http://www.cnr.it/ontology/cnr/individuo/prodotto/ID4612
Retinoblastoma protein acts as Pax 8 transcriptional coactivator. (Articolo in rivista)
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- Label
- Retinoblastoma protein acts as Pax 8 transcriptional coactivator. (Articolo in rivista) (literal)
- Anno
- 2005-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1038/sj.onc.1208861 (literal)
- Alternative label
Miccadei S.1, Provenzano C.2, Mojzisek M.3, Natali P.G.4, Civitareale D.5. (2005)
Retinoblastoma protein acts as Pax 8 transcriptional coactivator.
in Oncogene (Basingstoke)
(literal)
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- Miccadei S.1, Provenzano C.2, Mojzisek M.3, Natali P.G.4, Civitareale D.5. (literal)
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- Impact Factor = 6.318 (literal)
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- ISI Web of Science (WOS) (literal)
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- 1,3,4,5 = Molecular Pathology Laboratory, Regina Elena Cancer Institute, Via delle Messi d'Oro 156, 00158 Rome, Italy;
2,5 = Institute of Neurobiology and Molecular Medicine, National Council Research, Via del Fosso del Cavaliere 100, 00133 Rome, Italy;
3 = Department of Medical Biology and Genetics, Charles University, Faculty of Medicine in Hradec Králové, Simkova 870, 500 01 Hradec Kralove, Czech Republic. (literal)
- Titolo
- Retinoblastoma protein acts as Pax 8 transcriptional coactivator. (literal)
- Abstract
- Control of cell proliferation and differentiation by the retinoblastoma protein (pRb) depends on its interactions with key cellular substrates. Available data indicate that pRb and the transcription factor Pax 8 play a crucial role in the differentiation of thyroid follicular cells. In this study, we show that pRb takes part in the complex assembled on the thyroperoxidase gene promoter acting as a transcriptional coactivator of Pax 8. Accordingly, pRb interacts with and potentiates Pax 8 transcriptional activity. In addition, we show that the downregulation of pRb gene expression, in thyrocytes, through RNA interference results in a reduction of the thyroperoxidase gene promoter activity mediated by the Pax 8-binding site. In agreement with these results and with the ability of the adenoviral protein E1A to bind pRb, we show that E1A downregulates Pax 8 activity and that such inhibition requires the E1A-Rb interaction. Furthermore, we show that the Pax 8/pRb synergy plays a role on the sodium/iodide symporter gene expression as well. (literal)
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