2026· Progress in Molecular Biology and Translational Science· Vol 223, pp.
115-146
· 0 citations
Medicine
TL;DR
The persistent bottleneck of sample preparation is addressed, detailing the physical challenges of fibril clumping and interfacial adsorption, alongside emerging solutions to these problems, and the translational value of high-resolution maps is highlighted, demonstrating how they enable the rational, structure-based design of peptide inhibitors and small molecules capable of disaggregating pathogenic fibrils.
Amyloid fibrils are implicated in a myriad of human diseases. A striking observation is that fibrils extracted from diseased tissues are characterized by a restricted set of folds unique to the specific pathology. In contrast, fibrils grown in vitro exhibit extensive structural diversity, suggesting that specific envir...
Mikołaj I Kuska, Łucja Kozicka, S. Prodhan et al.· bioRxiv· 0 citations
Structural studies of amyloid fibrils extracted from brain tissue have identified disease-specific fibril polymorphs. However, the mechanisms driving distinct polymorphs remain unclear because no method currently links the cellular context, composition and ultrastructure of individual aggregates to their constituent fi...
Lukas van den Heuvel, Daniel A. Stähli, Julika Radecke et al.· bioRxiv· 0 citations
Cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET) are powerful technologies for determining the three-dimensional structures of biological macromolecules. However, particle identification, a crucial step in these workflows, remains challenging due to limited annotated training data, low signal-t...
This study investigates the eukaryotic chaperonin CCT, a ~1 MDa hetero-oligomeric complex essential for the folding of key substrates such as actin, tubulin, and WD40 family members and demonstrates that subunit assignment and atomic modeling are achievable by exploiting subunit-intrinsic structural features alone.
Jorge Gutiérrez-Seijo, Ana Cuervo, Sergio Pipaón et al.· Methods in molecular biology· 0 citations
Neurodegeneration unfolds across scales, from nanometer-scale protein assemblies to millimeter-scale tissue reorganization. This review examines how electron and X-ray methods connect these levels. Single-particle cryo-electron microscopy (cryo-EM) resolves isolated molecular assemblies, cryo-electron tomography places...
Inayathulla Mohammed· Current Opinion in Structura...· 0 citations
Findings provide direct structural evidence for amyloid evolution in vivo and support a chaperone-mediated mechanism of conformer selection within a polymorphic amyloid population.
Ziang Wang, Samantha L. Weetman, Barbara Altenhuber et al.· bioRxiv· 0 citations
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