Publications

Found 2819 results
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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
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
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., 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., Porter, N. J., Decroos, C., Lee, M. S., Watson, P. R., Raible, S. E., Krantz, I. D., Deardorff, M. A., and Christianson, D. W. (2020) Structural analysis of histone deacetylase 8 mutants associated with Cornelia de Lange Syndrome spectrum disorders. J Struct Biol. 213, 107681
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
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
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
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
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
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
Owens, D. D. G., Maitland, M. E. R., Yazdi, A. Khalili, Song, X., Reber, V., Schwalm, M. P., Machado, R. A. C., Bauer, N., Wang, X., Szewczyk, M. M., Dong, C., Dong, A., Loppnau, P., Calabrese, M. F., Dowling, M. S., Lee, J., Montgomery, J. I., O'Connell, T. N., Subramanyam, C., Wang, F., Adamson, E. C., Schapira, M., Gstaiger, M., Knapp, S., Vedadi, M., Min, J., Lajoie, G. A., Barsyte-Lovejoy, D., Owen, D. R., Schild-Poulter, C., and Arrowsmith, C. H. (2024) A chemical probe to modulate human GID4 Pro/N-degron interactions. Nat Chem Biol. 10.1038/s41589-024-01618-0
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
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Padayatti, P. S., Leung, J. H., Mahinthichaichan, P., Tajkhorshid, E., Ishchenko, A., Cherezov, V., S Soltis, M., J Jackson, B., C Stout, D., Gennis, R. B., and Zhang, Q. (2017) Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. Structure. 25, 1111-1119.e3
Padayatti, P., Palczewska, G., Sun, W., Palczewski, K., and Salom, D. (2012) Imaging of protein crystals with two-photon microscopy. Biochemistry. 51, 1625-37
Pak, J. S., DeLoughery, Z. J., Wang, J., Acharya, N., Park, Y., Jaworski, A., and zkan, E. Ö. (2020) NELL2-Robo3 complex structure reveals mechanisms of receptor activation for axon guidance. Nat Commun. 11, 1489
Pakhomova, S., Boeglin, W. E., Neau, D. B., Bartlett, S. G., Brash, A. R., and Newcomer, M. E. (2019) An ensemble of lipoxygenase structures reveals novel conformations of the Fe coordination sphere. Protein Sci. 10.1002/pro.3602
Pakotiprapha, D., Inuzuka, Y., Bowman, B. R., Moolenaar, G. F., Goosen, N., Jeruzalmi, D., and Verdine, G. L. (2008) Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding. Mol Cell. 29, 122-33
Pakotiprapha, D., Samuels, M., Shen, K., Hu, J. H., and Jeruzalmi, D. (2012) Structure and mechanism of the UvrA-UvrB DNA damage sensor. Nat Struct Mol Biol. 19, 291-8
Pakotiprapha, D., Liu, Y., Verdine, G. L., and Jeruzalmi, D. (2009) A structural model for the damage-sensing complex in bacterial nucleotide excision repair. J Biol Chem. 284, 12837-44
Palani, S., Machida, Y., Alvey, J. R., Mishra, V., Welter, A. L., Cui, G., Bragantini, B., Botuyan, M. Victoria, Cong, A. T. Q., Mer, G., Schellenberg, M. J., and Machida, Y. J. (2024) Dimerization-dependent serine protease activity of FAM111A prevents replication fork stalling at topoisomerase 1 cleavage complexes. Nat Commun. 15, 2064
Palioura, S., R Sherrer, L., Steitz, T. A., Söll, D., and Simonovic, M. (2009) The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation. Science. 325, 321-5
Pan, C., Zimmer, A., Shah, M., Huynh, M. Sang, Lai, C. Chieh- Lin, Sit, B., Hooda, Y., Curran, D. M., and Moraes, T. F. (2021) Actinobacillus utilizes a binding-protein dependent ABC transporter to acquire the active form of Vitamin B. J Biol Chem. 10.1016/j.jbc.2021.101046
Pandya, R. K., Partridge, J. R., Love, K. Routenberg, Schwartz, T. U., and Ploegh, H. L. (2010) A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities. J Biol Chem. 285, 5664-73
Pantel, L., Florin, T., Dobosz-Bartoszek, M., Racine, E., Sarciaux, M., Serri, M., Houard, J., Campagne, J. - M., de Figueiredo, R. Marcia, Midrier, C., Gaudriault, S., Givaudan, A., Lanois, A., Forst, S., Aumelas, A., Cotteaux-Lautard, C., Bolla, J. - M., Lundberg, C. Vingsbo, Huseby, D. L., Hughes, D., Villain-Guillot, P., Mankin, A. S., Polikanov, Y. S., and Gualtieri, M. (2018) Odilorhabdins, Antibacterial Agents that Cause Miscoding by Binding at a New Ribosomal Site. Mol Cell. 70, 83-94.e7

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