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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
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
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
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
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
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., 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., 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., 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., 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
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
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
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
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., 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., 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
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
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
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
Duda, D. M., Olszewski, J. L., Tron, A. E., Hammel, M., Lambert, L. J., M Waddell, B., Mittag, T., DeCaprio, J. A., and Schulman, B. A. (2012) Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase through masking of its E2-binding surface. Mol Cell. 47, 371-82
Duda, D. M., Olszewski, J. L., Schuermann, J. P., Kurinov, I., Miller, D. J., Nourse, A., Alpi, A. F., and Schulman, B. A. (2013) Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism. Structure. 21, 1030-41
Dufrisne, M. Belcher, Petrou, V. I., Clarke, O. B., and Mancia, F. (2017) Structural basis for catalysis at the membrane-water interface. Biochim Biophys Acta Mol Cell Biol Lipids. 1862, 1368-1385
Dufrisne, M. Belcher, Jorge, C. D., Timóteo, C. G., Petrou, V. I., Ashraf, K. U., Banerjee, S., Clarke, O. B., Santos, H., and Mancia, F. (2020) Structural and Functional Characterization of Phosphatidylinositol-Phosphate Biosynthesis in Mycobacteria. J Mol Biol. 10.1016/j.jmb.2020.04.028
Duggan, K. C., Hermanson, D. J., Musee, J., Prusakiewicz, J. J., Scheib, J. L., Carter, B. D., Banerjee, S., Oates, J. A., and Marnett, L. J. (2011) (R)-Profens are substrate-selective inhibitors of endocannabinoid oxygenation by COX-2. Nat Chem Biol. 7, 803-9
Dumitrescu, D. G., Gordon, E. M., Kovalyova, Y., Seminara, A. B., Duncan-Lowey, B., Forster, E. R., Zhou, W., Booth, C. J., Shen, A., Kranzusch, P. J., and Hatzios, S. K. (2022) A microbial transporter of the dietary antioxidant ergothioneine. Cell. 185, 4526-4540.e18

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