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| pubmed-article:2001591 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2001591 | pubmed:dateCreated | 1991-4-18 | lld:pubmed |
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| pubmed-article:2001591 | pubmed:abstractText | The sequence and biochemical properties of the product of the cloned cDNA for the p65 subunit of nuclear factor kappa B (NF-kappa B) have been determined. The cDNA has an open reading frame of 549 amino acids capable of encoding a 60 kd protein. NF-kappa B p65 contains an amino-terminal region of 320 amino acids with extensive similarity to the oncogene c-rel and lesser similarity to NF-kappa B p50. In vitro translated p65 forms a DNA-binding complex with NF-kappa B p50, and the binding of this complex can be specifically inhibited by purified I kappa B. Progressive carboxy-terminal deletions of p65 show that, contrary to previous assumptions, p65 does include a DNA-binding domain that in vivo might become activated only through hetero-oligomerization with p50. DNA binding by truncated p65 is inhibited by I kappa B, thus mapping the I kappa B interaction domain to the rel-homologous region and suggesting that I kappa B exerts its inhibitory effect upon NF-kappa B primarily through interaction with p65. | lld:pubmed |
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| pubmed-article:2001591 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2001591 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2001591 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2001591 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2001591 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:2001591 | pubmed:author | pubmed-author:BaltimoreDD | lld:pubmed |
| pubmed-article:2001591 | pubmed:author | pubmed-author:GhoshSS | lld:pubmed |
| pubmed-article:2001591 | pubmed:author | pubmed-author:TempstPP | lld:pubmed |
| pubmed-article:2001591 | pubmed:author | pubmed-author:NolanG PGP | lld:pubmed |
| pubmed-article:2001591 | pubmed:author | pubmed-author:LashP RPR | lld:pubmed |
| pubmed-article:2001591 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2001591 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:2001591 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:2001591 | pubmed:geneSymbol | c-rel | lld:pubmed |
| pubmed-article:2001591 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2001591 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2001591 | pubmed:pagination | 961-9 | lld:pubmed |
| pubmed-article:2001591 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:2001591 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2001591 | pubmed:articleTitle | DNA binding and I kappa B inhibition of the cloned p65 subunit of NF-kappa B, a rel-related polypeptide. | lld:pubmed |
| pubmed-article:2001591 | pubmed:affiliation | Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, Massachusetts 02142. | lld:pubmed |
| pubmed-article:2001591 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2001591 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2001591 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2001591 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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