PUBLICATIONS:

Nathan Wlodarchak & Yongna Xing (2016) PP2A as a master regulator of the cell cycle, Critical Reviews in Biochemistry and Molecular Biology, 51:3, 162-184. PDF

Guo F*, Wan L*, Zheng A, Stanevich V, Chen H, Wei Y, Satyshur KA, Shen M, Lee W, Kang Y* and Xing Y*. (2014) Structural Insights into the Tumor-Promoting Function of the MTDH-SND1 Complex. Cell Report, in press. [The first two authors contributed equally to this work.] PDF

Kim H, Guo F, Brahma S, Xing Y, and Burkard ME (2014) Centralspindlin assembly and two phosphorylations on MgcRacGAP by Polo-like kinase 1 initiate Ect2 binding in early cytokinesis. Cell Cycle, in press. PDF

Wan L, Lu X, Yuan S, Wei Y, Guo F, Shen M, Yuan M, Chakrabarti R, Hua Y, Smith HA, Blanco MA, Chekmareva M, Wu H, Bronson RT, Haffty BG, Xing Y, Kang Y. (2014) MTDH-SND1 Interaction Is Crucial for Expansion and Activity of Tumor-Initiating Cells in Diverse Oncogene- and Carcinogen-Induced Mammary Tumors. Cancer Cell, 14;26(1):92-105. PDF

Stanevich V, Zhang A, Guo F, Jiang L, Wlodarchak N, Xing Y. Mechanisms of the Scaffold Subunit in Facilitating Protein Phosphatase 2A Methylation. 2014 PLoS One. 9(1)e86955. PDF

Kotlo K, Xing Y, Lather S, Grillon JM, Johnson K, Skidgel RA, Solaro RJ, Danziger RS. (2014) PR65A Phosphorylation Regulates PP2A Complex Signaling. PLoS One. 9(1):e85000. PDF

Guo F, Stanevich V, Wlodarchak N, Sengupta R, Jiang L, Satyshur K A, Xing Y. Structural basis of PP2A activation by PTPA, an ATP-dependent activation chaperone. 2014 Cell Research. 24(2):190-203. PDF, Cover, Science Editor's Choice.

Wlodarchak N, Guo F, Satyshur K A, Jiang L, Jeffrey P D, Sun T, Stanevich V, Mumby M C, Xing Y. Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation. 2013 Cell Research. 23(7):931-46. PDF, Cover.

Jiang, L., Stanevich, V., Satyshur, K.A., Kong, M., Watkins, G.R., Wadzinski, B.E., Sengupta, R., and Xing Y. (2013). Structural basis of protein phosphatase 2A stable latency. Nat Commun 4, 1699. PDF

Xing Y, Nukaya, M., Satyshur, K.A., Jiang, L., Stanevich, V., Korkmaz, E.N., Burdette, L., Kennedy, G.D., Cui, Q., and Bradfield, C.A. (2012). Identification of the Ah-receptor structural determinants for ligand preferences. Toxicol Sci 129, 86-97. PDF, Cover.

Mezrich, J.D., Nguyen, L.P., Kennedy, G., Nukaya, M., Fechner, J.H., Zhang, X., Xing Y, and Bradfield, C.A. (2012). SU5416, a VEGF receptor inhibitor and ligand of the AHR, represents a new alternative for immunomodulation. PLoS One 7, e44547. PDF

Stanevich, V., Jiang, L., Satyshur, K.A., Li, Y., Jeffrey, P.D., Li, Z., Menden, P., Semmelhack, M.F., and Xing Y. (2011). The structural basis for tight control of PP2A methylation and function by LCMT-1. Molecular cell 41, 331-342. PDF

Dickerson, SJ, Xing Y, Robinson AR, Seaman WT, Gruffat H, and Kenney SC, (2009) Methylation-dependent binding of the Epstein-Barr virus BZLF1 protein to viral promoters. PLOS Pathogen, Mar; 5(3):e1000356. PDF

Yongna's publications prior to independence:

Xing Y, Li, Z., Chen, Y., Stock, J. B., Jeffrey, P. D., and Shi, Y. Structural Mechanism of Demethylation and Inactivation of Protein Phosphatase 2A. Cell, 133: 154-163, 2008. PDF

Chen, Y., Xu, Y., Bao, Q., Xing Y, Li, Z., Lin, Z., Stock, J. B., Jeffrey, P. D., and Shi Y. Structural and Biochemical Insights Into the Regulation of Protein Phosphatase 2A by Small T Antigen of SV40. Nat. Struct. Mol. Biol., 14: 527-534, 2007. PDF

