pubmed-article:9252186 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9252186 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
pubmed-article:9252186 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
pubmed-article:9252186 | lifeskim:mentions | umls-concept:C0663914 | lld:lifeskim |
pubmed-article:9252186 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
pubmed-article:9252186 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:9252186 | pubmed:issue | 6642 | lld:pubmed |
pubmed-article:9252186 | pubmed:dateCreated | 1997-8-27 | lld:pubmed |
pubmed-article:9252186 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9252186 | pubmed:abstractText | Nuclear transcription factors of the NF-kappaB/Rel family are inhibited by IkappaB proteins, which inactivate NF-kappaB by trapping it in the cell cytoplasm. Phosphorylation of IkappaBs marks them out for destruction, thereby relieving their inhibitory effect on NF-kappaB. A cytokine-activated protein kinase complex, IKK (for IkappaB kinase), has now been purified that phosphorylates IkappaBs on the sites that trigger their degradation. A component of IKK was molecularly cloned and identified as a serine kinase. IKK turns out to be the long-sought-after protein kinase that mediates the critical regulatory step in NF-kappaB activation. | lld:pubmed |
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pubmed-article:9252186 | pubmed:language | eng | lld:pubmed |
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pubmed-article:9252186 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9252186 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9252186 | pubmed:month | Aug | lld:pubmed |
pubmed-article:9252186 | pubmed:issn | 0028-0836 | lld:pubmed |
pubmed-article:9252186 | pubmed:author | pubmed-author:HayakawaMM | lld:pubmed |
pubmed-article:9252186 | pubmed:author | pubmed-author:KarinMM | lld:pubmed |
pubmed-article:9252186 | pubmed:author | pubmed-author:RothwarfD MDM | lld:pubmed |
pubmed-article:9252186 | pubmed:author | pubmed-author:DiDonatoJ AJA | lld:pubmed |
pubmed-article:9252186 | pubmed:author | pubmed-author:ZandaMM | lld:pubmed |
pubmed-article:9252186 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9252186 | pubmed:day | 7 | lld:pubmed |
pubmed-article:9252186 | pubmed:volume | 388 | lld:pubmed |
pubmed-article:9252186 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9252186 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9252186 | pubmed:pagination | 548-54 | lld:pubmed |
pubmed-article:9252186 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:9252186 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9252186 | pubmed:articleTitle | A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB. | lld:pubmed |
pubmed-article:9252186 | pubmed:affiliation | Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, University of California at San Diego, La Jolla 92093-0636, USA. | lld:pubmed |
pubmed-article:9252186 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9252186 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9252186 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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