Publications

Found 1336 results
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2013
Monda, J. K., Scott, D. C., Miller, D. J., Lydeard, J., King, D., J Harper, W., Bennett, E. J., and Schulman, B. A. (2013) Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes. Structure. 21, 42-53
Grigg, J. C., and Ke, A. (2013) Structural determinants for geometry and information decoding of tRNA by T box leader RNA. Structure. 21, 2025-32
Kirouac, K. N., Basu, A. K., and Ling, H. (2013) Structural mechanism of replication stalling on a bulky amino-polycyclic aromatic hydrocarbon DNA adduct by a y family DNA polymerase. J Mol Biol. 425, 4167-76
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
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
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
Duda, D. M., Olszewski, J. L., Schuermann, J. P., Kurinov, I., Miller, D. J., Nourse, A., Alpi, A. F., and Schulman, B. A. (2013) Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism. Structure. 21, 1030-41
Sharkey, M. A., Oliveira, T. F., Engel, P. C., and Khan, A. R. (2013) Structure of NADP(+)-dependent glutamate dehydrogenase from Escherichia coli--reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases. FEBS J. 280, 4681-92
Krishnan, V., Dwivedi, P., Kim, B. J., Samal, A., Macon, K., Ma, X., Mishra, A., Doran, K. S., Ton-That, H., and Narayana, S. V. L. (2013) Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions. Acta Crystallogr D Biol Crystallogr. 69, 1073-89
Krishnan, V., Dwivedi, P., Kim, B. J., Samal, A., Macon, K., Ma, X., Mishra, A., Doran, K. S., Ton-That, H., and Narayana, S. V. L. (2013) Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions. Acta Crystallogr D Biol Crystallogr. 69, 1073-89
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
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
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
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
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
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
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
Fera, D., Schmidt, A. G., Haynes, B. F., Gao, F., Liao, H. - X., Kepler, T. B., and Harrison, S. C. (2014) Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains. Proc Natl Acad Sci U S A. 111, 10275-80
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
Sui, X., Kiser, P. D., Che, T., Carey, P. R., Golczak, M., Shi, W., von Lintig, J., and Palczewski, K. (2014) Analysis of carotenoid isomerase activity in a prototypical carotenoid cleavage enzyme, apocarotenoid oxygenase (ACO). J Biol Chem. 289, 12286-99
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
Yang, G., Fu, Y., Malakhova, M., Kurinov, I., Zhu, F., Yao, K., Li, H., Chen, H., Li, W., Lim, D. Young, Sheng, Y., Bode, A. M., Dong, Z., and Dong, Z. (2014) Caffeic acid directly targets ERK1/2 to attenuate solar UV-induced skin carcinogenesis. Cancer Prev Res (Phila). 7, 1056-66

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