pubmed-article:7663427 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7663427 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
pubmed-article:7663427 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
pubmed-article:7663427 | lifeskim:mentions | umls-concept:C1148673 | lld:lifeskim |
pubmed-article:7663427 | lifeskim:mentions | umls-concept:C2266866 | lld:lifeskim |
pubmed-article:7663427 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:7663427 | lifeskim:mentions | umls-concept:C0058090 | lld:lifeskim |
pubmed-article:7663427 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:7663427 | pubmed:dateCreated | 1995-10-12 | lld:pubmed |
pubmed-article:7663427 | pubmed:abstractText | NF-kappa B transcription factor regulates a wide variety of cellular and viral genes including the human immunodeficiency virus type 1. Here, we demonstrate that dihydrolipoate/alpha-lipoate redox couple which is a cofactor for mitochondrial dehydrogenases reactions, influences the DNA binding activity of NF-kappa B. The elimination of dithiothreitol in the electrophoretic mobility shift assay protocol resulted in the inability to detect DNA binding activity of activated NF-kappa B. The DNA binding activity was restored by the addition of dihydrolipoate in the binding reaction mixture. Inhibition of NF-kappa B DNA binding activity by in vitro exposure to a sulfhydryl oxidizing agent, diamide was also blocked by dihydrolipoate. In contrast, the addition of the oxidized form, alpha-lipoate inhibited the NF-kappa B DNA binding activity. Coincidentally, preincubation of Jurkat cells with dihydrolipoate potentiated and alpha-lipoate inhibited the okadaic acid-induced NF-kappa B activation as detected by assessing its DNA binding activity. These results suggest the redox exchange between lipoate and NF-kappa B molecules. Furthermore, since the inhibition of AP-1 DNA binding activity by diamide was also blocked by dihydrolipoate, this natural reductant may participate in the redox regulation of transcription factors by enhancing the DNA-protein interactions. | lld:pubmed |
pubmed-article:7663427 | pubmed:language | eng | lld:pubmed |
pubmed-article:7663427 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7663427 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7663427 | pubmed:month | Jun | lld:pubmed |
pubmed-article:7663427 | pubmed:issn | 1039-9712 | lld:pubmed |
pubmed-article:7663427 | pubmed:author | pubmed-author:PackerLL | lld:pubmed |
pubmed-article:7663427 | pubmed:author | pubmed-author:MizunoMM | lld:pubmed |
pubmed-article:7663427 | pubmed:author | pubmed-author:SuzukiY JYJ | lld:pubmed |
pubmed-article:7663427 | pubmed:author | pubmed-author:TritschlerH... | lld:pubmed |
pubmed-article:7663427 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7663427 | pubmed:volume | 36 | lld:pubmed |
pubmed-article:7663427 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7663427 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7663427 | pubmed:pagination | 241-6 | lld:pubmed |
pubmed-article:7663427 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
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pubmed-article:7663427 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7663427 | pubmed:articleTitle | Redox regulation of NF-kappa B DNA binding activity by dihydrolipoate. | lld:pubmed |
pubmed-article:7663427 | pubmed:affiliation | Department of Molecular & Cell Biology, University of California, Berkeley 94720, USA. | lld:pubmed |
pubmed-article:7663427 | pubmed:publicationType | Journal Article | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7663427 | lld:pubmed |