| http://purl.uniprot.org/citations/20133843 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20133843 | http://www.w3.org/2000/01/rdf-schema#comment | "Apolipoprotein A-I (apoA-I) is the major protein component of HDL, where it plays an important role in cholesterol transport. The deposition of apoA-I derived amyloid is associated with various hereditary systemic amyloidoses and atherosclerosis; however, very little is known about the mechanism of apoA-I amyloid formation. Methionine residues in apoA-I are oxidized via several mechanisms in vivo to form methionine sulfoxide (MetO), and significant levels of methionine oxidized apoA-I (MetO-apoA-I) are present in normal human serum. We investigated the effect of methionine oxidation on the structure, stability, and aggregation of full-length, lipid-free apoA-I. Circular dichrosim spectroscopy showed that oxidation of all three methionine residues in apoA-I caused partial unfolding of the protein and decreased its thermal stability, reducing the melting temperature (T(m)) from 58.7 degrees C for native apoA-I to 48.2 degrees C for MetO-apoA-I. Analytical ultracentrifugation revealed that methionine oxidation inhibited the native self association of apoA-I to form dimers and tetramers. Incubation of MetO-apoA-I for extended periods resulted in aggregation of the protein, and these aggregates bound Thioflavin T and Congo Red. Inspection of the aggregates by electron microscopy revealed fibrillar structures with a ribbon-like morphology, widths of approximately 11 nm, and lengths of up to several microns. X-ray fibre diffraction studies of the fibrils revealed a diffraction pattern with orthogonal peaks at spacings of 4.64 A and 9.92 A, indicating a cross-beta amyloid structure. This systematic study of fibril formation by full-length apoA-I represents the first demonstration that methionine oxidation can induce amyloid fibril formation."xsd:string |
| http://purl.uniprot.org/citations/20133843 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0910136107"xsd:string |
| http://purl.uniprot.org/citations/20133843 | http://purl.uniprot.org/core/author | "Howlett G.J."xsd:string |
| http://purl.uniprot.org/citations/20133843 | http://purl.uniprot.org/core/author | "Griffin M.D."xsd:string |
| http://purl.uniprot.org/citations/20133843 | http://purl.uniprot.org/core/author | "Binger K.J."xsd:string |
| http://purl.uniprot.org/citations/20133843 | http://purl.uniprot.org/core/author | "Wong Y.Q."xsd:string |
| http://purl.uniprot.org/citations/20133843 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20133843 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
| http://purl.uniprot.org/citations/20133843 | http://purl.uniprot.org/core/pages | "1977-1982"xsd:string |
| http://purl.uniprot.org/citations/20133843 | http://purl.uniprot.org/core/title | "Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I."xsd:string |
| http://purl.uniprot.org/citations/20133843 | http://purl.uniprot.org/core/volume | "107"xsd:string |
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