Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

  title={Common core structure of amyloid fibrils by synchrotron X-ray diffraction.},
  author={Margaret Sunde and Louise C. Serpell and Mark Bartlam and Paul E. Fraser and Mark B. Pepys and Colin C. F. Blake},
  journal={Journal of molecular biology},
  volume={273 3},
Tissue deposition of normally soluble proteins as insoluble amyloid fibrils is associated with serious diseases including the systemic amyloidoses, maturity onset diabetes, Alzheimer's disease and transmissible spongiform encephalopathy. Although the precursor proteins in different diseases do not share sequence homology or related native structure, the morphology and properties of all amyloid fibrils are remarkably similar. Using intense synchrotron sources we observed that six different ex… 

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The common architecture of cross-beta amyloid.

Review: structure of amyloid fibril in diseases

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Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid.

The core structure of an Alzheimer's amyloid fibril is revealed by direct visualisation using cryo-electron microscopy to help understand the abnormal assembly and deposition of these fibrils and could lead to the rational design of therapeutic agents for their prevention or disaggregation.

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Solid-state NMR spectroscopy, and more specifically rotational echo double-resonance (REDOR) experiments, are a powerful tool to unambiguously determine the register of constituent b strands within an amyloid fibril.

Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy.

It is concluded that ex vivo amyloid fibrils, although variable, assemble as characteristic structures according to the identity of the precursor protein.

The formation of amyloid fibrils by relaxin

Amyloid is characterised by a typical ‘cross-13’ X-ray diffraction pattern indicative of a stacked 13-sheet structure in which the strands are arranged perpendicular to the fibril axis; by a long, unbranched appearance under electron microscopy; and by staining with the dye Congo Red, which exhibits a green birefringence when viewed under polarised light.

X-ray scattering and diffraction by wet gels of AA amyloid fibrils.

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Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro.

These findings on these homologous synthetic assemblies help to define the specific sequence that is required to form Alzheimer-type amyloid fibrils, thus providing an in vitro model of age-related cerebral amyloidsogenesis.


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The filamentous protein component of amyloid-laden tissue was studied by x-ray diffraction procedures and it is suggested that the axes of the chain segments run transverse to the filament axis.

X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.

The cross-beta conformation of PHF and amyloid fibers that the authors have found from x-ray diffraction is in contrast to the predominant alpha-helical coiled-coil conformed of the neurofilaments with which they share epitopes and from which they have been postulated to derive.

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.

A molecular model of the amyloid fibril.

This newly-described helix reconciles the classical cross-beta structure of amyloid with the twisted beta-sheet that is known to be the most stable form of the structure.

Structural studies on FAP fibrils: removal of contaminants is essential for the interpretation of X-ray data

Amyloid fibrils were isolated from heterozygous Met 30 familial amyloidotic polyneuropathy patients and X-ray diffraction experiments indicate the presence of a lipid structure in all the samples that had not been previously delipidated.