Výsledky vyhledávání - "Karetsou, Z."

Identification of distinct SET/TAF-Ibeta domains required for core histone binding and quantitative characterisation of the interaction

Autor: Karetsou, Z., Emmanouilidou, A., Sanidas, I., Liokatis, S., Nikolakaki, E., Politou, A. S., Papamarcaki, T.

BACKGROUND: The assembly of nucleosomes to higher-order chromatin structures is finely tuned by the relative affinities of histones for chaperones and nucleosomal binding sites. The myeloid leukaemia protein SET/TAF-Ibeta belongs to the NAP1 family o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_____10561::9547c8c5a020e67df945dfb063e21a20
http://olympias.lib.uoi.gr/jspui/handle/123456789/21058

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On the intracellular trafficking of mouse S5 ribosomal protein from cytoplasm to nucleoli

Autor: Matragkou, Ch, Papachristou, H., Karetsou, Z., Papadopoulos, G., Papamarcaki, T., Vizirianakis, I. S., Tsiftsoglou, A. S., Choli-Papadopoulou, T.

The non-ribosomal functions of mammalian ribosomal proteins have recently attracted worldwide attention. The mouse ribosomal protein S5 (rpS5) derived from ribosomal material is an assembled non-phosphorylated protein. The free form of rpS5 protein,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_____10561::35ee5948585938f7b6f700e6acd689ea
http://olympias.lib.uoi.gr/jspui/handle/123456789/19638

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The histone chaperone SET/TAF-Ibeta interacts functionally with the CREB-binding protein

Autor: Karetsou, Z., Martic, G., Sflomos, G., Papamarcaki, T.

The oncoprotein SET/TAF-Ibeta is a histone chaperone which is involved in cell-cycle control and chromatin remodeling. Confocal laser scanning microscopy reveals that SET is localized in distinct foci of variable size throughout the nucleoplasm of in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::e55a8abf577acbab9eb2c252f8237e19
http://olympias.lib.uoi.gr/jspui/handle/123456789/24455

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Parathymosin affects the binding of linker histone H1 to nucleosomes and remodels chromatin structure

Autor: Martic, G., Karetsou, Z., Kefala, K., Politou, A. S., Clapier, C. R., Straub, T., Papamarcaki, T.

Linker histone H1 is the major factor that stabilizes higher order chromatin structure and modulates the action of chromatin-remodeling enzymes. We have previously shown that parathymosin, an acidic, nuclear protein binds to histone H1 in vitro and i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_____10561::f7ce1418ca82a697c07ad29799ac5e88
http://olympias.lib.uoi.gr/jspui/handle/123456789/19463

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Prothymosin alpha associates with the oncoprotein SET and is involved in chromatin decondensation

Autor: Karetsou, Z., Martic, G., Tavoulari, S., Christoforidis, S., Wilm, M., Gruss, C., Papamarcaki, T.

Prothymosin alpha (ProTalpha) is a histone H1-binding protein that interacts with the transcription coactivator CREB-binding protein and potentiates transcription. Based on coimmunoprecipitation and mammalian two-hybrid assays, we show here that ProT

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_____10561::124a32b34d61cdfaddc76642d32ebd1c
http://olympias.lib.uoi.gr/jspui/handle/123456789/18944

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Prothymosin alpha interacts with the CREB-binding protein and potentiates transcription

Autor: Karetsou, Z., Kretsovali, A., Murphy, C., Tsolas, O., Papamarcaki, T.

Prothymosin alpha (ProTalpha) is a histone H1-binding protein localized in sites of active transcription in the nucleus. We report here that ProTalpha physically interacts with the CREB-binding protein (CBP), which is a versatile transcription co-act

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_____10561::7c9578218825fa047d573ae41263084c
http://olympias.lib.uoi.gr/jspui/handle/123456789/18939

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