(2001). Phosphorylation of the EWS IQ domain regulates transcriptional activity of the EWS/ATF1 and EWS/FLI1 fusion proteins. Oncogene 20, 1756–1764.Olsen, R. J., and Hinrichs, S. H. (2001) Phosphorylation of the EWS IQ domain regulates transcriptional activity of the EWS/ATF1 and EWS...
The Ewing's sarcoma (EWS) oncogene contains an N-terminal transcriptional activation domain (EWSactivation domain, EAD) and a C-terminal RNA-binding domain (RBD). Although it has been established that the EAD is a potent trans-activation domain that is required for the oncogenic activity of ...
ews/ets fusion genes consistently maintain an intact and functional ets DNA binding domain (DBD) in all of these cases. We demonstrate here, however, that EWS/FLI1, the most prevalent EWS/ETS fusion, activates oncogenic pathways independent of its DBD. In in vivo tumor assays, EWS/FLI1 ...
EAT2A/EAT2B (Sh2d1b, SH2 domain protein 1B [Mus musculus], MGI:1349420, EAT-2, EAT-2A, Eat2, Eat2a, EWS/FLI1 activated transcript 2, Sh2d1b, SH2 domain protein 1B2, EAT-2B, Eat2b, Sh2d1c, EAT-2-related transducer)
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K. A. W. Lee, "Molecular recognition by the EWS transcrip- tional activation domain," Advances in Experimental Medicine and Biology, vol. 725, pp. 106-125, 2012.Lee, K.A.W. (2012) Molecular recognition by the EWS transcriptional activation domain. Adv. Exp. Med. Biol. 725, 106-125...
The EWS/ATF1 fusion protein contains a dispersed activation domain that functions directly. Oncogene . 1998; 16 (12):1625–1631.Pan S., Ming K. Y., Dunn T. A., Li K. K. C., Lee K. A. W. The EWS/ATF1 fusion protein contains a dispersed activation domain that functions directly...
An EWS/ERG fusion with a truncated N-terminal domain of EWS in a Ewing's tumor. Int J Cancer. 1996 Jul 29;67(3):339-42Peter M, Mugneret F, Aurias A, et al. An EWS/ERG fusion with a truncated N-terminal domain of EWS in a Ewing's tumor. Int J Cancer 1996;67:339-3...
It is one of the FET (FUS, EWS and TAF15) family of RNA binding proteins that contain an intrinsically disordered, low-complexity N-terminal domain. The FET family proteins are prone to chromosomal translocations, often fusing their low-complexity domain with a transcription factor derived DNA-...