Publications

Unciuleac, M. - C., Goldgur, Y., and Shuman, S. (2019) Structures of ATP-bound DNA ligase D in a closed domain conformation reveal a network of amino acid and metal contacts to the ATP phosphates. J Biol Chem. 10.1074/jbc.RA119.007445
Braffman, N. R., Piscotta, F. J., Hauver, J., Campbell, E. A., A Link, J., and Darst, S. A. (2019) Structural mechanism of transcription inhibition by lasso peptides microcin J25 and capistruin. Proc Natl Acad Sci U S A. 116, 1273-1278
Clancy-Thompson, E., Devlin, C. A., Tyler, P. M., Servos, M. M., Ali, L. R., Ventre, K. S., M Bhuiyan, A., Bruck, P. T., Birnbaum, M. E., and Dougan, S. K. (2018) Altered Binding of Tumor Antigenic Peptides to MHC Class I Affects CD8 T Cell-Effector Responses. Cancer Immunol Res. 6, 1524-1536
Jha, V., and Ling, H. (2018) 2.0 Å resolution crystal structure of human polκ reveals a new catalytic function of N-clasp in DNA replication.. Sci Rep. 8, 15125
Porter, N. J., Shen, S., Barinka, C., Kozikowski, A. P., and Christianson, D. W. (2018) Molecular Basis for the Selective Inhibition of Histone Deacetylase 6 by a Mercaptoacetamide Inhibitor. ACS Med Chem Lett. 9, 1301-1305
Banerjee, A., Ghosh, S., Goldgur, Y., and Shuman, S. (2018) Structure and two-metal mechanism of fungal tRNA ligase. Nucleic Acids Res. 10.1093/nar/gky1275
Mondal, S., Jacoby, G., Sawaya, M. R., Arnon, Z. A., Adler-Abramovich, L., Rehak, P., Vuković, L., Shimon, L. J. W., Král, P., Beck, R., and Gazit, E. (2018) Transition of metastable cross-α crystals into cross-β fibrils by β-turn flipping.. J Am Chem Soc. 10.1021/jacs.8b10289
Novikova, I. V., Sharma, N., Moser, T., Sontag, R., Liu, Y., Collazo, M. J., Cascio, D., Shokuhfar, T., Hellmann, H., Knoblauch, M., and Evans, J. E. (2018) Protein structural biology using cell-free platform from wheat germ. Adv Struct Chem Imaging. 4, 13
Lv, Z., Yuan, L., Atkison, J. H., Williams, K. M., Vega, R., E Sessions, H., Divlianska, D. B., Davies, C., Chen, Y., and Olsen, S. K. (2018) Molecular mechanism of a covalent allosteric inhibitor of SUMO E1 activating enzyme. Nat Commun. 9, 5145
Melnikov, S. V., Khabibullina, N. F., Mairhofer, E., Vargas-Rodriguez, O., Reynolds, N. M., Micura, R., Söll, D., and Polikanov, Y. S. (2018) Mechanistic insights into the slow peptide bond formation with D-amino acids in the ribosomal active site. Nucleic Acids Res. 10.1093/nar/gky1211
Ji, T., Zhang, C., Zheng, L., Dunaway-Mariano, D., and Allen, K. N. (2018) Structural Basis of the Molecular Switch between Phosphatase and Mutase Functions of Human Phosphomannomutase 1 under Ischemic Conditions. Biochemistry. 57, 3480-3492
Oi, C., Treado, J. D., Levine, Z. A., Lim, C. S., Knecht, K. M., Xiong, Y., O'Hern, C. S., and Regan, L. (2018) A threonine zipper that mediates protein-protein interactions: Structure and prediction. Protein Sci. 27, 1969-1977
Miller, B. R., and Kung, Y. (2018) Structural insight into substrate and product binding in an archaeal mevalonate kinase. PLoS One. 13, e0208419
Omattage, N. S., Deng, Z., Pinkner, J. S., Dodson, K. W., Almqvist, F., Yuan, P., and Hultgren, S. J. (2018) Structural basis for usher activation and intramolecular subunit transfer in P pilus biogenesis in Escherichia coli. Nat Microbiol. 10.1038/s41564-018-0255-y
Martin, S. E. S., Tan, Z. - W., Itkonen, H. M., Duveau, D. Y., Paulo, J. A., Janetzko, J., Boutz, P. L., Törk, L., Moss, F. A., Thomas, C. J., Gygi, S. P., Lazarus, M. B., and Walker, S. (2018) Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. J Am Chem Soc. 10.1021/jacs.8b07328
Liou, G., Chiang, Y. - C., Wang, Y., and Weng, J. - K. (2018) Mechanistic basis for the evolution of chalcone synthase catalytic cysteine reactivity in land plants. J Biol Chem. 10.1074/jbc.RA118.005695
Ragwan, E. R., Arai, E., and Kung, Y. (2018) New Crystallographic Snapshots of Large Domain Movements in Bacterial 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase. Biochemistry. 57, 5715-5725
