DOI: 10.1083/jcb.200304074. Amyloid as a natural product

10.1083/jcb.200304074

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

Amyloid fibrils, such as those found in Alzheimer's and the gelsolin amyloid diseases, result from the misassembly of peptides produced by either normal or aberrant intracellular proteolytic processing. A paper in this issue by Marks and colleagues (Berson et al., 2003) demonstrates that intra-melanosome fibrils are formed through normal biological proteolytic processing of an integral membrane protein. The resulting peptide fragment assembles into fibrils promoting the formation of melanin pigment granules. These results, along with the observation that amyloid fibril formation by bacteria is highly orchestrated, suggest that fibril formation is an evolutionary conserved biological pathway used to generate natural product nanostructures.

Bibliography

Kelly, J. W., & Balch, W. E. (2003). Amyloid as a natural product. The Journal of Cell Biology, 161(3), 461â462.

Authors 2

Jeffery W. Kelly (first)
William E. Balch (additional)

References 9 Referenced 94

10.1038/10466 / Nat. Med. (1999)
10.1083/jcb.200302072 / J. Cell Biol (2003)
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Dates

Type	When
Created	22 years, 3 months ago (May 12, 2003, 3:38 p.m.)
Deposited	2 years, 1 month ago (July 22, 2023, 11:41 a.m.)
Indexed	1 year ago (Aug. 12, 2024, 7:18 a.m.)
Issued	22 years, 3 months ago (May 12, 2003)
Published	22 years, 3 months ago (May 12, 2003)
Published Online	22 years, 3 months ago (May 12, 2003)
Published Print	22 years, 3 months ago (May 12, 2003)

Funders 0

None

BibTeX

@article{Kelly_2003, title={Amyloid as a natural product}, volume={161}, ISSN={0021-9525}, url={http://dx.doi.org/10.1083/jcb.200304074}, DOI={10.1083/jcb.200304074}, number={3}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Kelly, Jeffery W. and Balch, William E.}, year={2003}, month=may, pages={461–462} }

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