| pubmed-article:9013886 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9013886 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:9013886 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9013886 | lifeskim:mentions | umls-concept:C1180347 | lld:lifeskim |
| pubmed-article:9013886 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:9013886 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:9013886 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9013886 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:9013886 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:9013886 | pubmed:issue | 2-3 | lld:pubmed |
| pubmed-article:9013886 | pubmed:dateCreated | 1997-2-27 | lld:pubmed |
| pubmed-article:9013886 | pubmed:abstractText | The effects of HIV-1 encoded proteins NCp7, vpr and NCp7:vpr complex on the activity of protein phosphatase-2A0 have been tested. We report that NCp7 is an activator of protein phosphatase-2A0 and that vpr activated protein phosphatase-2A0 only slightly. We also report that NCp7 and vpr form a tight complex which becomes a more potent activator of protein phosphatase-2A0 than NCp7 alone. The ability of NCp7 to activate protein phosphatase-2A0 is regulated by vpr. The C-terminal portion of vpr prevents NCp7 from activating protein phosphatase-2A0 while the N-terminal portion of vpr potentiates the effect of NCp7 on the activity of protein phosphatase-2A0. Our findings indicate that vpr may be acting as a targeting subunit which directs NCp7 to activate protein phosphatase-2A0. In view of the fact that protein phosphatase-2A functions as an inhibitor of G0 to M transition of the cell cycle and is involved in other key cellular processes such as the control of RNA transcription, the results presented in this report may explain how HIV-1 causes cell cycle arrest which may lead to CD4+ T cell depletion and also how it disturbs normal cellular processes of its host cell. | lld:pubmed |
| pubmed-article:9013886 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9013886 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9013886 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9013886 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9013886 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:9013886 | pubmed:author | pubmed-author:RoquesB PBP | lld:pubmed |
| pubmed-article:9013886 | pubmed:author | pubmed-author:OzonRR | lld:pubmed |
| pubmed-article:9013886 | pubmed:author | pubmed-author:TungH YHY | lld:pubmed |
| pubmed-article:9013886 | pubmed:author | pubmed-author:ZhaoL JLJ | lld:pubmed |
| pubmed-article:9013886 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:9013886 | pubmed:author | pubmed-author:CaylaXX | lld:pubmed |
| pubmed-article:9013886 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9013886 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:9013886 | pubmed:volume | 401 | lld:pubmed |
| pubmed-article:9013886 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9013886 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9013886 | pubmed:pagination | 197-201 | lld:pubmed |
| pubmed-article:9013886 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:9013886 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9013886 | pubmed:articleTitle | Direct activation of protein phosphatase-2A0 by HIV-1 encoded protein complex NCp7:vpr. | lld:pubmed |
| pubmed-article:9013886 | pubmed:affiliation | Laboratoire de Physiologie de la Reproduction, CNRS URA 1449, INRA, Université Pierre et Marie Curie, Paris, France. ltung@hall.snv.jussieu.fr | lld:pubmed |
| pubmed-article:9013886 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9013886 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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