| pubmed-article:7814425 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7814425 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7814425 | lifeskim:mentions | umls-concept:C0167954 | lld:lifeskim |
| pubmed-article:7814425 | lifeskim:mentions | umls-concept:C0026473 | lld:lifeskim |
| pubmed-article:7814425 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
| pubmed-article:7814425 | lifeskim:mentions | umls-concept:C1514570 | lld:lifeskim |
| pubmed-article:7814425 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:7814425 | lifeskim:mentions | umls-concept:C0127400 | lld:lifeskim |
| pubmed-article:7814425 | lifeskim:mentions | umls-concept:C1363844 | lld:lifeskim |
| pubmed-article:7814425 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7814425 | pubmed:dateCreated | 1995-2-3 | lld:pubmed |
| pubmed-article:7814425 | pubmed:abstractText | Proteolytic processing of select constituents of the nuclear factor kappa B (NF-kappa B)/inhibitor kappa B alpha (I kappa B) transcription factor system plays an important role in regulating the biological responses of monocytes to pro-inflammatory mediators. Nuclear translocation of NF-kappa B is preceded by the proteolytic degradation of I kappa B alpha, an ankyrin motif-rich inhibitor that traps NF-kappa B in the cytoplasm. In addition, formation of cytoplasmic NF-kappa B/I kappa B alpha complexes in quiescent cells requires constitutive proteolytic processing of p105, another ankyrin motif-rich inhibitory protein from which the p50 subunit of NF-kappa B is generated. We have demonstrated that, following stimulation of human monocytic cells with lipopolysaccharide or tumor necrosis factor-alpha, this critical p105 processing event is up-regulated in concert with the inactivation of I kappa B alpha. Moreover, the degradative loss of both p105 and I kappa B alpha is prevented in cells depleted of intracellular ATP. In activated monocytes, however, I kappa B alpha degradation occurs more rapidly than p105 processing to p50. Together these findings provide direct biochemical evidence that p105 and I kappa B alpha are differentially sensitive targets for inducible proteolysis via ATP-dependent degradative pathways. | lld:pubmed |
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| pubmed-article:7814425 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7814425 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7814425 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7814425 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7814425 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:7814425 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7814425 | pubmed:author | pubmed-author:HawigerJJ | lld:pubmed |
| pubmed-article:7814425 | pubmed:author | pubmed-author:BallardD WDW | lld:pubmed |
| pubmed-article:7814425 | pubmed:author | pubmed-author:DonaldRR | lld:pubmed |
| pubmed-article:7814425 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7814425 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:7814425 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7814425 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7814425 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7814425 | pubmed:pagination | 9-12 | lld:pubmed |
| pubmed-article:7814425 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7814425 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7814425 | pubmed:articleTitle | Proteolytic processing of NF-kappa B/I kappa B in human monocytes. ATP-dependent induction by pro-inflammatory mediators. | lld:pubmed |
| pubmed-article:7814425 | pubmed:affiliation | Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232. | lld:pubmed |
| pubmed-article:7814425 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7814425 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7814425 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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