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Oyala, P. H., Ravichandran, K. R., Funk, M. A., Stucky, P. A., Stich, T. A., Drennan, C. L., R Britt, D., and Stubbe, J. A. (2016) Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example. J Am Chem Soc. 138, 7951-64
Owens, T. W., Taylor, R. J., Pahil, K. S., Bertani, B. R., Ruiz, N., Kruse, A. C., and Kahne, D. (2019) Structural basis of unidirectional export of lipopolysaccharide to the cell surface. Nature. 567, 550-553
Ostrander, E. L., Larson, J. D., Schuermann, J. P., and Tanner, J. J. (2009) A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate. Biochemistry. 48, 951-9
Osterman, I. A., Khabibullina, N. F., Komarova, E. S., Kasatsky, P., Kartsev, V. G., Bogdanov, A. A., Dontsova, O. A., Konevega, A. L., Sergiev, P. V., and Polikanov, Y. S. (2017) Madumycin II inhibits peptide bond formation by forcing the peptidyl transferase center into an inactive state. Nucleic Acids Res. 10.1093/nar/gkx413
Osmundson, J., Montero-Diez, C., Westblade, L. F., Hochschild, A., and Darst, S. A. (2012) Promoter-specific transcription inhibition in Staphylococcus aureus by a phage protein. Cell. 151, 1005-16
Osko, J. D., Porter, N. J., Reddy, P. Adi Naraya, Xiao, Y. - C., Rokka, J., Jung, M., Hooker, J. M., Salvino, J. M., and Christianson, D. W. (2020) Exploring Structural Determinants of Inhibitor Affinity and Selectivity in Complexes with Histone Deacetylase 6. J Med Chem. 63, 295-308
Osko, J. D., and Christianson, D. W. (2019) Structural Basis of Catalysis and Inhibition of HDAC6 CD1, the Enigmatic Catalytic Domain of Histone Deacetylase 6. Biochemistry. 10.1021/acs.biochem.9b00934
Osko, J. D., and Christianson, D. W. (2020) Binding of inhibitors to active-site mutants of CD1, the enigmatic catalytic domain of histone deacetylase 6. Acta Crystallogr F Struct Biol Commun. 76, 428-437
Osko, J. D., Roose, B. W., Shinsky, S. A., and Christianson, D. W. (2019) Structure and Function of the Acetylpolyamine Amidohydrolase from the Deep Earth Halophile . Biochemistry. 58, 3755-3766
Oruganti, S., Zhang, Y., Li, H., Robinson, H., Terns, M. P., Terns, R. M., Yang, W., and Li, H. (2007) Alternative conformations of the archaeal Nop56/58-fibrillarin complex imply flexibility in box C/D RNPs. J Mol Biol. 371, 1141-50
Orman, M., Bodea, S., Funk, M. A., Del Campo, A. Martínez-, Bollenbach, M., Drennan, C. L., and Balskus, E. P. (2018) Structure-Guided Identification of a Small Molecule That Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. J Am Chem Soc. 10.1021/jacs.8b04883
Orlova, N., Gerding, M., Ivashkiv, O., Olinares, P. Dominic B., Chait, B. T., Waldor, M. K., and Jeruzalmi, D. (2017) The replication initiator of the cholera pathogen's second chromosome shows structural similarity to plasmid initiators. Nucleic Acids Res. 45, 3724-3737
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
Olsen, S. K., and Lima, C. D. (2013) Structure of a ubiquitin E1-E2 complex: insights to E1-E2 thioester transfer. Mol Cell. 49, 884-96
Olsen, S. K., Capili, A. D., Lu, X., Tan, D. S., and Lima, C. D. (2010) Active site remodelling accompanies thioester bond formation in the SUMO E1. Nature. 463, 906-12
Oliveira, T., Sharkey, M. A., Engel, P. C., and Khan, A. R. (2016) Crystal structure of a chimaeric bacterial glutamate dehydrogenase. Acta Crystallogr F Struct Biol Commun. 72, 462-6
Okamoto, R., Mandal, K., Sawaya, M. R., Kajihara, Y., Yeates, T. O., and Kent, S. B. H. (2014) (Quasi-)racemic X-ray structures of glycosylated and non-glycosylated forms of the chemokine Ser-CCL1 prepared by total chemical synthesis. Angew Chem Int Ed Engl. 53, 5194-8
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
Oh, Y. - S., Gao, P., Lee, K. - W., Ceglia, I., Seo, J. - S., Zhang, X., Ahn, J. - H., Chait, B. T., Patel, D. J., Kim, Y., and Greengard, P. (2013) SMARCA3, a chromatin-remodeling factor, is required for p11-dependent antidepressant action. Cell. 152, 831-43
Ogunjimi, A. A., Zeqiraj, E., Ceccarelli, D. F., Sicheri, F., Wrana, J. L., and David, L. (2012) Structural basis for specificity of TGFβ family receptor small molecule inhibitors.. Cell Signal. 24, 476-83
Ogawa, H., Qiu, Y., Ogata, C. M., and Misono, K. S. (2004) Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction. J Biol Chem. 279, 28625-31
Oellerich, T., Schneider, C., Thomas, D., Knecht, K. M., Buzovetsky, O., Kaderali, L., Schliemann, C., Bohnenberger, H., Angenendt, L., Hartmann, W., Wardelmann, E., Rothenburger, T., Mohr, S., Scheich, S., Comoglio, F., Wilke, A., Ströbel, P., Serve, H., Michaelis, M., Ferreirós, N., Geisslinger, G., Xiong, Y., Keppler, O. T., and Cinatl, J. (2019) Selective inactivation of hypomethylating agents by SAMHD1 provides a rationale for therapeutic stratification in AML. Nat Commun. 10, 3475
Ochoa, J. M., Nguyen, V. N., Nie, M., Sawaya, M. R., Bobik, T. A., and Yeates, T. O. (2020) Symmetry Breaking and Structural Polymorphism in a Bacterial Microcompartment Shell Protein for Choline Utilization. Protein Sci. 10.1002/pro.3941
Obiero, J., Bonderoff, S. A., Goertzen, M. M., and Sanders, D. A. R. (2006) Expression, purification, crystallization and preliminary X-ray crystallographic studies of Deinococcus radiodurans thioredoxin reductase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 62, 757-60
Obiero, J., Pittet, V., Bonderoff, S. A., and Sanders, D. A. R. (2010) Thioredoxin system from Deinococcus radiodurans. J Bacteriol. 192, 494-501