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Journal article

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 ability of human apolipoprotein C-II amyloid fibrils to circularize and form closed rings. Here we explore in detail the structure of apoC-II...

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Publication status:
Published

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Journal:
Biophysical journal
Volume:
85
Issue:
6
Pages:
3979-3990
Publication date:
2003-12-05
DOI:
EISSN:
1542-0086
ISSN:
0006-3495
URN:
uuid:0b80db8b-4b92-4df8-96a3-32f365b926d8
Source identifiers:
18489
Local pid:
pubs:18489

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