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dc.contributor.authorLONG, AIDEENen
dc.contributor.authorKELLEHER, DERMOTen
dc.contributor.authorDEMPSEY, EUGENEen
dc.contributor.authorVOLKOV, YURIen
dc.contributor.authorFREELEY, MICHAELen
dc.contributor.authorVERMA, NAVINen
dc.date.accessioned2011-06-27T14:40:54Z
dc.date.available2011-06-27T14:40:54Z
dc.date.issued2011en
dc.date.submitted2011en
dc.identifier.citationVerma NK, Dempsey E, Freeley M, Botting CH, Long A, Kelleher D, Volkov Y, Analysis of dynamic tyrosine phosphoproteome in LFA-1 triggered migrating T-cells., Journal of Cellular Physiology, 226, 6, 2011, 1489 1498en
dc.identifier.issn0021-9541en
dc.identifier.otherYen
dc.identifier.urihttp://hdl.handle.net/2262/57288
dc.descriptionPUBLISHEDen
dc.description.abstractThe ordered, directional migration of T-lymphocytes is a key process during immune surveillance and response. This requires cell adhesion to the high endothelial venules or to the extracellular matrix by a series of surface receptor/ligand interactions involving adhesion molecules of the integrin family including lymphocyte function associated molecule-1 (LFA-1) and intercellular adhesion molecules (ICAMs). Reversible protein phosphorylation is emerging as a key player in the regulation of biological functions with tyrosine phosphorylation playing a crucial role in signal transduction. Thus, the study of this type of post-translational modification at the proteomic level has great biological significance. In this work, phospho-enriched cell lysates from LFA-1-triggered migrating human T-cells were subjected to immunoaffinity purification of tyrosine phosphorylated proteins, mass spectrometric, and bioinformatic analysis. In addition to the identification of several well-documented proteins, the analysis suggested involvement of a number of new and novel proteins in LFA-1 induced T-cell migration. This dataset expands the list of the signaling components of the LFA-1 induced phosphotyrosine protein complexes in migrating T-cells that will be extremely useful in the study of their specific roles within LFA-1 associated signaling pathways. Identification of proteins previously not reported in the context of LFA-1 stimulated signal transduction might provide new insights into understanding the LFA-1 signaling networks and aid in the search for new potential therapeutic targets.en
dc.format.extent1489-1498en
dc.language.isoenen
dc.relation.ispartofseriesJournal of Cellular Physiologyen
dc.relation.ispartofseries226en
dc.relation.ispartofseries6en
dc.rightsYen
dc.subjectImmunologyen
dc.subjectT-lymphocytesen
dc.titleAnalysis of dynamic tyrosine phosphoproteome in LFA-1 triggered migrating T-cells.en
dc.typeJournal Articleen
dc.contributor.sponsorHigher Education Authority (HEA)en
dc.contributor.sponsorHealth Research Board (HRB)en
dc.type.supercollectionscholarly_publicationsen
dc.type.supercollectionrefereed_publicationsen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/longaien
dc.identifier.peoplefinderurlhttp://people.tcd.ie/freeleymen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/dempseeuen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/yvolkoven
dc.identifier.peoplefinderurlhttp://people.tcd.ie/kellehdpen
dc.identifier.rssinternalid69553en
dc.identifier.doihttp://dx.doi.org/10.1002/jcp.22478en
dc.subject.TCDThemeImmunology, Inflammation & Infectionen
dc.subject.TCDThemeInternational Integrationen
dc.identifier.rssurihttp://dx.doi.org/10.1002/jcp.22478en


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