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Amyloid as a natural product

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-...

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Detalles Bibliográficos
Autores principales: Kelly, Jeffery W., Balch, William E.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2003
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172945/
https://www.ncbi.nlm.nih.gov/pubmed/12743097
http://dx.doi.org/10.1083/jcb.200304074
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author Kelly, Jeffery W.
Balch, William E.
author_facet Kelly, Jeffery W.
Balch, William E.
author_sort Kelly, Jeffery W.
collection PubMed
description 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.
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spelling pubmed-21729452008-05-01 Amyloid as a natural product Kelly, Jeffery W. Balch, William E. J Cell Biol Comment 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. The Rockefeller University Press 2003-05-12 /pmc/articles/PMC2172945/ /pubmed/12743097 http://dx.doi.org/10.1083/jcb.200304074 Text en Copyright © 2003, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Comment
Kelly, Jeffery W.
Balch, William E.
Amyloid as a natural product
title Amyloid as a natural product
title_full Amyloid as a natural product
title_fullStr Amyloid as a natural product
title_full_unstemmed Amyloid as a natural product
title_short Amyloid as a natural product
title_sort amyloid as a natural product
topic Comment
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172945/
https://www.ncbi.nlm.nih.gov/pubmed/12743097
http://dx.doi.org/10.1083/jcb.200304074
work_keys_str_mv AT kellyjefferyw amyloidasanaturalproduct
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