| pubmed-article:12456886 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12456886 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:12456886 | lifeskim:mentions | umls-concept:C1515568 | lld:lifeskim |
| pubmed-article:12456886 | lifeskim:mentions | umls-concept:C1449651 | lld:lifeskim |
| pubmed-article:12456886 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:12456886 | pubmed:dateCreated | 2002-12-11 | lld:pubmed |
| pubmed-article:12456886 | pubmed:abstractText | Identification of therapeutic strategies to prevent or cure diseases associated with amyloid fibril deposition in tissue (Alzheimer's disease, spongiform encephalopathies, etc.) requires a rational understanding of the driving forces involved in the formation of these organized assemblies rich in beta-sheet structure. To this end, we used a computer-designed algorithm to search for hexapeptide sequences with a high propensity to form homopolymeric beta-sheets. Sequences predicted to be highly favorable on this basis were found experimentally to self-associate efficiently into beta-sheets, whereas point mutations predicted to be unfavorable for this structure inhibited polymerization. However, the property to form polymeric beta-sheets is not a sufficient requirement for fibril formation because, under the conditions used here, preformed beta-sheets from these peptides with charged residues form well defined fibrils only if the total net charge of the molecule is +/-1. This finding illustrates the delicate balance of interactions involved in the formation of fibrils relative to more disordered aggregates. The present results, in conjunction with x-ray fiber diffraction, electron microscopy, and Fourier transform infrared measurements, have allowed us to propose a detailed structural model of the fibrils. | lld:pubmed |
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| pubmed-article:12456886 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12456886 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12456886 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12456886 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12456886 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:12456886 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:12456886 | pubmed:author | pubmed-author:LacroixEmmanu... | lld:pubmed |
| pubmed-article:12456886 | pubmed:author | pubmed-author:SerranoLuisL | lld:pubmed |
| pubmed-article:12456886 | pubmed:author | pubmed-author:DobsonChristo... | lld:pubmed |
| pubmed-article:12456886 | pubmed:author | pubmed-author:ZurdoJesúsJ | lld:pubmed |
| pubmed-article:12456886 | pubmed:author | pubmed-author:HoengerAndrea... | lld:pubmed |
| pubmed-article:12456886 | pubmed:author | pubmed-author:GoldieKenneth... | lld:pubmed |
| pubmed-article:12456886 | pubmed:author | pubmed-author:López De La... | lld:pubmed |
| pubmed-article:12456886 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12456886 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:12456886 | pubmed:volume | 99 | lld:pubmed |
| pubmed-article:12456886 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12456886 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12456886 | pubmed:pagination | 16052-7 | lld:pubmed |
| pubmed-article:12456886 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:12456886 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12456886 | pubmed:articleTitle | De novo designed peptide-based amyloid fibrils. | lld:pubmed |
| pubmed-article:12456886 | pubmed:affiliation | European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany Europe. delapaz@embl-heidelberg.de | lld:pubmed |
| pubmed-article:12456886 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12456886 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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