| pubmed-article:8816457 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8816457 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8816457 | lifeskim:mentions | umls-concept:C0166033 | lld:lifeskim |
| pubmed-article:8816457 | lifeskim:mentions | umls-concept:C0205322 | lld:lifeskim |
| pubmed-article:8816457 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:8816457 | lifeskim:mentions | umls-concept:C1749855 | lld:lifeskim |
| pubmed-article:8816457 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:8816457 | pubmed:dateCreated | 1996-11-15 | lld:pubmed |
| pubmed-article:8816457 | pubmed:abstractText | Stimulation with inducers that cause persistent activation of NF-kappa B results in the degradation of the NF-kappa B inhibitors, I kappa B alpha and I kappa B beta. Despite the rapid resynthesis and accumulation of I kappa B alpha, NF-kappa B remains induced under these conditions. We now report that I kappa B beta is also resynthesized in stimulated cells and appears as an unphosphorylated protein. The unphosphorylated I kappa B beta forms a stable complex with NF-kappa B in the cytosol; however, this binding fails to mask the nuclear localization signal and DNA binding domain on NF-kappa B, and the I kappa B beta-NF-kappa B complex enters the nucleus. It appears therefore that during prolonged stimulation, I kappa B beta functions as a chaperone for NF-kappa B by protecting it from I kappa B alpha and allowing it to be transported to the nucleus. | lld:pubmed |
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| pubmed-article:8816457 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8816457 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8816457 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8816457 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8816457 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:8816457 | pubmed:author | pubmed-author:GhoshSS | lld:pubmed |
| pubmed-article:8816457 | pubmed:author | pubmed-author:PhillipsRR | lld:pubmed |
| pubmed-article:8816457 | pubmed:author | pubmed-author:DouglasII | lld:pubmed |
| pubmed-article:8816457 | pubmed:author | pubmed-author:SuyangHH | lld:pubmed |
| pubmed-article:8816457 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8816457 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:8816457 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8816457 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8816457 | pubmed:pagination | 5444-9 | lld:pubmed |
| pubmed-article:8816457 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8816457 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8816457 | pubmed:articleTitle | Role of unphosphorylated, newly synthesized I kappa B beta in persistent activation of NF-kappa B. | lld:pubmed |
| pubmed-article:8816457 | pubmed:affiliation | Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut, USA. | lld:pubmed |
| pubmed-article:8816457 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8816457 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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