| pubmed-article:16797587 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16797587 | lifeskim:mentions | umls-concept:C0002716 | lld:lifeskim |
| pubmed-article:16797587 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:16797587 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:16797587 | lifeskim:mentions | umls-concept:C0332621 | lld:lifeskim |
| pubmed-article:16797587 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16797587 | pubmed:dateCreated | 2006-7-10 | lld:pubmed |
| pubmed-article:16797587 | pubmed:abstractText | Amyloid fibrils are insoluble mainly beta-sheet aggregates of proteins or peptides. The multi-step process of amyloid aggregation is one of the major research topics in structural biology and biophysics because of its relevance in protein misfolding diseases like Alzheimer's, Parkinson's, Creutzfeld-Jacob's, and type II diabetes. Yet, the detailed mechanism of oligomer formation and the influence of protein stability on the aggregation kinetics are still matters of debate. Here a coarse-grained model of an amphipathic polypeptide, characterized by a free energy profile with distinct amyloid-competent (i.e. beta-prone) and amyloid-protected states, is used to investigate the kinetics of aggregation and the pathways of fibril formation. The simulation results suggest that by simply increasing the relative stability of the beta-prone state of the polypeptide, disordered aggregation changes into fibrillogenesis with the presence of oligomeric on-pathway intermediates, and finally without intermediates in the case of a very stable beta-prone state. The minimal-size aggregate able to form a fibril is generated by collisions of oligomers or monomers for polypeptides with unstable or stable beta-prone state, respectively. The simulation results provide a basis for understanding the wide range of amyloid-aggregation mechanisms observed in peptides and proteins. Moreover, they allow us to interpret at a molecular level the much faster kinetics of assembly of a recently discovered functional amyloid with respect to the very slow pathological aggregation. | lld:pubmed |
| pubmed-article:16797587 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16797587 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16797587 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16797587 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16797587 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16797587 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16797587 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16797587 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:16797587 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:16797587 | pubmed:author | pubmed-author:CaflischAmede... | lld:pubmed |
| pubmed-article:16797587 | pubmed:author | pubmed-author:PellarinRicca... | lld:pubmed |
| pubmed-article:16797587 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16797587 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:16797587 | pubmed:volume | 360 | lld:pubmed |
| pubmed-article:16797587 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16797587 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16797587 | pubmed:pagination | 882-92 | lld:pubmed |
| pubmed-article:16797587 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:16797587 | pubmed:meshHeading | pubmed-meshheading:16797587... | lld:pubmed |
| pubmed-article:16797587 | pubmed:meshHeading | pubmed-meshheading:16797587... | lld:pubmed |
| pubmed-article:16797587 | pubmed:meshHeading | pubmed-meshheading:16797587... | lld:pubmed |
| pubmed-article:16797587 | pubmed:meshHeading | pubmed-meshheading:16797587... | lld:pubmed |
| pubmed-article:16797587 | pubmed:meshHeading | pubmed-meshheading:16797587... | lld:pubmed |
| pubmed-article:16797587 | pubmed:meshHeading | pubmed-meshheading:16797587... | lld:pubmed |
| pubmed-article:16797587 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16797587 | pubmed:articleTitle | Interpreting the aggregation kinetics of amyloid peptides. | lld:pubmed |
| pubmed-article:16797587 | pubmed:affiliation | Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland. | lld:pubmed |
| pubmed-article:16797587 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16797587 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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