| pubmed-article:3500792 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3500792 | lifeskim:mentions | umls-concept:C0312738 | lld:lifeskim |
| pubmed-article:3500792 | lifeskim:mentions | umls-concept:C0162326 | lld:lifeskim |
| pubmed-article:3500792 | lifeskim:mentions | umls-concept:C2246553 | lld:lifeskim |
| pubmed-article:3500792 | lifeskim:mentions | umls-concept:C0949374 | lld:lifeskim |
| pubmed-article:3500792 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:3500792 | pubmed:dateCreated | 1988-1-29 | lld:pubmed |
| pubmed-article:3500792 | pubmed:abstractText | DNA-nuclear protein interactions were studied with synthetic recombination signal sequences (RSSs) for immunoglobulin V-J joining. With a gel retardation assay, a DNA-binding protein that specifically interacts with RSSs was detected in nuclear extracts from a pre-B cell line, 38B9. This protein was found in all the recombination-competent pre-B cell lines tested in this study, but not in myeloma, mature T cell, monocyte, or fibroblast cell lines. DNA footprint analysis with dimethyl sulfate demonstrated that the 7-mer region of the RSS was strongly protected when complexed with the binding protein. Furthermore, a single base substitution in the 7-mer region totally abolished the binding. The molecular mechanism of V-J joining is discussed in the context of the RSS-binding protein. | lld:pubmed |
| pubmed-article:3500792 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3500792 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3500792 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3500792 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3500792 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3500792 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3500792 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3500792 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3500792 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:3500792 | pubmed:author | pubmed-author:OkazakiKK | lld:pubmed |
| pubmed-article:3500792 | pubmed:author | pubmed-author:SakanoHH | lld:pubmed |
| pubmed-article:3500792 | pubmed:author | pubmed-author:AkiraSS | lld:pubmed |
| pubmed-article:3500792 | pubmed:author | pubmed-author:AguileraR JRJ | lld:pubmed |
| pubmed-article:3500792 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3500792 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:3500792 | pubmed:volume | 51 | lld:pubmed |
| pubmed-article:3500792 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3500792 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3500792 | pubmed:pagination | 909-17 | lld:pubmed |
| pubmed-article:3500792 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:3500792 | pubmed:meshHeading | pubmed-meshheading:3500792-... | lld:pubmed |
| pubmed-article:3500792 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3500792 | pubmed:articleTitle | A pre-B cell nuclear protein that specifically interacts with the immunoglobulin V-J recombination sequences. | lld:pubmed |
| pubmed-article:3500792 | pubmed:affiliation | Department of Microbiology and Immunology, University of California, Berkeley 94720. | lld:pubmed |
| pubmed-article:3500792 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3500792 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3500792 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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