Publications

Found 1285 results
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Journal Article
Park, E., Kim, N., Ficarro, S. B., Zhang, Y., Lee, B. Il, Cho, A., Kim, K., Park, A. K. J., Park, W. - Y., Murray, B., Meyerson, M., Beroukhim, R., Marto, J. A., Cho, J., and Eck, M. J. (2015) Structure and mechanism of activity-based inhibition of the EGF receptor by Mig6. Nat Struct Mol Biol. 22, 703-711
Morrison, E., Kantz, A., Gassner, G. T., and Sazinsky, M. H. (2013) Structure and mechanism of styrene monooxygenase reductase: new insight into the FAD-transfer reaction. Biochemistry. 52, 6063-75
Kattke, M. D., Gosschalk, J. E., Martinez, O. E., Kumar, G., Gale, R. T., Cascio, D., Sawaya, M. R., Philips, M., Brown, E. D., and Clubb, R. T. (2019) Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria. PLoS Pathog. 15, e1007723
Kattke, M. D., Gosschalk, J. E., Martinez, O. E., Kumar, G., Gale, R. T., Cascio, D., Sawaya, M. R., Philips, M., Brown, E. D., and Clubb, R. T. (2019) Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria. PLoS Pathog. 15, e1007723
Köksal, M., Hu, H., Coates, R. M., Peters, R. J., and Christianson, D. W. (2011) Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase. Nat Chem Biol. 7, 431-3
Dieck, C. L., Tzoneva, G., Forouhar, F., Carpenter, Z., Ambesi-Impiombato, A., Sanchez-Martin, M., Kirschner-Schwabe, R., Lew, S., Seetharaman, J., Tong, L., and Ferrando, A. A. (2018) Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. Cancer Cell. 34, 136-147.e6
Wang, Q., Kaan, H. Yi Kristal, Hooda, R. Noordin, Goh, S. Lin, and Sondermann, H. (2008) Structure and plasticity of Endophilin and Sorting Nexin 9. Structure. 16, 1574-87
Schaefer, K., Owens, T. W., Page, J. E., Santiago, M., Kahne, D., and Walker, S. (2020) Structure and reconstitution of a hydrolase complex that may release peptidoglycan from the membrane after polymerization. Nat Microbiol. 10.1038/s41564-020-00808-5
Yang, T., Liu, Q., Kloss, B., Bruni, R., Kalathur, R. C., Guo, Y., Kloppmann, E., Rost, B., Colecraft, H. M., and Hendrickson, W. A. (2014) Structure and selectivity in bestrophin ion channels. Science. 346, 355-9
Yang, T., Liu, Q., Kloss, B., Bruni, R., Kalathur, R. C., Guo, Y., Kloppmann, E., Rost, B., Colecraft, H. M., and Hendrickson, W. A. (2014) Structure and selectivity in bestrophin ion channels. Science. 346, 355-9
Yang, T., Liu, Q., Kloss, B., Bruni, R., Kalathur, R. C., Guo, Y., Kloppmann, E., Rost, B., Colecraft, H. M., and Hendrickson, W. A. (2014) Structure and selectivity in bestrophin ion channels. Science. 346, 355-9
Sui, X., Weitz, A. C., Farquhar, E. R., Badiee, M., Banerjee, S., von Lintig, J., Tochtrop, G. P., Palczewski, K., Hendrich, M. P., and Kiser, P. D. (2017) Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center. Biochemistry. 56, 2836-2852
Hall, D., Giaimo, B. Daniele, Park, S. - S., Hemmer, W., Friedrich, T., Ferrante, F., Bartkuhn, M., Yuan, Z., Oswald, F., Borggrefe, T., Rual, J. - F., and Kovall, R. A. (2022) The structure, binding and function of a Notch transcription complex involving RBPJ and the epigenetic reader protein L3MBTL3.. Nucleic Acids Res. 50, 13083-13099
Strunk, R. J., Piemonte, K. M., Petersen, N. M., Koutsioulis, D., Bouriotis, V., Perry, K., and Cole, K. E. (2014) Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis. Acta Crystallogr F Struct Biol Commun. 70, 156-9
York, N. J., Lockart, M. M., Sardar, S., Khadka, N., Shi, W., Stenkamp, R. E., Zhang, J., Kiser, P. D., and Pierce, B. S. (2021) Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center. J Biol Chem. 10.1016/j.jbc.2021.100492
York, N. J., Lockart, M. M., Sardar, S., Khadka, N., Shi, W., Stenkamp, R. E., Zhang, J., Kiser, P. D., and Pierce, B. S. (2021) Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center. J Biol Chem. 10.1016/j.jbc.2021.100492
Cramer, E. R., Starcovic, S. A., Avey, R. M., Kaya, A. I., and Robart, A. R. (2023) Structure of a 10-23 deoxyribozyme exhibiting a homodimer conformation. Commun Chem. 6, 119
Thompson, M. C., Crowley, C. S., Kopstein, J., Bobik, T. A., and Yeates, T. O. (2014) Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor. Acta Crystallogr F Struct Biol Commun. 70, 1584-90
Lee, K., Gu, S., Jin, L., Le, T. Tuc Nghi, Cheng, L. W., Strotmeier, J., Kruel, A. Magdalena, Yao, G., Perry, K., Rummel, A., and Jin, R. (2013) Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity. PLoS Pathog. 9, e1003690
Klein, D. E., Choi, J. L., and Harrison, S. C. (2013) Structure of a dengue virus envelope protein late-stage fusion intermediate. J Virol. 87, 2287-93
Bale, J. B., Park, R. U., Liu, Y., Gonen, S., Gonen, T., Cascio, D., King, N. P., Yeates, T. O., and Baker, D. (2015) Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression. Protein Sci. 24, 1695-701
Schlieker, C., Weihofen, W. A., Frijns, E., Kattenhorn, L. M., Gaudet, R., and Ploegh, H. L. (2007) Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes. Mol Cell. 25, 677-87
Toms, A. V., Deshpande, A., McNally, R., Jeong, Y., Rogers, J. M., Kim, C. Un, Gruner, S. M., Ficarro, S. B., Marto, J. A., Sattler, M., Griffin, J. D., and Eck, M. J. (2013) Structure of a pseudokinase-domain switch that controls oncogenic activation of Jak kinases. Nat Struct Mol Biol. 20, 1221-3
AhYoung, A. P., Koehl, A., Vizcarra, C. L., Cascio, D., and Egea, P. F. (2016) Structure of a putative ClpS N-end rule adaptor protein from the malaria pathogen Plasmodium falciparum. Protein Sci. 25, 689-701
Benavides, B. S., Valandro, S., Cioloboc, D., Taylor, A. B., Schanze, K. S., and Kurtz, D. M. (2020) Structure of a Zinc Porphyrin-Substituted Bacterioferritin and Photophysical Properties of Iron Reduction. Biochemistry. 59, 1618-1629

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