Publications

Found 1654 results
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2013
Sikowitz, M. D., Shome, B., Zhang, Y., Begley, T. P., and Ealick, S. E. (2013) Structure of a Clostridium botulinum C143S thiaminase I/thiamin complex reveals active site architecture . Biochemistry. 52, 7830-9
Schormann, N., Banerjee, S., Ricciardi, R., and Chattopadhyay, D. (2013) Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 69, 1328-34
Gao, P., Ascano, M., Zillinger, T., Wang, W., Dai, P., Serganov, A. A., Gaffney, B. L., Shuman, S., Jones, R. A., Deng, L., Hartmann, G., Barchet, W., Tuschl, T., and Patel, D. J. (2013) Structure-function analysis of STING activation by c[G(2',5')pA(3',5')p] and targeting by antiviral DMXAA. Cell. 154, 748-62
Alicea-Velázquez, N. L., Jakoncic, J., and Boggon, T. J. (2013) Structure-guided studies of the SHP-1/JAK1 interaction provide new insights into phosphatase catalytic domain substrate recognition. J Struct Biol. 181, 243-51
Rajagopalan, S., Teter, S. J., Zwart, P. H., Brennan, R. G., Phillips, K. J., and Kiley, P. J. (2013) Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity. Nat Struct Mol Biol. 20, 740-7
Shnitsar, V., Li, J., Li, X., Calmettes, C., Basu, A., Casey, J. R., Moraes, T. F., and Reithmeier, R. A. F. (2013) A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters. J Biol Chem. 288, 33848-60
Gao, J., Ha, B. Hak, Lou, H. Jane, Morse, E. M., Zhang, R., Calderwood, D. A., Turk, B. E., and Boggon, T. J. (2013) Substrate and inhibitor specificity of the type II p21-activated kinase, PAK6. PLoS One. 8, e77818
Broussard, T. C., Kobe, M. J., Pakhomova, S., Neau, D. B., Price, A. E., Champion, T. S., and Waldrop, G. L. (2013) The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase. Structure. 21, 650-7
Hitosugi, T., Zhou, L., Fan, J., Elf, S., Zhang, L., Xie, J., Wang, Y., Gu, T. - L., Alečković, M., LeRoy, G., Kang, Y., Kang, H. - B., Seo, J. - H., Shan, C., Jin, P., Gong, W., Lonial, S., Arellano, M. L., Khoury, H. J., Chen, G. Z., Shin, D. M., Khuri, F. R., Boggon, T. J., Kang, S., He, C., and Chen, J. (2013) Tyr26 phosphorylation of PGAM1 provides a metabolic advantage to tumours by stabilizing the active conformation. Nat Commun. 4, 1790
Wang, P., Bashiri, G., Gao, X., Sawaya, M. R., and Tang, Y. (2013) Uncovering the enzymes that catalyze the final steps in oxytetracycline biosynthesis. J Am Chem Soc. 135, 7138-41
Goldman, P. J., Grove, T. L., Booker, S. J., and Drennan, C. L. (2013) X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry. Proc Natl Acad Sci U S A. 110, 15949-54
Goldman, P. J., Grove, T. L., Sites, L. A., McLaughlin, M. I., Booker, S. J., and Drennan, C. L. (2013) X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification. Proc Natl Acad Sci U S A. 110, 8519-24
2014
King, N. P., Bale, J. B., Sheffler, W., McNamara, D. E., Gonen, S., Gonen, T., Yeates, T. O., and Baker, D. (2014) Accurate design of co-assembling multi-component protein nanomaterials. Nature. 510, 103-8
King, N. P., Bale, J. B., Sheffler, W., McNamara, D. E., Gonen, S., Gonen, T., Yeates, T. O., and Baker, D. (2014) Accurate design of co-assembling multi-component protein nanomaterials. Nature. 510, 103-8
Sinha, S., Cheng, S., Sung, Y. Won, McNamara, D. E., Sawaya, M. R., Yeates, T. O., and Bobik, T. A. (2014) Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the Pdu microcompartment. J Mol Biol. 426, 2328-45
Polikanov, Y. S., Osterman, I. A., Szal, T., Tashlitsky, V. N., Serebryakova, M. V., Kusochek, P., Bulkley, D., Malanicheva, I. A., Efimenko, T. A., Efremenkova, O. V., Konevega, A. L., Shaw, K. J., Bogdanov, A. A., Rodnina, M. V., Dontsova, O. A., Mankin, A. S., Steitz, T. A., and Sergiev, P. V. (2014) Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome. Mol Cell. 56, 531-40
Polikanov, Y. S., Osterman, I. A., Szal, T., Tashlitsky, V. N., Serebryakova, M. V., Kusochek, P., Bulkley, D., Malanicheva, I. A., Efimenko, T. A., Efremenkova, O. V., Konevega, A. L., Shaw, K. J., Bogdanov, A. A., Rodnina, M. V., Dontsova, O. A., Mankin, A. S., Steitz, T. A., and Sergiev, P. V. (2014) Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome. Mol Cell. 56, 531-40
Bulkley, D., Brandi, L., Polikanov, Y. S., Fabbretti, A., O'Connor, M., Gualerzi, C. O., and Steitz, T. A. (2014) The antibiotics dityromycin and GE82832 bind protein S12 and block EF-G-catalyzed translocation. Cell Rep. 6, 357-65
Bulkley, D., Brandi, L., Polikanov, Y. S., Fabbretti, A., O'Connor, M., Gualerzi, C. O., and Steitz, T. A. (2014) The antibiotics dityromycin and GE82832 bind protein S12 and block EF-G-catalyzed translocation. Cell Rep. 6, 357-65
Simanshu, D. K., Zhai, X., Munch, D., Hofius, D., Markham, J. E., Bielawski, J., Bielawska, A., Malinina, L., Molotkovsky, J. G., Mundy, J. W., Patel, D. J., and Brown, R. E. (2014) Arabidopsis accelerated cell death 11, ACD11, is a ceramide-1-phosphate transfer protein and intermediary regulator of phytoceramide levels. Cell Rep. 6, 388-99
Simanshu, D. K., Zhai, X., Munch, D., Hofius, D., Markham, J. E., Bielawski, J., Bielawska, A., Malinina, L., Molotkovsky, J. G., Mundy, J. W., Patel, D. J., and Brown, R. E. (2014) Arabidopsis accelerated cell death 11, ACD11, is a ceramide-1-phosphate transfer protein and intermediary regulator of phytoceramide levels. Cell Rep. 6, 388-99
Simanshu, D. K., Zhai, X., Munch, D., Hofius, D., Markham, J. E., Bielawski, J., Bielawska, A., Malinina, L., Molotkovsky, J. G., Mundy, J. W., Patel, D. J., and Brown, R. E. (2014) Arabidopsis accelerated cell death 11, ACD11, is a ceramide-1-phosphate transfer protein and intermediary regulator of phytoceramide levels. Cell Rep. 6, 388-99
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
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
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

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