Xu, Y., Xing Y, Chen, Y., Chao, Y., Lin, Z., Fan, E., Yu, J. W., Strack, S., Jeffrey, P. D., and Shi Y. Structure of the Protein Phosphatase 2A Holoenzyme. Cell, 127: 1239-1251, 2006. [The first four authors contributed equally to this work.] PDF

Xing Y, Xu, Y., Chen, Y., Jeffrey, P. D., Chao, Y., Lin, Z., Li, Z., Strack, S., Stock, J. B., and Shi, Y. Structure of Protein Phosphatase 2A Core Enzyme Bound to Tumor-Inducing Toxins. Cell, 127: 341-353, 2006. [The first three authors contributed equally to this work.] PDF

Chao, Y., Xing Y, Chen, Y., Xu, Y., Lin, Z., Li, Z., Jeffrey, P. D., Stock, J. B., and Shi, Y. Structure and Mechanism of the Phosphotyrosyl Phosphatase Activator. Mol. Cell, 23: 535-546, 2006. PDF

Bernard, M. P., Lin, W., Myers, R., Cao, D., Xing Y, and Moyle, W. R. Crosslinked Bifunctional Gonadotropin Analogs with Reduced Efficacy. Mol. Cell. Endocrinol., 233: 25-31, 2005. PDF

Xing Y, Myers, R. V., Cao, D., Lin, W., Jiang, M., Bernard, M. P., and Moyle, W. R. Glycoprotein Hormone Assembly in the Endoplasmic Reticulum. I. The Glycosylated End of Human a-Subunit Loop 2 Is Threaded through a b-Subunit Hole. J. Biol. Chem., 279: 35426-35436, 2004. PDF

Xing Y, Myers, R. V., Cao, D., Lin, W., Jiang, M., Bernard, M. P., and Moyle, W. R. Glycoprotein Hormone Assembly in the Endoplasmic Reticulum. II. Multiple Roles of a Redox Sensitive b-Subunit Disulfide Switch. J. Biol. Chem., 279: 35437-35448, 2004. PDF

Xing Y, Myers, R. V., Cao, D., Lin, W., Jiang, M., Bernard, M. P., and Moyle, W. R. Glycoprotein Hormone Assembly in the Endoplasmic Reticulum. III. The Seatbelt and Its Latch Site Determine the Assembly Pathway. J. Biol. Chem., 279: 35449-35457, 2004. PDF

Xing Y, Myers, R. V., Cao, D., Lin, W., Jiang, M., Bernard, M. P., and Moyle, W. R. Glycoprotein Hormone Assembly in the Endoplasmic Reticulum. IV. Probable Mechanism of Subunit Docking and Completion of Assembly. J. Biol. Chem., 279: 35458-35468, 2004. PDF

Xing Y, Lin, W., Jiang, M., Cao, D., Myers, R. V., Bernard, M. P., and Moyle, W. R. Use of Protein Knobs to Characterize the Position of Conserved a-Subunit Regions in Lutropin Receptor Complexes. J. Biol. Chem., 279: 44427-44437, 2004. PDF

Moyle, W. R., Xing Y, Lin, W., Cao, D., Myers, R. V., Kerrigan, J. E., and Bernard, M. P. Model of Glycoprotein Hormone Receptor Ligand Binding and Signaling. J. Biol. Chem., 279: 44442-44459, 2004. PDF

Bernard, M. P., Lin, W., Cao, D., Myers, R. V., Xing Y, and Moyle, W. R. Only a Portion of the Small Seatbelt Loop in Human Choriogonadotropin Appears Capable of Contacting the Lutropin Receptor. J. Biol. Chem., 279: 44438-44441, 2004. PDF

Xing Y, and Moyle, W. R. Efficient Preparation of Glycoprotein Hormones Lacking an a-Subunit Oligosaccharide. Biochem. Biophys. Res. Commun., 303: 201-205, 2003. PDF

Xing Y, Williams, C., Campbell, R. K., Cook, S., Knoppers, M., Addona, T., Altarocca, V., and Moyle, W. R. Threading of a Glycosylated Protein Loop through a Protein Hole: Implications for Combination of Human Chorionic Gonadotropin Subunits. Protein Sci., 10: 226-235, 2001. PDF

Xing Y, Lin, W., Jiang, M., Myers, R. V., Cao, D., Bernard, M. P., and Moyle, W. R. Alternatively Folded Choriogonadotropin Analogs. Implications for Hormone Folding and Biological Activity. J. Biol. Chem., 276: 46953-46960, 2001. PDF