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1. Tan M, Peng C, Anderson KA, Chhoy P, Xie Z, Dai L, Park J, Chen Y, Huang H, Zhang Y, Ro J, Wagner GR, Green MF, Madsen AS, Schmiesing J, Peterson BS, Xu G, Ilkayeva OR, Muehlbauer MJ, Braulke T, Mühlhausen C, Backos DS, Olsen CA, McGuire PJ, Pletcher SD, Lombard DB, Hirschey MD, Zhao Y. Lysine Glutarylation Is a Protein Posttranslational Modification Regulated by SIRT5. Cell Metab 2014; 19(4):605-17
2. Dai L, Peng C, Montellier E, Lu Z, Chen Y, Ishii H, Debernardi A, Buchou T, Rousseaux S, Jin F, Sabari BR, Deng Z, Allis CD, Ren B, Khochbin S, Zhao Y. Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark. Nat Chem Biol 2014; doi: 10.1038
3. Park, J., Chen, Y., Tishkoff, D. X., Peng, C., Tan, M., Dai, L., Xie, Z., Zhang, Y., Zwaans, B. M., Skinner, M. E., Lombard, D. B., and Zhao, Y. SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways. Mol Cell 2013; 50, 919-930
4. Qiang, L., Wang, L., Kon, N., Zhao, W., Lee, S., Zhang, Y., Rosenbaum, M., Zhao, Y., Gu, W., Farmer, S. R., and Accili, D. Brown remodeling of white adipose tissue by SirT1-dependent deacetylation of Ppargamma. Cell 2012; 150, 620-632
5. Li, T., Kon, N., Jiang, L., Tan, M., Ludwig, T., Zhao, Y., Baer, R., and GU, W. Tumor suppression in the absence of p53-mediated cell-cycle arrest, apoptosis, and senescence. Cell 2012; 149, 1269-1283
6. Choi, M. C., Cohen, T. J., Barrientos, T., Wang, B., Li, M., Simmons, B. J., Yang, J. S., Cox, G. A., Zhao, Y., and Yao, T. P. A direct HDAC4-MAP kinase crosstalk activates muscle atrophy program. Mol cell 2012; 47, 122-132
7. Chen, Y., Zhao, W., Yang, J. S., Cheng, Z., Luo, H., Lu, Z., Tan, M., Gu, W., and Zhao, Y. Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways. Mol Cell Proteomics 2012; 11, 1048-1062
8. Peng, C., Lu, Z., Xie, Z., Cheng, Z., Chen, Y., Tan, M., Luo, H., Zhang, Y., He, W., Yang, K., Zwaans, B. M., Tishkoff, D., Ho, L., Lombard, D., He, T. C., Dai, J., Verdin, E., Ye, Y., and Zhao, Y. The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics 2011; 10, M111 012658
9. Tan, M., Luo,H., Lee, S., Jin, F., Yang, J.-S., Montellier, E., Buchou,T., Cheng, Z., Rousseaux, S., Rajagopal, N., Lu, Z., Ye, Z., Zhu, Q., Wysocka, J., Ye, Y., Khochbin, S., Ren, B., Zhao, Y., Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 2011; 146, 1016-1028
10. Lu, J., Lin, Y., Sheu, J., Wu, J., Lee, F., Chen, Y., Lin, M., Chiang, F., Tai, T., Berger, S.L., Zhao, Y., Tsai, K., Zhu, H., Chuang, L., Boeke, J.D., A protein acetylation-phosphorylation signaling cascade coordinates growth and lifespan. Cell 2011; 146, 969-979
11. Zhang, Z., Tan, M., Xie, Z., Dai, L., Chen, Y., and Zhao, Y., Identification of lysine succinylation as a new post-translational modification. Nature Chem Biol 2011; 7(1): p. 58-63
12. Bajpai, R., Chen, D.A., Rada-Iglesias, A., Zhang, J., Xiong, Y., Helms, J., Chang, C.P., Zhao, Y., Swigut, T., and Wysocka, J., CHD7 cooperates with PBAF to control multipotent neural crest formation. Nature 2010; 463: p.958-62
13. Chen, Y., Chen, W., Cobb, M.H. and Zhao, Y., PTMap--a sequence alignment software for unrestricted, accurate, and full-spectrum identification of post-translational modification sites. Proc Natl Acad Sci USA 2009; 106(3): p. 761-6
14. Cheng, Z., Tang, Y., Chen, Y., Kim, S., Liu, H., Li, S.S., Gu, W. and Zhao, Y., Molecular characterization of propionyllysines in non-histone proteins. Mol Cell Proteomics 2009; 8(1): p. 45-52
15. Lin, Y.Y., Lu, J.Y., Zhang, J., Walter, W., Dang, W., Wan, J., Tao, S.C., Qian, J., Zhao, Y., Boeke, J.D., Berger, S.L. and Zhu, H., Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis. Cell 2009; 136(6): p. 1073-84
16. Peng, J.C., Valouev, A., Swigut, T., Zhang, J., Zhao, Y., Sidow, A. and Wysocka, J., Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target gene occupancy in pluripotent cells. Cell 2009; 139(7): p. 1290-302
17. Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C.F., Grishin, N.V. and Zhao, Y., Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics 2009; 8(2): p. 215-25