The circularization of amyloid fibrils formed by apolipoprotein C-II.

Abstract

Amyloid fibrils have historically been characterized by diagnostic dye-binding assays, their fibrillar morphology, and a "cross-beta" x-ray diffraction pattern. Whereas the latter demonstrates that amyloid fibrils have a common beta-sheet core structure, they display a substantial degree of morphological variation. One striking example is the remarkable… (More)

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@article{Hatters2003TheCO, title={The circularization of amyloid fibrils formed by apolipoprotein C-II.}, author={Danny M Hatters and Christopher A MacRaild and R. W. Daniels and Walraj S. Gosal and N. H. Thomson and Jonathan A. Jones and Jason J Davis and Cait E. MacPhee and Christopher M. Dobson and Geoffrey J. Howlett}, journal={Biophysical journal}, year={2003}, volume={85 6}, pages={3979-90} }