Publications

Found 2717 results
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Dubiella, C., Pinch, B. J., Koikawa, K., Zaidman, D., Poon, E., Manz, T. D., Nabet, B., He, S., Resnick, E., Rogel, A., Langer, E. M., Daniel, C. J., Seo, H. - S., Chen, Y., Adelmant, G., Sharifzadeh, S., Ficarro, S. B., Jamin, Y., da Costa, B. Martins, Zimmerman, M. W., Lian, X., Kibe, S., Kozono, S., Doctor, Z. M., Browne, C. M., Yang, A., Stoler-Barak, L., Shah, R. B., Vangos, N. E., Geffken, E. A., Oren, R., Koide, E., Sidi, S., Shulman, Z., Wang, C., Marto, J. A., Dhe-Paganon, S., Look, T., Zhou, X. Zhen, Lu, K. Ping, Sears, R. C., Chesler, L., Gray, N. S., and London, N. (2021) Sulfopin is a covalent inhibitor of Pin1 that blocks Myc-driven tumors in vivo. Nat Chem Biol. 10.1038/s41589-021-00786-7
Duan, X., Sarangi, P., Liu, X., Rangi, G. K., Zhao, X., and Ye, H. (2009) Structural and functional insights into the roles of the Mms21 subunit of the Smc5/6 complex. Mol Cell. 35, 657-68
Duan, X., and Ye, H. (2009) Purification, crystallization and preliminary X-ray crystallographic studies of the complex between Smc5 and the SUMO E3 ligase Mms21. Acta Crystallogr Sect F Struct Biol Cryst Commun. 65, 849-52
Du, J., Johnson, L. M., Groth, M., Feng, S., Hale, C. J., Li, S., Vashisht, A. A., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2014) Mechanism of DNA methylation-directed histone methylation by KRYPTONITE. Mol Cell. 55, 495-504
Du, J., Zhong, X., Bernatavichute, Y. V., Stroud, H., Feng, S., Caro, E., Vashisht, A. A., Terragni, J., Chin, H. Gyeong, Tu, A., Hetzel, J., Wohlschlegel, J. A., Pradhan, S., Patel, D. J., and Jacobsen, S. E. (2012) Dual binding of chromomethylase domains to H3K9me2-containing nucleosomes directs DNA methylation in plants. Cell. 151, 167-80
Du, J., Kelly, A. E., Funabiki, H., and Patel, D. J. (2012) Structural basis for recognition of H3T3ph and Smac/DIABLO N-terminal peptides by human Survivin. Structure. 20, 185-95
Draheim, K. M., Li, X., Zhang, R., Fisher, O. S., Villari, G., Boggon, T. J., and Calderwood, D. A. (2015) CCM2-CCM3 interaction stabilizes their protein expression and permits endothelial network formation. J Cell Biol. 208, 987-1001
Draganova, E. B., Wang, H., Wu, M., Liao, S., Vu, A., Del Pino, G. L. Gonzalez, Z Zhou, H., Roller, R. J., and Heldwein, E. E. (2024) The universal suppressor mutation restores membrane budding defects in the HSV-1 nuclear egress complex by stabilizing the oligomeric lattice. PLoS Pathog. 20, e1011936
Dowling, D. P., Gantt, S. L., Gattis, S. G., Fierke, C. A., and Christianson, D. W. (2008) Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors. Biochemistry. 47, 13554-63
Dowling, D. P., Ilies, M., Olszewski, K. L., Portugal, S., Mota, M. M., Llinás, M., and Christianson, D. W. (2010) Crystal structure of arginase from Plasmodium falciparum and implications for L-arginine depletion in malarial infection . Biochemistry. 49, 5600-8
Dowling, D. P., Gattis, S. G., Fierke, C. A., and Christianson, D. W. (2010) Structures of metal-substituted human histone deacetylase 8 provide mechanistic inferences on biological function . Biochemistry. 49, 5048-56
Dowling, D. P., Bruender, N. A., Young, A. P., McCarty, R. M., Bandarian, V., and Drennan, C. L. (2014) Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism. Nat Chem Biol. 10, 106-12
Dowling, D. P., Kung, Y., Croft, A. K., Taghizadeh, K., Kelly, W. L., Walsh, C. T., and Drennan, C. L. (2016) Structural elements of an NRPS cyclization domain and its intermodule docking domain. Proc Natl Acad Sci U S A. 113, 12432-12437
Dowling, D. P., Miles, Z. D., Köhrer, C., Maiocco, S. J., Elliott, S. J., Bandarian, V., and Drennan, C. L. (2016) Molecular basis of cobalamin-dependent RNA modification. Nucleic Acids Res. 44, 9965-9976
Dow, B. A., Sukumar, N., Matos, J. O., Choi, M., Schulte, A., Tatulian, S. A., and Davidson, V. L. (2014) The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site. Arch Biochem Biophys. 550-551, 20-7
Dove, K. K., Olszewski, J. L., Martino, L., Duda, D. M., Wu, X. S., Miller, D. J., Reiter, K. H., Rittinger, K., Schulman, B. A., and Klevit, R. E. (2017) Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1.. Structure. 25, 890-900.e5
Doud, M. B., Koksal, A. C., Mi, L. - Z., Song, G., Lu, C., and Springer, T. A. (2012) Unexpected fold in the circumsporozoite protein target of malaria vaccines. Proc Natl Acad Sci U S A. 109, 7817-22
Dong, G., Medkova, M., Novick, P., and Reinisch, K. M. (2007) A catalytic coiled coil: structural insights into the activation of the Rab GTPase Sec4p by Sec2p. Mol Cell. 25, 455-62
Dong, C., Chen, S. - J., Melnykov, A., Weirich, S., Sun, K., Jeltsch, A., Varshavsky, A., and Min, J. (2020) Recognition of nonproline N-terminal residues by the Pro/N-degron pathway. Proc Natl Acad Sci U S A. 117, 14158-14167
Dong, C., Liu, Y., Lyu, T. - J., Beldar, S., Lamb, K. N., Tempel, W., Li, Y., Li, Z., James, L. I., Qin, S., Wang, Y., and Min, J. (2020) Structural Basis for the Binding Selectivity of Human CDY Chromodomains. Cell Chem Biol. 10.1016/j.chembiol.2020.05.007
Dong, G., Hutagalung, A. H., Fu, C., Novick, P., and Reinisch, K. M. (2005) The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat Struct Mol Biol. 12, 1094-100
Dong, G., Wearsch, P. A., Peaper, D. R., Cresswell, P., and Reinisch, K. M. (2009) Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity. 30, 21-32
Dong, C., Mao, Y., Tempel, W., Qin, S., Li, L., Loppnau, P., Huang, R., and Min, J. (2015) Structural basis for substrate recognition by the human N-terminal methyltransferase 1. Genes Dev. 29, 2343-8
Dong, C., Zhang, H., Li, L., Tempel, W., Loppnau, P., and Min, J. (2018) Molecular basis of GID4-mediated recognition of degrons for the Pro/N-end rule pathway. Nat Chem Biol. 14, 466-473
Dong, N., Zhu, Y., Lu, Q., Hu, L., Zheng, Y., and Shao, F. (2012) Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses. Cell. 150, 1029-41

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