Department of Pathological Physiology Faculty of Medicine Masaryk University Brno Kamenice 5 625 00 Brno Czech Republic

Joint Repair and Regeneration Orthopaedic Clinic University Hospital Brno and Faculty of Medicine Masaryk University Brno Brno Czech Republic

Zobrazit více v PubMed

Takahashi, K., & Yamanaka, S. (2006). Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors. Cell, 126, 663–676. DOI

Piskacek, M., Havelka, M., Jendruchova, K., Knight, A., & Keegan, L. P. (2019). The evolution of the 9aaTAD domain in Sp2 proteins: Inactivation with valines and intron reservoirs. Cellular and Molecular Life Sciences. https://doi.org/10.1007/s00018-019-03251-w PubMed DOI

Sandholzer, J., Hoeth, M., Piskacek, M., Mayer, H., & de Martin, R. (2007). A novel 9-amino-acid transactivation domain in the C-terminal part of Sox18. Biochemical and Biophysical Research Communications, 360, 370–374. DOI

Piskacek, M., Vasku, A., Hajek, R., & Knight, A. (2015). Shared structural features of the 9aaTAD family in complex with CBP. Molecular BioSystems, 11, 844–851. DOI

Hofrova, A., Lousa, P., Kubickova, M., Hritz, J., Otasevic, T., Repko, M., Knight, A., & Piskacek, M. (2021). Universal two-point interaction of mediator KIX with 9aaTAD activation domains. Journal of Cellular Biochemistry. https://doi.org/10.1002/jcb.30075 PubMed DOI

Haseeb, A., & Lefebvre, V. (2019). The SOXE transcription factors—SOX8, SOX9 and SOX10—share a bi-partite transactivation mechanism. Nucleic Acids Research. https://doi.org/10.1093/nar/gkz523 PubMed DOI PMC

Piskacek, M., Havelka, M., Rezacova, M., & Knight, A. (2016). The 9aaTAD transactivation domains: From Gal4 to p53. PLoS ONE, 11, e0162842. DOI

Teufel, D. P., Freund, S. M., Bycroft, M., & Fersht, A. R. (2007). Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. Proceedings of the National academy of Sciences of the United States of America, 104, 7009–7014. DOI

De Guzman, R. N., Goto, N. K., Dyson, H. J., & Wright, P. E. (2006). Structural basis for cooperative transcription factor binding to the CBP coactivator. Journal of Molecular Biology, 355, 1005–1013. DOI

Denis, C. M., Chitayat, S., Plevin, M. J., Wang, F., Thompson, P., Liu, S., Spencer, H. L., Ikura, M., LeBrun, D. P., & Smith, S. P. (2012). Structural basis of CBP/p300 recruitment in leukemia induction by E2A-PBX1. Blood, 120, 3968–3977. DOI

Piskacek, M., Havelka, M., Rezacova, M., & Knight, A. (2017). Gal4 activation domain 9aaTAD could be inactivated by adjacent mini-inhibitory domain and reactivated by distal re-activation domain. bioRxiv. https://doi.org/10.1101/110882

Lam, C. S., Mistri, T. K., Foo, Y. H., Sudhaharan, T., Gan, H. T., Rodda, D., Lim, L. H., Chou, C., Robson, P., Wohland, T., et al. (2012). DNA-dependent Oct4-Sox2 interaction and diffusion properties characteristic of the pluripotent cell state revealed by fluorescence spectroscopy. The Biochemical Journal, 448, 21–33. DOI

Adikusuma, F., Pederick, D., McAninch, D., Hughes, J., & Thomas, P. (2017). Functional equivalence of the SOX2 and SOX3 transcription factors in the developing mouse brain and testes. Genetics, 206, 1495–1503. DOI

Niwa, H., Nakamura, A., Urata, M., Shirae-Kurabayashi, M., Kuraku, S., Russell, S., & Ohtsuka, S. (2016). The evolutionally-conserved function of group B1 Sox family members confers the unique role of Sox2 in mouse ES cells. BMC Evolutionary Biology, 16, 1–12. DOI

Narayan, S., Bryant, G., Shah, S., Berrozpe, G., & Ptashne, M. (2017). OCT4 and SOX2 work as transcriptional activators in reprogramming human fibroblasts. Cell Reports, 20, 1585–1596. DOI

Lefebvre, V., Angelozzi, M., & Haseeb, A. (2019). SOX9 in cartilage development and disease. Current Opinion in Cell Biology, 61, 39–47. DOI

Myc 9aaTAD activation domain binds to mediator of transcription with superior high affinity