| pubmed-article:15657065 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15657065 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:15657065 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:15657065 | lifeskim:mentions | umls-concept:C1420556 | lld:lifeskim |
| pubmed-article:15657065 | lifeskim:mentions | umls-concept:C1424530 | lld:lifeskim |
| pubmed-article:15657065 | lifeskim:mentions | umls-concept:C1328815 | lld:lifeskim |
| pubmed-article:15657065 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:15657065 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:15657065 | lifeskim:mentions | umls-concept:C1637379 | lld:lifeskim |
| pubmed-article:15657065 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:15657065 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15657065 | pubmed:dateCreated | 2005-3-11 | lld:pubmed |
| pubmed-article:15657065 | pubmed:abstractText | NO is an important factor that induces post-translational modifications of proteins by cellular reduction and oxidation mechanism: cysteinyl-nitrosylation or Tyr nitration. Nuclear factor (NF)-kappaB activity can be rapidly suppressed by sodium nitroprusside, a NO donor. This effect was effectively reversed by peroxynitrite scavenger deferoxamine, suggesting a Tyr nitration-mediated mechanism. Western blot with nitrotyrosine-specific antibody demonstrated that the p65 subunit of NF-kappaB was predominantly nitrated on Tyr residues. Tyr nitration of p65 induced its dissociation from p50, its association with IkappaBalpha, and subsequent sequestration of p65 in the cytoplasm by IkappaBalpha-mediated export. Liquid chromatography-coupled nanoelectrospray mass spectrometry revealed specific nitration on Tyr-66 and Tyr-152 residues of p65. Mutation studies confirmed that both Tyr-66 and Tyr-152 residues were important for the direct effects of NO on p65, which resulted in more p65 export and inactivation of NF-kappaB activity. This study identified a novel and efficient pathway where NO rapidly inactivated NF-kappaB activity by inducing Tyr nitration on p65. | lld:pubmed |
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| pubmed-article:15657065 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15657065 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15657065 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15657065 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:15657065 | pubmed:issn | 1535-9476 | lld:pubmed |
| pubmed-article:15657065 | pubmed:author | pubmed-author:WeiLi-NaLN | lld:pubmed |
| pubmed-article:15657065 | pubmed:author | pubmed-author:ParkSung... | lld:pubmed |
| pubmed-article:15657065 | pubmed:author | pubmed-author:HuXinliX | lld:pubmed |
| pubmed-article:15657065 | pubmed:author | pubmed-author:HuqM D... | lld:pubmed |
| pubmed-article:15657065 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15657065 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:15657065 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15657065 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15657065 | pubmed:pagination | 300-9 | lld:pubmed |
| pubmed-article:15657065 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:15657065 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15657065 | pubmed:articleTitle | Tyrosine nitration on p65: a novel mechanism to rapidly inactivate nuclear factor-kappaB. | lld:pubmed |
| pubmed-article:15657065 | pubmed:affiliation | Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455, USA. | lld:pubmed |
| pubmed-article:15657065 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15657065 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15657065 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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