Publications

Found 1620 results
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2011
Nam, Y., Chen, C., Gregory, R. I., Chou, J. J., and Sliz, P. (2011) Molecular basis for interaction of let-7 microRNAs with Lin28. Cell. 147, 1080-91
Chinai, J. M., Taylor, A. B., Ryno, L. M., Hargreaves, N. D., Morris, C. A., P Hart, J., and Urbach, A. R. (2011) Molecular recognition of insulin by a synthetic receptor. J Am Chem Soc. 133, 8810-3
Chang, Y., Sun, L., Kokura, K., Horton, J. R., Fukuda, M., Espejo, A., Izumi, V., Koomen, J. M., Bedford, M. T., Zhang, X., Shinkai, Y., Fang, J., and Cheng, X. (2011) MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a. Nat Commun. 2, 533
Chang, Y., Sun, L., Kokura, K., Horton, J. R., Fukuda, M., Espejo, A., Izumi, V., Koomen, J. M., Bedford, M. T., Zhang, X., Shinkai, Y., Fang, J., and Cheng, X. (2011) MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a. Nat Commun. 2, 533
Cho, U. - S., and Harrison, S. C. (2011) Ndc10 is a platform for inner kinetochore assembly in budding yeast. Nat Struct Mol Biol. 19, 48-55
Rajakumara, E., Wang, Z., Ma, H., Hu, L., Chen, H., Lin, Y., Guo, R., Wu, F., Li, H., Lan, F., Shi, Y. Geno, Xu, Y., Patel, D. J., and Shi, Y. (2011) PHD finger recognition of unmodified histone H3R2 links UHRF1 to regulation of euchromatic gene expression. Mol Cell. 43, 275-284
Xi, Q., Wang, Z., Zaromytidou, A. - I., Zhang, X. H. - F., Chow-Tsang, L. - F., Liu, J. X., Kim, H., Barlas, A., Manova-Todorova, K., Kaartinen, V., Studer, L., Mark, W., Patel, D. J., and Massagué, J. (2011) A poised chromatin platform for TGF-β access to master regulators.. Cell. 147, 1511-24
Choi, M., Sukumar, N., F Mathews, S., Liu, A., and Davidson, V. L. (2011) Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface. Biochemistry. 50, 1265-73
Cho, U. - S., and Harrison, S. C. (2011) Recognition of the centromere-specific histone Cse4 by the chaperone Scm3. Proc Natl Acad Sci U S A. 108, 9367-71
Sukumar, N., Choi, M., and Davidson, V. L. (2011) Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper. J Inorg Biochem. 105, 1638-44
Calabrese, M. F., Scott, D. C., Duda, D. M., Grace, C. R. R., Kurinov, I., Kriwacki, R. W., and Schulman, B. A. (2011) A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nat Struct Mol Biol. 18, 947-9
Duggan, K. C., Hermanson, D. J., Musee, J., Prusakiewicz, J. J., Scheib, J. L., Carter, B. D., Banerjee, S., Oates, J. A., and Marnett, L. J. (2011) (R)-Profens are substrate-selective inhibitors of endocannabinoid oxygenation by COX-2. Nat Chem Biol. 7, 803-9
Di Paolo, J. A., Huang, T., Balazs, M., Barbosa, J., Barck, K. H., Bravo, B. J., Carano, R. A. D., Darrow, J., Davies, D. R., DeForge, L. E., Diehl, L., Ferrando, R., Gallion, S. L., Giannetti, A. M., Gribling, P., Hurez, V., Hymowitz, S. G., Jones, R., Kropf, J. E., Lee, W. P., Maciejewski, P. M., Mitchell, S. A., Rong, H., Staker, B. L., J Whitney, A., Yeh, S., Young, W. B., Yu, C., Zhang, J., Reif, K., and Currie, K. S. (2011) Specific Btk inhibition suppresses B cell- and myeloid cell-mediated arthritis. Nat Chem Biol. 7, 41-50
Di Paolo, J. A., Huang, T., Balazs, M., Barbosa, J., Barck, K. H., Bravo, B. J., Carano, R. A. D., Darrow, J., Davies, D. R., DeForge, L. E., Diehl, L., Ferrando, R., Gallion, S. L., Giannetti, A. M., Gribling, P., Hurez, V., Hymowitz, S. G., Jones, R., Kropf, J. E., Lee, W. P., Maciejewski, P. M., Mitchell, S. A., Rong, H., Staker, B. L., J Whitney, A., Yeh, S., Young, W. B., Yu, C., Zhang, J., Reif, K., and Currie, K. S. (2011) Specific Btk inhibition suppresses B cell- and myeloid cell-mediated arthritis. Nat Chem Biol. 7, 41-50
Chou, C. - Y., and Tong, L. (2011) Structural and biochemical studies on the regulation of biotin carboxylase by substrate inhibition and dimerization. J Biol Chem. 286, 24417-25
Horton, J. R., Upadhyay, A. K., Hashimoto, H., Zhang, X., and Cheng, X. (2011) Structural basis for human PHF2 Jumonji domain interaction with metal ions. J Mol Biol. 406, 1-8
Armache, K. - J., Garlick, J. D., Canzio, D., Narlikar, G. J., and Kingston, R. E. (2011) Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution.. Science. 334, 977-82
Hausmann, J., Kamtekar, S., Christodoulou, E., Day, J. E., Wu, T., Fulkerson, Z., Albers, H. M. H. G., van Meeteren, L. A., Houben, A. J. S., van Zeijl, L., Jansen, S., Andries, M., Hall, ii, T., Pegg, L. E., Benson, T. E., Kasiem, M., Harlos, K., Kooi, C. W. Vander, Smyth, S. S., Ovaa, H., Bollen, M., Morris, A. J., Moolenaar, W. H., and Perrakis, A. (2011) Structural basis of substrate discrimination and integrin binding by autotaxin. Nat Struct Mol Biol. 18, 198-204
Thomas, S. R., Keller, C. A., Szyk, A., Cannon, J. R., and Laronde-Leblanc, N. A. (2011) Structural insight into the functional mechanism of Nep1/Emg1 N1-specific pseudouridine methyltransferase in ribosome biogenesis. Nucleic Acids Res. 39, 2445-57
Chang, Y., Horton, J. R., Bedford, M. T., Zhang, X., and Cheng, X. (2011) Structural insights for MPP8 chromodomain interaction with histone H3 lysine 9: potential effect of phosphorylation on methyl-lysine binding. J Mol Biol. 408, 807-14
Chang, Y., Horton, J. R., Bedford, M. T., Zhang, X., and Cheng, X. (2011) Structural insights for MPP8 chromodomain interaction with histone H3 lysine 9: potential effect of phosphorylation on methyl-lysine binding. J Mol Biol. 408, 807-14
Köksal, M., Hu, H., Coates, R. M., Peters, R. J., and Christianson, D. W. (2011) Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase. Nat Chem Biol. 7, 431-3
Köksal, M., Hu, H., Coates, R. M., Peters, R. J., and Christianson, D. W. (2011) Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase. Nat Chem Biol. 7, 431-3
Vaidya, A. T., Chen, C. - H., Dunlap, J. C., Loros, J. J., and Crane, B. R. (2011) Structure of a light-activated LOV protein dimer that regulates transcription. Sci Signal. 4, ra50
Vaidya, A. T., Chen, C. - H., Dunlap, J. C., Loros, J. J., and Crane, B. R. (2011) Structure of a light-activated LOV protein dimer that regulates transcription. Sci Signal. 4, ra50

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