Publications

Found 2797 results
Journal Article
Lin, L. Yingqi, McCarthy, S., Powell, B. M., Manurung, Y., Xiang, I. M., Dean, W. L., Chaires, B., and Yatsunyk, L. A. (2020) Biophysical and X-ray structural studies of the (GGGTT)3GGG G-quadruplex in complex with N-methyl mesoporphyrin IX. PLoS One. 15, e0241513
Fenwick, M. K., Almabruk, K. H., Ealick, S. E., Begley, T. P., and Philmus, B. (2017) Biochemical Characterization and Structural Basis of Reactivity and Regioselectivity Differences between Burkholderia thailandensis and Burkholderia glumae 1,6-Didesmethyltoxoflavin N-Methyltransferase. Biochemistry. 10.1021/acs.biochem.7b00476
Hicks, K. A., and Ealick, S. E. (2016) Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway. Acta Crystallogr D Struct Biol. 72, 808-16
French, J. B., and Ealick, S. E. (2010) Biochemical and structural characterization of a ureidoglycine aminotransferase in the Klebsiella pneumoniae uric acid catabolic pathway. Biochemistry. 49, 5975-7
Grell, T. A. J., Young, A. P., Drennan, C. L., and Bandarian, V. (2018) Biochemical and Structural Characterization of a Schiff Base in the Radical-Mediated Biosynthesis of 4-Demethylwyosine by TYW1. J Am Chem Soc. 10.1021/jacs.8b01493
van Rosenburgh, I. K. van Alde, Lu, D. M., Grant, M. J., Stayrook, S. E., Phadke, M., Walther, Z., Goldberg, S. B., Politi, K., Lemmon, M. A., Ashtekar, K. D., and Tsutsui, Y. (2022) Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutations. Nat Commun. 13, 6791
Winter, J. M., Cascio, D., Dietrich, D., Sato, M., Watanabe, K., Sawaya, M. R., Vederas, J. C., and Tang, Y. (2015) Biochemical and Structural Basis for Controlling Chemical Modularity in Fungal Polyketide Biosynthesis. J Am Chem Soc. 137, 9885-93
Jonnalagadda, R., Flores, A. Del Rio, Cai, W., Mehmood, R., Narayanamoorthy, M., Ren, C., Zaragoza, J. Paulo T., Kulik, H. J., Zhang, W., and Drennan, C. L. (2020) Biochemical and crystallographic investigations into isonitrile formation by a non-heme iron-dependent oxidase/decarboxylase. J Biol Chem. 10.1074/jbc.RA120.015932
Borowska, M. T., Boughter, C. T., Bunker, J. J., Guthmiller, J. J., Wilson, P. C., Roux, B., Bendelac, A., and Adams, E. J. (2023) Biochemical and biophysical characterization of natural polyreactivity in antibodies. Cell Rep. 42, 113190
Gao, P., Zillinger, T., Wang, W., Ascano, M., Dai, P., Hartmann, G., Tuschl, T., Deng, L., Barchet, W., and Patel, D. J. (2014) Binding-pocket and lid-region substitutions render human STING sensitive to the species-specific drug DMXAA. Cell Rep. 8, 1668-1676
Chen, P. Yang- Ting, Aman, H., Can, M., Ragsdale, S. W., and Drennan, C. L. (2018) Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from . Proc Natl Acad Sci U S A. 115, 3846-3851
Ilies, M., Di Costanzo, L., Dowling, D. P., Thorn, K. J., and Christianson, D. W. (2011) Binding of α,α-disubstituted amino acids to arginase suggests new avenues for inhibitor design.. J Med Chem. 54, 5432-43
Schormann, N., Banerjee, S., Ricciardi, R., and Chattopadhyay, D. (2015) Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase. BMC Struct Biol. 15, 10
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
