Download scientific diagram | Aggregated Q51 exhibits lamination sheets and predominantly lumpy, 174 slab-shaped filaments. (a) 175 Representative sections of 176 annotated Q51 filamentous 177 aggregates from cryoET 178 tomograms showing their 179 most common 180 branching/crossover angle 181 (~60°), often in an asterisk-182 like pattern, and (b) thicker 183 regions (right) akin to 184 lamination, onside thinner 185 ones (left). (c) Subtomogram 186 average of a subpopulation of 187 filament segments exhibiting a 188 lumpy 7x15 nm slab-shaped 189 morphology. 190 from publication: Topological Insights into Mutant Huntingtin Exon 1 and PolyQ Aggregates by Cryo-Electron Tomography | Huntington disease (HD) is a neurodegenerative trinucleotide repeat disorder caused by an expanded poly-glutamine (polyQ) tract in the mutant huntingtin (mHTT) protein. The formation and topology of filamentous mHTT inclusions in the brain (hallmarks of HD implicated in | Exons, Aggregation and Topology | ResearchGate, the professional network for scientists.
Quasi-Isotropic Laminate - an overview
Quasi-Isotropic Laminate - an overview
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Lumpy Q51 filaments exhibit a large range of widths. (a) Schematic
PDF) Topological Insights into Mutant Huntingtin Exon 1 and PolyQ Aggregates by Cryo-Electron Tomography
Quasi-Isotropic Laminate - an overview
PDF) Topological Insights into Mutant Huntingtin Exon 1 and PolyQ Aggregates by Cryo-Electron Tomography
PDF) Cryo-electron tomography provides topological insights into mutant huntingtin exon 1 and polyQ aggregates
PDF) Topological Insights into Mutant Huntingtin Exon 1 and PolyQ Aggregates by Cryo-Electron Tomography
CCT5 complexes can encapsulate mHTTQ46-Ex1 oligomers. A and B, the
Aggregated Q51 exhibits lamination sheets and predominantly lumpy
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