| pubmed-article:18164680 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18164680 | lifeskim:mentions | umls-concept:C1416380 | lld:lifeskim |
| pubmed-article:18164680 | lifeskim:mentions | umls-concept:C1511997 | lld:lifeskim |
| pubmed-article:18164680 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:18164680 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:18164680 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
| pubmed-article:18164680 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18164680 | pubmed:dateCreated | 2008-1-18 | lld:pubmed |
| pubmed-article:18164680 | pubmed:abstractText | NEMO is an essential regulatory component of the IkappaB kinase (IKK) complex, which controls activation of the NF-kappaB signaling pathway. Herein, we show that NEMO exists as a disulfide-bonded dimer when isolated from several cell types and analyzed by SDS-polyacrylamide gel electrophoresis under non-reducing conditions. Treatment of cells with hydrogen peroxide (H(2)O(2)) induces further formation of NEMO dimers. Disulfide bond-mediated formation of NEMO dimers requires Cys54 and Cys347. The ability of these residues to form disulfide bonds is consistent with their location in a NEMO dimer structure that we generated by molecular modeling. We also show that pretreatment with H(2)O(2) decreases TNFalpha-induced IKK activity in NEMO-reconstituted cells, and that TNFalpha has a diminished ability to activate NF-kappaB DNA binding in cells reconstituted with NEMO mutant C54/347A. This study implicates NEMO as a target of redox regulation and presents the first structural model for the NEMO protein. | lld:pubmed |
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| pubmed-article:18164680 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18164680 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18164680 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18164680 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18164680 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18164680 | pubmed:issn | 1090-2104 | lld:pubmed |
| pubmed-article:18164680 | pubmed:author | pubmed-author:KalaitzidisDe... | lld:pubmed |
| pubmed-article:18164680 | pubmed:author | pubmed-author:GilmoreThomas... | lld:pubmed |
| pubmed-article:18164680 | pubmed:author | pubmed-author:ChandaniSushi... | lld:pubmed |
| pubmed-article:18164680 | pubmed:author | pubmed-author:ColemanKateK | lld:pubmed |
| pubmed-article:18164680 | pubmed:author | pubmed-author:HerscovitchMe... | lld:pubmed |
| pubmed-article:18164680 | pubmed:author | pubmed-author:CombWilliamW | lld:pubmed |
| pubmed-article:18164680 | pubmed:author | pubmed-author:EnnisThomasT | lld:pubmed |
| pubmed-article:18164680 | pubmed:author | pubmed-author:YongSheilaS | lld:pubmed |
| pubmed-article:18164680 | pubmed:author | pubmed-author:ArmsteadBrind... | lld:pubmed |
| pubmed-article:18164680 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18164680 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:18164680 | pubmed:volume | 367 | lld:pubmed |
| pubmed-article:18164680 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18164680 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18164680 | pubmed:pagination | 103-8 | lld:pubmed |
| pubmed-article:18164680 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:18164680 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18164680 | pubmed:articleTitle | Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347. | lld:pubmed |
| pubmed-article:18164680 | pubmed:affiliation | Department of Biology, Boston University, 5 Cummington Street, Boston, MA 02215, USA. | lld:pubmed |
| pubmed-article:18164680 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18164680 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:18164680 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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