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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1996-9-9
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pubmed:abstractText |
It has been suggested that the NF-kappaB transcription factor family may mediate expression of the gene encoding the cytokine-inducible form of nitric oxide synthase (iNOS). To establish if nitric oxide (NO) could in turn affect activity of NF-kappaB, the ability of NO-donor compounds to influence NF-kappaB DNA binding activity in vitro was investigated. NO-donor compounds sodium nitroprusside (SNP) and S-nitroso-N-acetylpenicillamine (SNAP) both inhibited the DNA binding activity of recombinant NF-kappaB p50 and p65 homodimers and of p50-p65 heterodimers. Inhibition of NF-kappaB p50 DNA binding by NO-donor compounds involved modification of the conserved redox-sensitive C62 residue, as a C62S p50 mutant was significantly more resistant to SNP-mediated inactivation. Non-reducing SDS-polyacrylamide gel electrophoresis demonstrated that SNP could inhibit p50 DNA binding by mechanisms other than the formation of intersubunit disulphide bonds involving p50 residue C62. Electrospray ionization mass spectrometry of a synthetic NF-kappaB p5O peptide containing the C62 residue suggested that NO gas can modify C62 by S-nitrosylation. This study indicates that NO-donors can directly inhibit the DNA binding activity of NF-kappaB family proteins, suggesting that cellular NO provides another control mechanism for modulating the expression of NF-kappaB-responsive genes.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-1281150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-1281928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-1508666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-1620118,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-1740105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-1903539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-2023633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-2065663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-2118682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-2536920,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-2544731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-3495737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7508926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7509810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7522345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7522969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7528106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7530332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7530762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7575553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7584622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7592903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7615515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7622526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7739549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7775482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7830764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7888182,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7923361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-7923362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8076680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8108414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8258718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8262046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8278379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8302865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8334993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8423807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8432991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8491191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8493089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710491-8496188
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2236-42
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8710491-Base Sequence,
pubmed-meshheading:8710491-Binding Sites,
pubmed-meshheading:8710491-DNA,
pubmed-meshheading:8710491-Mass Spectrometry,
pubmed-meshheading:8710491-Molecular Sequence Data,
pubmed-meshheading:8710491-NF-kappa B,
pubmed-meshheading:8710491-NF-kappa B p50 Subunit,
pubmed-meshheading:8710491-Nitric Oxide,
pubmed-meshheading:8710491-Nitroprusside,
pubmed-meshheading:8710491-Penicillamine,
pubmed-meshheading:8710491-Protein Binding,
pubmed-meshheading:8710491-Recombinant Fusion Proteins,
pubmed-meshheading:8710491-S-Nitroso-N-Acetylpenicillamine,
pubmed-meshheading:8710491-Transcription Factor RelA
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pubmed:year |
1996
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pubmed:articleTitle |
Inhibition of NF-kappaB DNA binding by nitric oxide.
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pubmed:affiliation |
School of Biological and Medical Sciences, Irvine Building, University of St. Andrews, Fife, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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