Publications

Found 1131 results
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2015
Kudalkar, S. N., Nikas, S. P., Kingsley, P. J., Xu, S., Galligan, J. J., Rouzer, C. A., Banerjee, S., Ji, L., Eno, M. R., Makriyannis, A., and Marnett, L. J. (2015) 13-Methylarachidonic acid is a positive allosteric modulator of endocannabinoid oxygenation by cyclooxygenase. J Biol Chem. 290, 7897-909
Blobaum, A. L., Xu, S., Rowlinson, S. W., Duggan, K. C., Banerjee, S., Kudalkar, S. N., Birmingham, W. R., Ghebreselasie, K., and Marnett, L. J. (2015) Action at a distance: mutations of peripheral residues transform rapid reversible inhibitors to slow, tight binders of cyclooxygenase-2. J Biol Chem. 290, 12793-803
Murphy, M. W., Lee, J. K., Rojo, S., Gearhart, M. D., Kurahashi, K., Banerjee, S., Loeuille, G. - A., Bashamboo, A., McElreavey, K., Zarkower, D., Aihara, H., and Bardwell, V. J. (2015) An ancient protein-DNA interaction underlying metazoan sex determination. Nat Struct Mol Biol. 22, 442-51
Kiser, P. D., Zhang, J., Badiee, M., Li, Q., Shi, W., Sui, X., Golczak, M., Tochtrop, G. P., and Palczewski, K. (2015) Catalytic mechanism of a retinoid isomerase essential for vertebrate vision. Nat Chem Biol. 11, 409-15
Wong, Y. Liang, Anzola, J. V., Davis, R. L., Yoon, M., Motamedi, A., Kroll, A., Seo, C. P., Hsia, J. E., Kim, S. K., Mitchell, J. W., Mitchell, B. J., Desai, A., Gahman, T. C., Shiau, A. K., and Oegema, K. (2015) Cell biology. Reversible centriole depletion with an inhibitor of Polo-like kinase 4. Science. 348, 1155-60
Lin, J., Gagnon, M. G., Bulkley, D., and Steitz, T. A. (2015) Conformational changes of elongation factor G on the ribosome during tRNA translocation. Cell. 160, 219-27
Chen, Y., Bauer, B. W., Rapoport, T. A., and Gumbart, J. C. (2015) Conformational Changes of the Clamp of the Protein Translocation ATPase SecA. J Mol Biol. 427, 2348-59
Suwa, Y., Gu, J., Baranovskiy, A. G., Babayeva, N. D., Pavlov, Y. I., and Tahirov, T. H. (2015) Crystal Structure of the Human Pol α B Subunit in Complex with the C-terminal Domain of the Catalytic Subunit.. J Biol Chem. 290, 14328-37
Baranovskiy, A. G., Zhang, Y., Suwa, Y., Babayeva, N. D., Gu, J., Pavlov, Y. I., and Tahirov, T. H. (2015) Crystal structure of the human primase. J Biol Chem. 290, 5635-46
Baker, B. Y., Gulati, S., Shi, W., Wang, B., Stewart, P. L., and Palczewski, K. (2015) Crystallization of proteins from crude bovine rod outer segments. Methods Enzymol. 557, 439-58
Tan, L., Akahane, K., McNally, R., Reyskens, K. M. S. E., Ficarro, S. B., Liu, S., Herter-Sprie, G. S., Koyama, S., Pattison, M. J., Labella, K., Johannessen, iv, L., Akbay, E. A., Wong, K. - K., Frank, D. A., Marto, J. A., Look, T. A., J Arthur, S. C., Eck, M. J., and Gray, N. S. (2015) Development of Selective Covalent Janus Kinase 3 Inhibitors. J Med Chem. 58, 6589-606
Lee, W. - G., Frey, K. M., Gallardo-Macias, R., Spasov, K. A., Chan, A. H., Anderson, K. S., and Jorgensen, W. L. (2015) Discovery and crystallography of bicyclic arylaminoazines as potent inhibitors of HIV-1 reverse transcriptase. Bioorg Med Chem Lett. 25, 4824-4827
Begley, M. J., Yun, C. -hong, Gewinner, C. A., Asara, J. M., Johnson, J. L., Coyle, A. J., Eck, M. J., Apostolou, I., and Cantley, L. C. (2015) EGF-receptor specificity for phosphotyrosine-primed substrates provides signal integration with Src. Nat Struct Mol Biol. 22, 983-90
Schwer, B., Ghosh, A., Sanchez, A. M., Lima, C. D., and Shuman, S. (2015) Genetic and structural analysis of the essential fission yeast RNA polymerase II CTD phosphatase Fcp1. RNA. 21, 1135-46
Sue, A. C. - H., Mannige, R. V., Deng, H., Cao, D., Wang, C., Gándara, F., J Stoddart, F., Whitelam, S., and Yaghi, O. M. (2015) Heterogeneity of functional groups in a metal-organic framework displays magic number ratios. Proc Natl Acad Sci U S A. 112, 5591-6
Zeqiraj, E., Tian, L., Piggott, C. A., Pillon, M. C., Duffy, N. M., Ceccarelli, D. F., Keszei, A. F. A., Lorenzen, K., Kurinov, I., Orlicky, S., Gish, G. D., Heck, A. J. R., Guarné, A., Greenberg, R. A., and Sicheri, F. (2015) Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function. Mol Cell. 59, 970-83
Zeqiraj, E., Tian, L., Piggott, C. A., Pillon, M. C., Duffy, N. M., Ceccarelli, D. F., Keszei, A. F. A., Lorenzen, K., Kurinov, I., Orlicky, S., Gish, G. D., Heck, A. J. R., Guarné, A., Greenberg, R. A., and Sicheri, F. (2015) Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function. Mol Cell. 59, 970-83
Zeqiraj, E., Tian, L., Piggott, C. A., Pillon, M. C., Duffy, N. M., Ceccarelli, D. F., Keszei, A. F. A., Lorenzen, K., Kurinov, I., Orlicky, S., Gish, G. D., Heck, A. J. R., Guarné, A., Greenberg, R. A., and Sicheri, F. (2015) Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function. Mol Cell. 59, 970-83
Ahmed, M., Cheng, M., Zhao, Q., Goldgur, Y., Cheal, S. M., Guo, H. - F., Larson, S. M., and Cheung, N. - K. V. (2015) Humanized Affinity-matured Monoclonal Antibody 8H9 Has Potent Antitumor Activity and Binds to FG Loop of Tumor Antigen B7-H3. J Biol Chem. 290, 30018-29
Ahmed, M., Cheng, M., Zhao, Q., Goldgur, Y., Cheal, S. M., Guo, H. - F., Larson, S. M., and Cheung, N. - K. V. (2015) Humanized Affinity-matured Monoclonal Antibody 8H9 Has Potent Antitumor Activity and Binds to FG Loop of Tumor Antigen B7-H3. J Biol Chem. 290, 30018-29

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