Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1887404#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B410409.
- aggregation creator B410410.
- aggregation creator B410411.
- aggregation creator person.
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- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1887404.bibtex.
- aggregation hasFormat 1887404.csv.
- aggregation hasFormat 1887404.dc.
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- aggregation hasFormat 1887404.doc.
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- aggregation isPartOf urn:issn:1535-9476.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Redox proteomics of protein-bound methionine oxidation".
- aggregation abstract "We here present a new method to measure the degree of protein-bound methionine sulfoxide formation at a proteome-wide scale. In human Jurkat cells that were stressed with hydrogen peroxide, over 2000 oxidation-sensitive methionines in more than 1600 different proteins were mapped and their extent of oxidation was quantified. Meta-analysis of the sequences surrounding the oxidized methionine residues revealed a high preference for neighboring polar residues. Using synthetic methionine sulfoxide containing peptides designed according to the observed sequence preferences in the oxidized Jurkat proteome, we discovered that the substrate specificity of the cellular methionine sulfoxide reductases is a major determinant for the steady-state of methionine oxidation. This was supported by a structural modeling of the MsrA catalytic center. Finally, we applied our method onto a serum proteome from a mouse sepsis model and identified 35 in vivo methionine oxidation events in 27 different proteins.".
- aggregation authorList BK727112.
- aggregation issue "5".
- aggregation volume "10".
- aggregation aggregates 3111893.
- aggregation isDescribedBy 1887404.
- aggregation similarTo mcp.M110.006866.
- aggregation similarTo LU-1887404.