Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Thymosin/*analogs & derivatives/*metabolism"'
Publikováno v:
European Journal of Biochemistry. 242:67-74
We have studied the molecular associations of parathymosin, an acidic polypeptide with a wide tissue distribution, by means of three approaches; ligand blotting; native electrophoresis; and immunoprecipitation. We report here that parathymosin binds
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98161721a41590c31bfd2b712e81d469
https://doi.org/10.1111/j.1432-1033.1996.0067r.x
https://doi.org/10.1111/j.1432-1033.1996.0067r.x
Autor:
Letsas, K. P., Frangou-Lazaridis, M.
Prothymosin alpha is an extremely abundant nuclear oncoprotein-transcription factor essential for cell cycle progression and proliferation that has been recently suggested as an anti- apoptotic factor. Similarly to other oncoproteins, prothymosin alp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_____10561::aa4d03a8e71cfed4a9fab664e907fb1c
http://olympias.lib.uoi.gr/jspui/handle/123456789/17979
http://olympias.lib.uoi.gr/jspui/handle/123456789/17979
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
http://olympias.lib.uoi.gr/jspui/handle/123456789/19463
Autor:
Yang, C. H., Murti, A., Baker, S. J., Frangou-Lazaridis, M., Vartapetian, A. B., Murti, K. G., Pfeffer, L. M.
Interferons (IFNs) play critical roles in host defense by modulating the expression of various genes via tyrosine phosphorylation of STAT transcription factors. Many cytokines including IFNs induce tyrosine phosphorylation of the STAT3 transcription
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_____10561::8d4daa5256ed927d0147deba62ad7571
http://olympias.lib.uoi.gr/jspui/handle/123456789/20710
http://olympias.lib.uoi.gr/jspui/handle/123456789/20710
Autor:
Vareli, K., Frangou-Lazaridis, M.
Prothymosin a is a small, acidic, ubiquitous protein, thought to play a role in cell proliferation, carcinogenesis and apoptosis. We have reported earlier that in the interphase nucleus prothymosin a exhibits a punctuated nuclear distribution associa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_____10561::9b1405d7676196b4fa72bd317cf8df0d
http://olympias.lib.uoi.gr/jspui/handle/123456789/18938
http://olympias.lib.uoi.gr/jspui/handle/123456789/18938
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
http://olympias.lib.uoi.gr/jspui/handle/123456789/18939
Prothymosin alpha and parathymosin are two ubiquitous small acidic nuclear proteins that are thought to be involved in cell cycle progression, proliferation, and cell differentiation. In an effort to investigate the molecular function of the two prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_____10561::b9c768bff92bdaf130eef9d0436b4fb1
http://olympias.lib.uoi.gr/jspui/handle/123456789/19686
http://olympias.lib.uoi.gr/jspui/handle/123456789/19686
Autor:
Maria Frangou-Lazaridis, Orestes Tsolas, Peter B. Becker, Raphael Sandaltzopoulos, Zoe Karetsou, Chun-Yen Lai, Thomais Papamarcaki
Publikováno v:
Nucleic acids research. 26(13)
Prothymosin alpha (ProTalpha) is an abundant acidic nuclear protein that may be involved in cell proliferation. In our search for its cellular partners, we have recently found that ProTalpha binds to linker histone H1. We now provide further evidence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4048ca432212ceb3ab22efae20f54188
https://pubmed.ncbi.nlm.nih.gov/9628907
https://pubmed.ncbi.nlm.nih.gov/9628907
Autor:
Papamarcaki, T., Tsolas, O.
Previous studies have shown that prothymosin alpha (ProT alpha) is a nuclear acidic protein implicated in cell proliferation. To identify proteins that interact with ProT alpha we have used ligand-blotting assays. We report here that purified ProT al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_____10561::93ea9c8b098240b5a474ca819317caa4
http://olympias.lib.uoi.gr/jspui/handle/123456789/18941
http://olympias.lib.uoi.gr/jspui/handle/123456789/18941
Autor:
Frillingos, S., Tsolas, O.
Differences in the tissue content of prothymosin alpha during the early postnatal development of male and female rats are reported. Thymus and spleen have been found to contain significantly higher amounts of prothymosin alpha in the newborn and prep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_____10561::7eafbc14e97a2896e5298e07cdaa54fe
http://olympias.lib.uoi.gr/jspui/handle/123456789/24013
http://olympias.lib.uoi.gr/jspui/handle/123456789/24013