| pubmed-article:16155201 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16155201 | lifeskim:mentions | umls-concept:C0029235 | lld:lifeskim |
| pubmed-article:16155201 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:16155201 | pubmed:dateCreated | 2005-9-30 | lld:pubmed |
| pubmed-article:16155201 | pubmed:abstractText | We introduce a novel approach to estimate differences in the beta-aggregation potential of eukaryotic proteomes. The approach is based on a statistical analysis of the beta-aggregation propensity of polypeptide segments, which is calculated by an equation derived from first principles using the physicochemical properties of the natural amino acids. Our analysis reveals a significant decreasing trend of the overall beta-aggregation tendency with increasing organism complexity and longevity. A comparison with randomized proteomes shows that natural proteomes have a higher degree of polarization in both low and high beta-aggregation prone sequences. The former originates from the requirement of intrinsically disordered proteins, whereas the latter originates from the necessity of proteins with a stable folded structure. | lld:pubmed |
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| pubmed-article:16155201 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16155201 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16155201 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16155201 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16155201 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16155201 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:16155201 | pubmed:author | pubmed-author:CaflischAmede... | lld:pubmed |
| pubmed-article:16155201 | pubmed:author | pubmed-author:CavalliAndrea... | lld:pubmed |
| pubmed-article:16155201 | pubmed:author | pubmed-author:TartagliaGian... | lld:pubmed |
| pubmed-article:16155201 | pubmed:author | pubmed-author:PellarinRicca... | lld:pubmed |
| pubmed-article:16155201 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16155201 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:16155201 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16155201 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16155201 | pubmed:pagination | 2735-40 | lld:pubmed |
| pubmed-article:16155201 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:16155201 | pubmed:meshHeading | pubmed-meshheading:16155201... | lld:pubmed |
| pubmed-article:16155201 | pubmed:meshHeading | pubmed-meshheading:16155201... | lld:pubmed |
| pubmed-article:16155201 | pubmed:meshHeading | pubmed-meshheading:16155201... | lld:pubmed |
| pubmed-article:16155201 | pubmed:meshHeading | pubmed-meshheading:16155201... | lld:pubmed |
| pubmed-article:16155201 | pubmed:meshHeading | pubmed-meshheading:16155201... | lld:pubmed |
| pubmed-article:16155201 | pubmed:meshHeading | pubmed-meshheading:16155201... | lld:pubmed |
| pubmed-article:16155201 | pubmed:meshHeading | pubmed-meshheading:16155201... | lld:pubmed |
| pubmed-article:16155201 | pubmed:meshHeading | pubmed-meshheading:16155201... | lld:pubmed |
| pubmed-article:16155201 | pubmed:meshHeading | pubmed-meshheading:16155201... | lld:pubmed |
| pubmed-article:16155201 | pubmed:meshHeading | pubmed-meshheading:16155201... | lld:pubmed |
| pubmed-article:16155201 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16155201 | pubmed:articleTitle | Organism complexity anti-correlates with proteomic beta-aggregation propensity. | lld:pubmed |
| pubmed-article:16155201 | pubmed:affiliation | Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland. gian@bioc.unizh.ch | lld:pubmed |
| pubmed-article:16155201 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16155201 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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