Ziervogel, B. K., and Roux, B. (2013) The binding of antibiotics in OmpF porin. Structure. 21, 76-87
Herbst-Gervasoni, C. J., and Christianson, D. W. (2019) Binding of -Acetylspermidine Analogues to Histone Deacetylase 10 Reveals Molecular Strategies for Blocking Polyamine Deacetylation. Biochemistry. 10.1021/acs.biochem.9b00906
Sjekloća, L., and Ferré-D'Amaré, A. R. (2019) Binding between G Quadruplexes at the Homodimer Interface of the Corn RNA Aptamer Strongly Activates Thioflavin T Fluorescence. Cell Chem Biol. 26, 1159-1168.e4
Profeta, G. S., Reis, C. V. Dos, Santiago, Ada S., Godoi, P. H. C., Fala, A. M., Wells, C. I., Sartori, R., Salmazo, A. P. T., Ramos, P. Z., Massirer, K. B., Elkins, J. M., Drewry, D. H., Gileadi, O., and Couñago, R. M. (2019) Binding and structural analyses of potent inhibitors of the human Ca/calmodulin dependent protein kinase kinase 2 (CAMKK2) identified from a collection of commercially-available kinase inhibitors. Sci Rep. 9, 16452
An, L., Said, M., Tran, L., Majumder, S., Goreshnik, I., Lee, G. Rie, Juergens, D., Dauparas, J., Anishchenko, I., Coventry, B., Bera, A. K., Kang, A., Levine, P. M., Alvarez, V., Pillai, A., Norn, C., Feldman, D., Zorine, D., Hicks, D. R., Li, X., Sanchez, M. Garcia, Vafeados, D. K., Salveson, P. J., Vorobieva, A. A., and Baker, D. (2024) Binding and sensing diverse small molecules using shape-complementary pseudocycles. Science. 385, 276-282
Seckute, J., McCloskey, D. E., H Thomas, J., Secrist, J. A., Pegg, A. E., and Ealick, S. E. (2011) Binding and inhibition of human spermidine synthase by decarboxylated S-adenosylhomocysteine. Protein Sci. 20, 1836-44
Chen, C. - W., Pavlova, J. A., Lukianov, D. A., Tereshchenkov, A. G., Makarov, G. I., Khairullina, Z. Z., Tashlitsky, V. N., Paleskava, A., Konevega, A. L., Bogdanov, A. A., Osterman, I. A., Sumbatyan, N. V., and Polikanov, Y. S. (2021) Binding and Action of Triphenylphosphonium Analog of Chloramphenicol upon the Bacterial Ribosome. Antibiotics (Basel). 10.3390/antibiotics10040390
Tereshchenkov, A. G., Dobosz-Bartoszek, M., Osterman, I. A., Marks, J., Sergeeva, V. A., Kasatsky, P., Komarova, E. S., Stavrianidi, A. N., Rodin, I. A., Konevega, A. L., Sergiev, P. V., Sumbatyan, N. V., Mankin, A. S., Bogdanov, A. A., and Polikanov, Y. S. (2018) Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome. J Mol Biol. 10.1016/j.jmb.2018.01.016
Xia, S., Eom, S. Hyun, Konigsberg, W. H., and Wang, J. (2012) Bidentate and tridentate metal-ion coordination states within ternary complexes of RB69 DNA polymerase. Protein Sci. 21, 447-51
McKeown, M. R., Shaw, D. L., Fu, H., Liu, S., Xu, X., Marineau, J. J., Huang, Y., Zhang, X., Buckley, D. L., Kadam, A., Zhang, Z., Blacklow, S. C., Qi, J., Zhang, W., and Bradner, J. E. (2014) Biased multicomponent reactions to develop novel bromodomain inhibitors. J Med Chem. 57, 9019-27
Batool, Z., Pavlova, J. A., Paranjpe, M. N., Tereshchenkov, A. G., Lukianov, D. A., Osterman, I. A., Bogdanov, A. A., Sumbatyan, N. V., and Polikanov, Y. S. (2024) Berberine analog of chloramphenicol exhibits a distinct mode of action and unveils ribosome plasticity. Structure. 10.1016/j.str.2024.06.013

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