pubmed-article:10882738 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10882738 | lifeskim:mentions | umls-concept:C0126732 | lld:lifeskim |
pubmed-article:10882738 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
pubmed-article:10882738 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:10882738 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:10882738 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
pubmed-article:10882738 | pubmed:issue | 38 | lld:pubmed |
pubmed-article:10882738 | pubmed:dateCreated | 2000-11-3 | lld:pubmed |
pubmed-article:10882738 | pubmed:abstractText | X-ray crystal structures of the NF-kappa B.I kappa B alpha complex revealed an extensive and complex protein-protein interface involving independent structural elements present in both I kappa B alpha and NF-kappa B. In this study, we employ a gel electrophoretic mobility shift assay to assess and quantitate the relative contributions of the observed interactions toward overall complex binding affinity. I kappa B alpha preferentially binds to the p50/p65 heterodimer and p65 homodimer, with binding to p50 homodimer being significantly weaker. Our results indicate that the nuclear localization sequence and the region C-terminal to it of the NF-kappa B p65 subunit is a major contributor to NF-kappa B. I kappa B alpha complex formation. Additionally, there are no contacts between the corresponding nuclear localization signal tetrapeptide of p50 and I kappa B alpha. A second set of interactions involving the acidic C-terminal/PEST-like region of I kappa B alpha and the NF-kappa B p65 subunit N-terminal domain also contributes binding energy toward formation of the complex. This interaction is highly dynamic and nonspecific in nature, as shown by oxidative cysteine cross-linking. Phosphorylation of the C-terminal/PEST-like region by casein kinase II further enhances binding. | lld:pubmed |
pubmed-article:10882738 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10882738 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10882738 | pubmed:language | eng | lld:pubmed |
pubmed-article:10882738 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10882738 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10882738 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10882738 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10882738 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10882738 | pubmed:month | Sep | lld:pubmed |
pubmed-article:10882738 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10882738 | pubmed:author | pubmed-author:GhoshGG | lld:pubmed |
pubmed-article:10882738 | pubmed:author | pubmed-author:HuxfordTT | lld:pubmed |
pubmed-article:10882738 | pubmed:author | pubmed-author:PhelpsC BCB | lld:pubmed |
pubmed-article:10882738 | pubmed:author | pubmed-author:Sengchanthala... | lld:pubmed |
pubmed-article:10882738 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10882738 | pubmed:day | 22 | lld:pubmed |
pubmed-article:10882738 | pubmed:volume | 275 | lld:pubmed |
pubmed-article:10882738 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10882738 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10882738 | pubmed:pagination | 29840-6 | lld:pubmed |
pubmed-article:10882738 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:10882738 | pubmed:meshHeading | pubmed-meshheading:10882738... | lld:pubmed |
pubmed-article:10882738 | pubmed:meshHeading | pubmed-meshheading:10882738... | lld:pubmed |
pubmed-article:10882738 | pubmed:meshHeading | pubmed-meshheading:10882738... | lld:pubmed |
pubmed-article:10882738 | pubmed:meshHeading | pubmed-meshheading:10882738... | lld:pubmed |
pubmed-article:10882738 | pubmed:meshHeading | pubmed-meshheading:10882738... | lld:pubmed |
pubmed-article:10882738 | pubmed:meshHeading | pubmed-meshheading:10882738... | lld:pubmed |
pubmed-article:10882738 | pubmed:meshHeading | pubmed-meshheading:10882738... | lld:pubmed |
pubmed-article:10882738 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10882738 | pubmed:articleTitle | Mechanism of I kappa B alpha binding to NF-kappa B dimers. | lld:pubmed |
pubmed-article:10882738 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, USA. | lld:pubmed |
pubmed-article:10882738 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10882738 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10882738 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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