| pubmed-article:7818536 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7818536 | lifeskim:mentions | umls-concept:C0040623 | lld:lifeskim |
| pubmed-article:7818536 | lifeskim:mentions | umls-concept:C0080055 | lld:lifeskim |
| pubmed-article:7818536 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
| pubmed-article:7818536 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7818536 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:7818536 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:7818536 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
| pubmed-article:7818536 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:7818536 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7818536 | pubmed:dateCreated | 1995-2-9 | lld:pubmed |
| pubmed-article:7818536 | pubmed:abstractText | By using a novel genetic approach, based on the properties of lambda cl repressor, we demonstrate that the HIV-1 Tat protein specifically interacts with the human p53 protein via the p53 O2 dimerization domain. By random and site-specific mutagenesis, we also identify the residues in Tat and O2 peptides which are involved in this interaction. Two alternative biological consequences are expected to result from Tat-p53 interaction: (i) Tat-O2 interaction inactivates p53 regulation function, thus producing cell transformation; (ii) Tat-O2 interaction favours the formation of p53 dimers, thus leading the cell towards apoptosis. | lld:pubmed |
| pubmed-article:7818536 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7818536 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7818536 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7818536 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7818536 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:7818536 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:7818536 | pubmed:author | pubmed-author:LongoFF | lld:pubmed |
| pubmed-article:7818536 | pubmed:author | pubmed-author:GiglianiFF | lld:pubmed |
| pubmed-article:7818536 | pubmed:author | pubmed-author:MarchettiM... | lld:pubmed |
| pubmed-article:7818536 | pubmed:author | pubmed-author:CastagnoliLL | lld:pubmed |
| pubmed-article:7818536 | pubmed:author | pubmed-author:BattagliaP... | lld:pubmed |
| pubmed-article:7818536 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7818536 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:7818536 | pubmed:volume | 206 | lld:pubmed |
| pubmed-article:7818536 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7818536 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7818536 | pubmed:pagination | 326-34 | lld:pubmed |
| pubmed-article:7818536 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:7818536 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7818536 | pubmed:articleTitle | A novel approach to protein-protein interaction: complex formation between the p53 tumor suppressor and the HIV Tat proteins. | lld:pubmed |
| pubmed-article:7818536 | pubmed:affiliation | Dipartimento di Biopatologia Umana Sezione di Biologia Cellulare Università di Roma La Sapienza, Rome, Italy. | lld:pubmed |
| pubmed-article:7818536 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7818536 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7818536 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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