| pubmed-article:17433711 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17433711 | lifeskim:mentions | umls-concept:C0033774 | lld:lifeskim |
| pubmed-article:17433711 | lifeskim:mentions | umls-concept:C0007589 | lld:lifeskim |
| pubmed-article:17433711 | lifeskim:mentions | umls-concept:C1155065 | lld:lifeskim |
| pubmed-article:17433711 | lifeskim:mentions | umls-concept:C0077678 | lld:lifeskim |
| pubmed-article:17433711 | lifeskim:mentions | umls-concept:C1704410 | lld:lifeskim |
| pubmed-article:17433711 | lifeskim:mentions | umls-concept:C1511938 | lld:lifeskim |
| pubmed-article:17433711 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:17433711 | pubmed:dateCreated | 2007-6-1 | lld:pubmed |
| pubmed-article:17433711 | pubmed:abstractText | Tagging a small molecule ubiquitin to a protein substrate, or protein ubiquitination, plays an important role in the immune responses. This process is catalyzed by a cascade of enzymatic reactions, with the E3 ubiquitin ligases being the critical enzymes that determine the specificity of substrate recognition. The E3 ligase Itch was identified from a mutant mouse which displays skin scratching and abnormal immune disorders. In the past few years, much progress has been made in our understanding of Itch-promoted protein ubiquitination, modulation of its ligase activity by upstream kinases, and the kinase-ligase interaction in T cell differentiation and tolerance induction. | lld:pubmed |
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| pubmed-article:17433711 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17433711 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17433711 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17433711 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17433711 | pubmed:month | Jun | lld:pubmed |
