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个人简介

Education BS, Chemistry, University of Colorado at Denver MS, Chemistry, University of Michigan PhD, Chemistry, University of Michigan Fellow, Chemistry, University of Colorado, Denver School of Medicine

研究领域

The genome of every eukaryotic cell resides in complex with histone proteins to form chromatin. Though originally thought to just package the genome into the nucleus, chromatin structure is now recognized to play an active role in the regulation of all DNA templated processes in eukaryotes. Such regulation requires the spatial and temporal alteration of chromatin structure, which is mediated by the chemical modification of histones and DNA as well as by the action of a large number of chromatin associated cofactors. My lab is interested in deciphering mechanisms of chromatin structure modulation and how misregulation of these pathways is associated with disease. Specifically, our goal is to elucidate, on the molecular level, the details of how cofactors target nucleosomes, especially in response to histone modification, and how this leads to the regulation of genes. Such knowledge will enhance our fundamental understanding of chromatin biology as well as reveal the etiology of many human diseases with the aim of eventually aiding in the development of targeted therapeutics. We employ NMR spectroscopy, X-ray crystallography as well as a variety of other biophysical and biochemical techniques to approach these questions.

近期论文

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Xing, S., Li, F., Zeng, Z., Zhao, Y., Yu, S., Shan, Q., Li, Y., Phillips, F. C., Maina, P. K., Qi, H. H., Liu, C., Zhu, J., Pope, R. M., Musselman, C. A., Zeng, C., Peng, W. & Xue, H. H. (2016). Tcf1 and Lef1 transcription factors establish CD8(+) T cell identity through intrinsic HDAC activity.. Nature immunology, 17(6), 695-703. DOI: 10.1038/ni.3456. Musselman, C. A., Kutateladze, T. G. (2016). Preparation, Biochemical Analysis, and Structure Determination of Methyllysine Readers.. Methods in enzymology, 573, 345-62. DOI: 10.1016/bs.mie.2015.12.005. Tong, Q., Cui, G., Botuyan, M. V., Rothbart, S. B., Hayashi, R., Musselman, C. A., Singh, N., Appella, E., Strahl, B. D., Mer, G. & Kutateladze, T. G. (2015). Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1.. Structure (London, England : 1993), 23(2), 312-21. DOI: 10.1016/j.str.2014.11.013. Wang, C., Chen, Z., Hong, X., Ning, F., Liu, H., Zang, J., Yan, X., Kemp, J., Musselman, C., Kutateladze, T., Zhao, R., Jiang, C. & Zhang, G. (2014). The structural basis of urea-induced protein unfolding in ß-catenin. Acta Crystallogr D Biol Crystallogr, 70(11), 2840-7. DOI: 10.1107/S1399004714018094. Ezhov, R., Metzel, G., Mukhina, O., Musselman, C., Kutateladze, T., Gustafson, T. & Kutateladze, A. (2014). Photoactive Spatial Proximity Probes for Binding Pairs with Epigenetic Marks. J Photochem Photobiol A Chem, 290, 101-108. Musselman, C., Khorasanizadeh, S. & Kutateladze, T. (2014). Towards understanding methyllysine readout. Biochim Biophys Acta, 1839(8), 686-93. DOI: 10.1016/j.bbagrm.2014.04.001. Allen, H., Daze, K., Shimbo, T., Lai, A., Musselman, C., Sims, J., Wade, P., Hof, F. & Kutateladze, T. (2014). Inhibition of histone binding by supramolecular hosts.. Biochem J, 459(3), 505-12. DOI: 10.1042/BJ20140145. Musselman, C. A., Gibson, M. D., Hartwick, E. W., North, J. A., Gatchalian, J., Poirier, M. G. & Kutateladze, T. G. (2013). Binding of PHF1 Tudor to H3K36me3 enhances nucleosome accessibility. Nat Commun,(4), 2969.

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