Stiegler, A. L., and Boggon, T. J. (2018) The N-Terminal GTPase Domain of p190RhoGAP Proteins Is a PseudoGTPase. Structure. 10.1016/j.str.2018.07.015
Santiago, Ada Silva, Couñago, R. M., Ramos, P. Zonzini, Godoi, P. H. C., Massirer, K. B., Gileadi, O., and Elkins, J. M. (2018) Structural Analysis of Inhibitor Binding to CAMKK1 Identifies Features Necessary for Design of Specific Inhibitors. Sci Rep. 8, 14800
Pourfarjam, Y., Ventura, J., Kurinov, I., Cho, A., Moss, J., and Kim, I. - K. (2018) Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. J Biol Chem. 293, 12350-12359
Sukumar, N., Liu, S., Li, W., Mathews, F. S., Mitra, B., and Kandavelu, P. (2018) Structure of the monotopic membrane protein (S)-mandelate dehydrogenase at 2.2Å resolution.. Biochimie. 10.1016/j.biochi.2018.07.017
Gorelik, M., Manczyk, N., Pavlenco, A., Kurinov, I., Sidhu, S. S., and Sicheri, F. (2018) A Structure-Based Strategy for Engineering Selective Ubiquitin Variant Inhibitors of Skp1-Cul1-F-Box Ubiquitin Ligases. Structure. 10.1016/j.str.2018.06.004
Iglesias, N., Currie, M. A., Jih, G., Paulo, J. A., Siuti, N., Kalocsay, M., Gygi, S. P., and Moazed, D. (2018) Automethylation-induced conformational switch in Clr4 (Suv39h) maintains epigenetic stability. Nature. 560, 504-508
Yang, Y., Kang, D., Nguyen, L. A., Smithline, Z. B., Pannecouque, C., Zhan, P., Liu, X., and Steitz, T. A. (2018) Structural basis for potent and broad inhibition of HIV-1 RT by thiophene[3,2-]pyrimidine non-nucleoside inhibitors. Elife. 10.7554/eLife.36340
Porter, N. J., Osko, J. D., Diedrich, D., Kurz, T., Hooker, J. M., Hansen, F. K., and Christianson, D. W. (2018) Histone Deacetylase 6-Selective Inhibitors and the Influence of Capping Groups on Hydroxamate-Zinc Denticity. J Med Chem. 10.1021/acs.jmedchem.8b01013
Lau, Y. - T. K., Baytshtok, V., Howard, T. A., Fiala, B. M., Johnson, J. L. M., Carter, L. P., Baker, D., Lima, C. D., and Bahl, C. D. (2018) Discovery and engineering of enhanced SUMO protease enzymes. J Biol Chem. 293, 13224-13233
Nowak, R. P., DeAngelo, S. L., Buckley, D., He, Z., Donovan, K. A., An, J., Safaee, N., Jedrychowski, M. P., Ponthier, C. M., Ishoey, M., Zhang, T., Mancias, J. D., Gray, N. S., Bradner, J. E., and Fischer, E. S. (2018) Plasticity in binding confers selectivity in ligand-induced protein degradation. Nat Chem Biol. 10.1038/s41589-018-0055-y
Knappenberger, A. John, Reiss, C. Wetheringt, and Strobel, S. A. (2018) Structures of two aptamers with differing ligand specificity reveal ruggedness in the functional landscape of RNA. Elife. 10.7554/eLife.36381
Sui, X., Farquhar, E. R., Hill, H. E., von Lintig, J., Shi, W., and Kiser, P. D. (2018) Preparation and characterization of metal-substituted carotenoid cleavage oxygenases. J Biol Inorg Chem. 23, 887-901
Gulati, S., Jin, H., Masuho, I., Orban, T., Cai, Y., Pardon, E., Martemyanov, K. A., Kiser, P. D., Stewart, P. L., Ford, C. P., Steyaert, J., and Palczewski, K. (2018) Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor. Nat Commun. 9, 1996
Kearney, C., Olenginski, L. T., Hirn, T. D., Fowler, G. D., Tariq, D., Brewer, S. H., and Phillips-Piro, C. M. (2018) Exploring local solvation environments of a heme protein using the spectroscopic reporter 4-cyano-l-phenylalanine. RSC Adv. 8, 13503-13512
Guenther, E. L., Cao, Q., Trinh, H., Lu, J., Sawaya, M. R., Cascio, D., Boyer, D. R., Rodriguez, J. A., Hughes, M. P., and Eisenberg, D. S. (2018) Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation. Nat Struct Mol Biol. 10.1038/s41594-018-0064-2
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
Zubcevic, L., Le, S., Yang, H., and Lee, S. - Y. (2018) Conformational plasticity in the selectivity filter of the TRPV2 ion channel. Nat Struct Mol Biol. 25, 405-415
Choi, E. H., Suh, S., Sander, C. L., Hernandez, C. J. Ortiz, Bulman, E. R., Khadka, N., Dong, Z., Shi, W., Palczewski, K., and Kiser, P. D. (2018) Insights into the pathogenesis of dominant retinitis pigmentosa associated with a D477G mutation in RPE65. Hum Mol Genet. 10.1093/hmg/ddy128

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