Covalent modifications of histone tails are highly correlated with different states of gene expression. Although the biological significance of many such modifications has been elucidated, the physiological role of Thr 11 phosphorylation on histone H3 (H3T11) has remained elusive.
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References
Di Croce, L. et al. EMBO J. 18, 6201–6210 (1999).
Bhaumik, S. R., Smith, E. & Shilatifard, A. Nature Struct. Mol. Biol. 14, 1008–1016 (2007).
Perissi, V. & Rosenfeld, M. G. Nature Rev. Mol. Cell Biol. 6, 542–554 (2005).
Villa, R. et al. Cancer Cell 11, 513–525 (2007).
Houben, A. et al. Biochim. Biophys. Acta 1769, 308–315 (2007).
Metzger, E. et al. Nature Cell Biol. 10, 53–60 (2008).
Metzger, E., Muller, J. M., Ferrari, S., Buettner, R. & Schule, R. EMBO J. 22, 270–280 (2003).
Wissmann, M. et al. Nature Cell Biol. 9, 347–353 (2007).
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K. & Jenuwein, T. Nature 410, 116–120 (2001).
Bannister, A. J. et al. Nature 410, 120–124 (2001).
Vicent, G. P. et al. Mol. Cell 24, 367–381 (2006).
Metivier, R. et al. Cell 115, 751–763 (2003).
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Croce, L., Shiekhattar, R. Thrilling transcription through threonine phosphorylation. Nat Cell Biol 10, 5–6 (2008). https://doi.org/10.1038/ncb0108-5
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DOI: https://doi.org/10.1038/ncb0108-5