin (TTR) amyloid deposition, yet the sequence-encoded events linking TTR misfolding to fibril nucleation and structural polymorphism remain incompletely defined. Here, we exploit the modular organization of patient-derived TTR fibrils to investigate two components of the patholo...
Laxmikant Gadhe, B. Nguyen, María del Carmen Fernández-Ramírez et al.· bioRxiv· 0 citations
Transthyretin amyloidosis (ATTR) is caused by the deposition of transthyretin (TTR) aggregates. While unstable TTR monomers, which are dissociated from the native tetramer, are known to be the primary amyloidogenic precursors of ATTR, the pathological role of other intermediates, such as dimers and oligomers, remains u...
Jinbeom Si, H. Bak, Hye-Yeon Kim et al.· Biochemical and Biophysical...· 0 citations
It is demonstrated that kinase-specific phosphorylation outside the amyloid core can be sufficient to bias tau toward a defined fibril structure, establishing a direct mechanistic link between kinase specificity, post-translational modification, and tau strain formation.
The potential of the β-hairpin structure, whether as a segment within the Kunitz-type proteins or isolated as a cyclic peptide, to interact with Aβ42, thereby reducing Aβ42 aggregation and hence its neurotoxicity is revealed.
Maya Rabinovich, Shiran Lacham-Hartman, N. Papo· New Biotechnology· 0 citations
Non-fibrillar oligomeric forms of amyloid β (Aβ) mediate toxicity in Alzheimer’s disease (AD) with Aβ accumulation preceding tau aggregation and synaptic damage. Aβ oligomerization is thought to initiate from the smallest stable unit, the dimer, yet structural details of this species remain unclear due to its transient...
V. Streltsov, Yumi Irie, Y. Hanaki et al.· npj Dementia· 0 citations
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