T lymphocytes mediate cellular and humoral defense against foreign bodies or autoantigens. An understanding of T-cell information processing furthers studies of the immunological response. We describe a large-scale phosphorylation analysis of primary T cells using a multidimensional separation strategy, involving preparative SDS-PAGE for prefractionation, in-gel digestion and sequential phosphopeptide enrichment using IMAC and TiO2. A total of 281 phosphorylation sites (197 of high confidence, Ascore > 15), mapping to 204 human gene sequences, were identified by LC-MS(n) analysis in an LTQ linear ion trap. Subsequently, we created the LymPHOS database (http://lymphos.org), which links mass spectrometric peptide information to phosphorylation sites and phosphoprotein sequences.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
T lymphocytes mediate cellular and humoral defense against foreign bodies or autoantigens. An understanding of T-cell information processing furthers studies of the immunological response. We describe a large-scale phosphorylation analysis of primary T cells using a multidimensional separation strategy, involving preparative SDS-PAGE for prefractionation, in-gel digestion and sequential phosphopeptide enrichment using IMAC and TiO2. A total of 281 phosphorylation sites (197 of high confidence, Ascore > 15), mapping to 204 human gene sequences, were identified by LC-MS(n) analysis in an LTQ linear ion trap. Subsequently, we created the LymPHOS database (http://lymphos.org), which links mass spectrometric peptide information to phosphorylation sites and phosphoprotein sequences.
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| skos:exactMatch | |
| uniprot:name |
J. Proteome Res.
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| uniprot:author |
Abian J.,
Carrascal M.,
Casas V.,
Gay M.,
Ovelleiro D.
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| uniprot:date |
2008
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| uniprot:pages |
5167-5176
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| uniprot:title |
Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.
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| uniprot:volume |
7
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| dc-term:identifier |
doi:10.1021/pr800500r
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