| pubmed-article:15282562 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15282562 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:15282562 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:15282562 | pubmed:dateCreated | 2004-7-29 | lld:pubmed |
| pubmed-article:15282562 | pubmed:abstractText | Protein kinase C molecules regulate both positive and negative signal transduction pathways essential for the initiation and homeostasis of immune responses. There are multiple isoforms of protein kinase C that are activated differently by calcium and diacylglycerol, and these are activated mainly by antigen receptors in T cells, B cells and mast cells. Additionally, mammals express several other diacylglycerol binding proteins that are linked to a network of key signal transduction pathways that control lymphocyte biology. Diacylglycerol and protein kinase C regulate a broad range of gene transcription programs but also modulate integrins, chemokine responses and antigen receptors, thereby regulating lymphocyte adhesion, migration, differentiation and proliferation. | lld:pubmed |
| pubmed-article:15282562 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15282562 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15282562 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15282562 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15282562 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15282562 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15282562 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15282562 | pubmed:issn | 1529-2908 | lld:pubmed |
| pubmed-article:15282562 | pubmed:author | pubmed-author:CantrellDoree... | lld:pubmed |
| pubmed-article:15282562 | pubmed:author | pubmed-author:SpitalerMarti... | lld:pubmed |
| pubmed-article:15282562 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15282562 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:15282562 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15282562 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15282562 | pubmed:pagination | 785-90 | lld:pubmed |
| pubmed-article:15282562 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:15282562 | pubmed:meshHeading | pubmed-meshheading:15282562... | lld:pubmed |
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| pubmed-article:15282562 | pubmed:meshHeading | pubmed-meshheading:15282562... | lld:pubmed |
| pubmed-article:15282562 | pubmed:meshHeading | pubmed-meshheading:15282562... | lld:pubmed |
| pubmed-article:15282562 | pubmed:meshHeading | pubmed-meshheading:15282562... | lld:pubmed |
| pubmed-article:15282562 | pubmed:meshHeading | pubmed-meshheading:15282562... | lld:pubmed |
| pubmed-article:15282562 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15282562 | pubmed:articleTitle | Protein kinase C and beyond. | lld:pubmed |
| pubmed-article:15282562 | pubmed:affiliation | School of Life Sciences, Division of Cell Biology & Immunology, University of Dundee, MSI/WTB Complex, Dow Street, Dundee DD1 5EH, UK. | lld:pubmed |
| pubmed-article:15282562 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15282562 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:15282562 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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