pubmed-article:8493533 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8493533 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:8493533 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:8493533 | lifeskim:mentions | umls-concept:C1519877 | lld:lifeskim |
pubmed-article:8493533 | lifeskim:mentions | umls-concept:C1567709 | lld:lifeskim |
pubmed-article:8493533 | lifeskim:mentions | umls-concept:C2698932 | lld:lifeskim |
pubmed-article:8493533 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:8493533 | pubmed:issue | 5110 | lld:pubmed |
pubmed-article:8493533 | pubmed:dateCreated | 1993-6-15 | lld:pubmed |
pubmed-article:8493533 | pubmed:abstractText | Antigen receptor genes are assembled by site-specific DNA rearrangement. The recombination activator genes RAG-1 and RAG-2 are essential for this process, termed V(D)J rearrangement. The activity and stability of the RAG-2 protein have now been shown to be regulated by phosphorylation. In fibroblasts RAG-2 was phosphorylated predominantly at two serine residues, one of which affected RAG-2 activity in vivo. The threonine at residue 490 was phosphorylated by p34cdc2 kinase in vitro; phosphorylation at this site in vivo was associated with rapid degradation of RAG-2. Instability was transferred to chimeric proteins by a 90-residue portion of RAG-2. Mutation of the p34cdc2 phosphorylation site of the tumor suppressor protein p53 conferred a similar phenotype, suggesting that this association between phosphorylation and degradation is a general mechanism. | lld:pubmed |
pubmed-article:8493533 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8493533 | pubmed:language | eng | lld:pubmed |
pubmed-article:8493533 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8493533 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8493533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8493533 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8493533 | pubmed:month | May | lld:pubmed |
pubmed-article:8493533 | pubmed:issn | 0036-8075 | lld:pubmed |
pubmed-article:8493533 | pubmed:author | pubmed-author:DesiderioSS | lld:pubmed |
pubmed-article:8493533 | pubmed:author | pubmed-author:TURM MMM | lld:pubmed |
pubmed-article:8493533 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8493533 | pubmed:day | 14 | lld:pubmed |
pubmed-article:8493533 | pubmed:volume | 260 | lld:pubmed |
pubmed-article:8493533 | pubmed:geneSymbol | RAG-2 | lld:pubmed |
pubmed-article:8493533 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8493533 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8493533 | pubmed:pagination | 953-9 | lld:pubmed |
pubmed-article:8493533 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:8493533 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8493533 | pubmed:articleTitle | Regulation of V(D)J recombination activator protein RAG-2 by phosphorylation. | lld:pubmed |
pubmed-article:8493533 | pubmed:affiliation | Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205. | lld:pubmed |
pubmed-article:8493533 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8493533 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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