| pubmed-article:17370265 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17370265 | lifeskim:mentions | umls-concept:C0038137 | lld:lifeskim |
| pubmed-article:17370265 | lifeskim:mentions | umls-concept:C0041538 | lld:lifeskim |
| pubmed-article:17370265 | lifeskim:mentions | umls-concept:C1956096 | lld:lifeskim |
| pubmed-article:17370265 | lifeskim:mentions | umls-concept:C0184511 | lld:lifeskim |
| pubmed-article:17370265 | lifeskim:mentions | umls-concept:C0679199 | lld:lifeskim |
| pubmed-article:17370265 | lifeskim:mentions | umls-concept:C0037813 | lld:lifeskim |
| pubmed-article:17370265 | lifeskim:mentions | umls-concept:C2348822 | lld:lifeskim |
| pubmed-article:17370265 | lifeskim:mentions | umls-concept:C0175675 | lld:lifeskim |
| pubmed-article:17370265 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:17370265 | pubmed:dateCreated | 2007-6-4 | lld:pubmed |
| pubmed-article:17370265 | pubmed:abstractText | Ubiquitination plays an essential role in maintaining cellular homeostasis by regulating a multitude of essential processes. The ability to identify ubiquitinated proteins by MS currently relies on a strategy in which ubiquitinated peptides are identified by a 114.1 Da diglycine (GG) tag on lysine residues, which is derived from the C-terminus of ubiquitin, following trypsin digestion. In the following study, we report a more comprehensive approach for mapping ubiquitination sites by trypsin digestion and MS/MS analysis. We demonstrate that ubiquitination sites can be identified by signature peptides containing a GG-tag (114.1 Da) and an LRGG-tag (383.2 Da) on internal lysine residues as well as a GG-tag found on the C-terminus of ubiquitinated peptides. Application of this MS-based approach enabled the identification of 96 ubiquitination sites from proteins purified from human MCF-7 breast cancer cells, representing a 2.4-fold increase in the number of ubiquitination sites that could be identified over standard methods. Our improved MS-based strategy will aid future studies which aim to identify and/or characterize ubiquitinated proteins in human cells. | lld:pubmed |
| pubmed-article:17370265 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17370265 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17370265 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17370265 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17370265 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17370265 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17370265 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:17370265 | pubmed:issn | 1615-9853 | lld:pubmed |
| pubmed-article:17370265 | pubmed:author | pubmed-author:SmithJeffrey... | lld:pubmed |
| pubmed-article:17370265 | pubmed:author | pubmed-author:FigeysDanielD | lld:pubmed |
| pubmed-article:17370265 | pubmed:author | pubmed-author:VasilescuJuli... | lld:pubmed |
| pubmed-article:17370265 | pubmed:author | pubmed-author:LambertJean-P... | lld:pubmed |
| pubmed-article:17370265 | pubmed:author | pubmed-author:DenisNicholas... | lld:pubmed |
| pubmed-article:17370265 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17370265 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:17370265 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17370265 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17370265 | pubmed:pagination | 868-74 | lld:pubmed |
| pubmed-article:17370265 | pubmed:meshHeading | pubmed-meshheading:17370265... | lld:pubmed |
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| pubmed-article:17370265 | pubmed:meshHeading | pubmed-meshheading:17370265... | lld:pubmed |
| pubmed-article:17370265 | pubmed:meshHeading | pubmed-meshheading:17370265... | lld:pubmed |
| pubmed-article:17370265 | pubmed:meshHeading | pubmed-meshheading:17370265... | lld:pubmed |
| pubmed-article:17370265 | pubmed:meshHeading | pubmed-meshheading:17370265... | lld:pubmed |
| pubmed-article:17370265 | pubmed:meshHeading | pubmed-meshheading:17370265... | lld:pubmed |
| pubmed-article:17370265 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17370265 | pubmed:articleTitle | Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry. | lld:pubmed |
| pubmed-article:17370265 | pubmed:affiliation | Ottawa Institute of Systems Biology, University of Ottawa, Ottawa, ON, Canada. | lld:pubmed |
| pubmed-article:17370265 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17370265 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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