pubmed-article:17488106 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17488106 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:17488106 | lifeskim:mentions | umls-concept:C0086168 | lld:lifeskim |
pubmed-article:17488106 | lifeskim:mentions | umls-concept:C0037813 | lld:lifeskim |
pubmed-article:17488106 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
pubmed-article:17488106 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:17488106 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
pubmed-article:17488106 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:17488106 | pubmed:dateCreated | 2007-6-1 | lld:pubmed |
pubmed-article:17488106 | pubmed:abstractText | Nonenzymatic glycation of peptides and proteins by d-glucose has important implications in the pathogenesis of diabetes mellitus, particularly in the development of diabetic complications. However, no effective high-throughput methods exist for identifying proteins containing this low-abundance post-translational modification in bottom-up proteomic studies. In this report, phenylboronate affinity chromatography was used in a two-step enrichment scheme to selectively isolate first glycated proteins and then glycated, tryptic peptides from human serum glycated in vitro. Enriched peptides were subsequently analyzed by alternating electron-transfer dissociation (ETD) and collision induced dissociation (CID) tandem mass spectrometry. ETD fragmentation mode permitted identification of a significantly higher number of glycated peptides (87.6% of all identified peptides) versus CID mode (17.0% of all identified peptides), when utilizing enrichment on first the protein and then the peptide level. This study illustrates that phenylboronate affinity chromatography coupled with LC-MS/MS and using ETD as the fragmentation mode is an efficient approach for analysis of glycated proteins and may have broad application in studies of diabetes mellitus. | lld:pubmed |
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pubmed-article:17488106 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17488106 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17488106 | pubmed:language | eng | lld:pubmed |
pubmed-article:17488106 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17488106 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17488106 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17488106 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17488106 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17488106 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17488106 | pubmed:month | Jun | lld:pubmed |
pubmed-article:17488106 | pubmed:issn | 1535-3893 | lld:pubmed |
pubmed-article:17488106 | pubmed:author | pubmed-author:MetzThomas... | lld:pubmed |
pubmed-article:17488106 | pubmed:author | pubmed-author:BaynesJohn... | lld:pubmed |
pubmed-article:17488106 | pubmed:author | pubmed-author:TangNingN | lld:pubmed |
pubmed-article:17488106 | pubmed:author | pubmed-author:SmithRichard... | lld:pubmed |
pubmed-article:17488106 | pubmed:author | pubmed-author:AmesJennifer... | lld:pubmed |
pubmed-article:17488106 | pubmed:author | pubmed-author:ZhangQibinQ | lld:pubmed |
pubmed-article:17488106 | pubmed:author | pubmed-author:BrockJonathan... | lld:pubmed |
pubmed-article:17488106 | pubmed:author | pubmed-author:MottazHeather... | lld:pubmed |
pubmed-article:17488106 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17488106 | pubmed:volume | 6 | lld:pubmed |
pubmed-article:17488106 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17488106 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17488106 | pubmed:pagination | 2323-30 | lld:pubmed |
pubmed-article:17488106 | pubmed:dateRevised | 2011-1-25 | lld:pubmed |
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pubmed-article:17488106 | pubmed:meshHeading | pubmed-meshheading:17488106... | lld:pubmed |
pubmed-article:17488106 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17488106 | pubmed:articleTitle | Enrichment and analysis of nonenzymatically glycated peptides: boronate affinity chromatography coupled with electron-transfer dissociation mass spectrometry. | lld:pubmed |
pubmed-article:17488106 | pubmed:affiliation | Biological Sciences Division and Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352, USA. | lld:pubmed |
pubmed-article:17488106 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17488106 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:17488106 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:17488106 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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