Amyloid fibril structure from the vascular variant of systemic AA amyloidosis This study reports the cryo-EM structures of AA amyloid fibrils from two patients with vascular AA amyloidosis. The findings imply that different disease variants in systemic amyloidosis are associated with different fibril stru...
Guo, J. T. & Xu, Y. (2008). Towards modeling of amyloid fibril structures. Front. Biosci., 13:4039-4050. URL https://www.ncbi.nlm.nih.gov/pubmed/18508498.Towards modeling of amyloid fibril structures. Guo J T,Xu Y. Frontiers in Bioscience . 2008...
Structure determination by cryo-EM Fibril formation by the full-length PI3K-SH3 domain under acidic solution conditions30led to long, straight fibrils of which the main population could be structurally determined by cryo-EM (Fig.1). High overall homogeneity of the preparation has been shown by ...
Pathogenesis, including chemical structure, fibrillogenesis and mechanism of disease Pathology Diagnosis, treatment and prognosis across a broad spectrum of clinical specialties impacted by various amyloid diseases and related disorders. The journal publishes research articles, letters to the Editor, review ...
Thus, well-aligned fibrils can sometimes give diffraction patterns that can be used to model (at low resolution) the fibril structure. Despite their highly ordered nature, amyloids are difficult to study by high-resolution structural methods. The one-dimensional nature of the order in the fibrils...
(red spheres) form an array of negative charges running along the length of the fibril. (C) Electrostatic surface of the structure in (B). Charged residues in the core of the fibril structure are labeled. The peptides [E11Q]-Aβ(1–40), [E22Q]-Aβ(1–40), and [H(6,13,14)...
2P022 Amyloid fibril structure proposed from IR-microscope linear dichroism A structural model of amyloid fibril formed by the #21-31 fragment of beta2-microglobulin is proposed from microscope IR measurements on specifically 13C-labeled peptide fibrils and Raman spectra of the dispersed fibril solutio...
In this study, we explored to use side-chain-based infrared (IR) probe to gain detailed structural insights into the amyloid fibril by a 21-residue model amyloidogenic peptide, A(8-28). We first proposed an approach to incorporate thiocyanate (SCN) IR probe in a site-specific manner into...
To investigate the potential effects of the microgravity environment on amyloid fibril structure, Aβ(1–40) fibril morphology between the microgravity-grown fibrils and the ground-grown fibrils was compared using cryo-EM combined with 3D image reconstruction. The cryo-EM data revealed that the Aβ...
Ser42, a phosphorylation site of FUS, is critical in the maintenance of the ordered-coil structure, which explains how phosphorylation controls fibril formation. The RAC2 structure shows a labile fibril spine with a wet interface. These structures illuminate the mechanism of reversible fibril ...