| pubmed-article:10876243 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C0205160 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C0079419 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C1419790 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:10876243 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:10876243 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:10876243 | pubmed:dateCreated | 2000-7-21 | lld:pubmed |
| pubmed-article:10876243 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:abstractText | A Ca2+ dependent conformational change in dimeric S100B(betabeta) is required for it to bind p53 and inhibit phosphorylation of this tumor suppressor in its C-terminal negative regulatory domain. A peptide derived from this region of p53 (residues 367-388) was found to have no regular structure in its native form by NMR spectroscopy, but becomes helical when bound to Ca2+ loaded S100B(betabeta). The three-dimensional structure of this complex reveals several favorable hydrophobic and electrostatic interactions between S100B(betabeta) and the p53 peptide in the binding pocket, where S100B(betabeta) sterically blocks sites of phosphorylation and acetylation on p53 that are important for transcription activation. | lld:pubmed |
| pubmed-article:10876243 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10876243 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10876243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10876243 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10876243 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10876243 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:10876243 | pubmed:author | pubmed-author:WeberD JDJ | lld:pubmed |
| pubmed-article:10876243 | pubmed:author | pubmed-author:BaldisseriD... | lld:pubmed |
| pubmed-article:10876243 | pubmed:author | pubmed-author:RustandiR RRR | lld:pubmed |
| pubmed-article:10876243 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10876243 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:10876243 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10876243 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10876243 | pubmed:pagination | 570-4 | lld:pubmed |
| pubmed-article:10876243 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:meshHeading | pubmed-meshheading:10876243... | lld:pubmed |
| pubmed-article:10876243 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10876243 | pubmed:articleTitle | Structure of the negative regulatory domain of p53 bound to S100B(betabeta). | lld:pubmed |
| pubmed-article:10876243 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N. Greene Street, Baltimore, Maryland 21201, USA. | lld:pubmed |
| pubmed-article:10876243 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10876243 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10876243 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:7157 | entrezgene:pubmed | pubmed-article:10876243 | lld:entrezgene |
| entrez-gene:6285 | entrezgene:pubmed | pubmed-article:10876243 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:10876243 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10876243 | lld:pubmed |
