pubmed-article:15822919 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15822919 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:15822919 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:15822919 | lifeskim:mentions | umls-concept:C0031684 | lld:lifeskim |
pubmed-article:15822919 | lifeskim:mentions | umls-concept:C1384511 | lld:lifeskim |
pubmed-article:15822919 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
pubmed-article:15822919 | lifeskim:mentions | umls-concept:C0037813 | lld:lifeskim |
pubmed-article:15822919 | lifeskim:mentions | umls-concept:C1283195 | lld:lifeskim |
pubmed-article:15822919 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:15822919 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
pubmed-article:15822919 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:15822919 | pubmed:dateCreated | 2005-4-12 | lld:pubmed |
pubmed-article:15822919 | pubmed:abstractText | A novel chemical-enzymatic approach was developed to facilitate identification of phosphorylation sites in isolated phosphoproteins. ESI-TOF mass spectrometry was used to characterize products from the chemical-enzymatic cleavage of specific phosphorylation sites in bovine alpha-S1 casein and synthetic phosphopeptides containing substitutions at a single phosphorylation site. Further refinements to this approach for identification of protein phosphorylation sites and its utility for the quantification of phosphopeptides by isotope-dilution mass spectrometry are presented. | lld:pubmed |
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pubmed-article:15822919 | pubmed:language | eng | lld:pubmed |
pubmed-article:15822919 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15822919 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:15822919 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15822919 | pubmed:issn | 1535-3893 | lld:pubmed |
pubmed-article:15822919 | pubmed:author | pubmed-author:McCormickDani... | lld:pubmed |
pubmed-article:15822919 | pubmed:author | pubmed-author:MuddimanDavid... | lld:pubmed |
pubmed-article:15822919 | pubmed:author | pubmed-author:HolmesMichael... | lld:pubmed |
pubmed-article:15822919 | pubmed:author | pubmed-author:MaddenBenjami... | lld:pubmed |
pubmed-article:15822919 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15822919 | pubmed:volume | 4 | lld:pubmed |
pubmed-article:15822919 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15822919 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15822919 | pubmed:pagination | 424-34 | lld:pubmed |
pubmed-article:15822919 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:15822919 | pubmed:meshHeading | pubmed-meshheading:15822919... | lld:pubmed |
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pubmed-article:15822919 | pubmed:articleTitle | Mapping sites of protein phosphorylation by mass spectrometry utilizing a chemical-enzymatic approach: characterization of products from alpha-S1 casein phosphopeptides. | lld:pubmed |
pubmed-article:15822919 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Mayo Clinic, Rochester, Minnesota 55905, USA. mccormick.daniel@mayo.edu | lld:pubmed |
pubmed-article:15822919 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15822919 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |