Publications

Found 2633 results
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2011
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
Nelersa, C. M., Schmier, B. J., and Malhotra, A. (2011) Purification and crystallization of Bacillus subtilis NrnA, a novel enzyme involved in nanoRNA degradation. Acta Crystallogr Sect F Struct Biol Cryst Commun. 67, 1235-8
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
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
Pickens, L. B., Sawaya, M. R., Rasool, H., Pashkov, I., Yeates, T. O., and Tang, Y. (2011) Structural and biochemical characterization of the salicylyl-acyltranferase SsfX3 from a tetracycline biosynthetic pathway. J Biol Chem. 286, 41539-51
Germane, K. L., and Spiller, B. W. (2011) Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase. Biochemistry. 50, 917-9
Guettler, S., LaRose, J., Petsalaki, E., Gish, G., Scotter, A., Pawson, T., Rottapel, R., and Sicheri, F. (2011) Structural basis and sequence rules for substrate recognition by Tankyrase explain the basis for cherubism disease. Cell. 147, 1340-54
Guettler, S., LaRose, J., Petsalaki, E., Gish, G., Scotter, A., Pawson, T., Rottapel, R., and Sicheri, F. (2011) Structural basis and sequence rules for substrate recognition by Tankyrase explain the basis for cherubism disease. Cell. 147, 1340-54
Tian, Y., Simanshu, D. K., Ma, J. - B., and Patel, D. J. (2011) Structural basis for piRNA 2'-O-methylated 3'-end recognition by Piwi PAZ (Piwi/Argonaute/Zwille) domains. Proc Natl Acad Sci U S A. 108, 903-10
Butler, E. B., Xiong, Y., Wang, J., and Strobel, S. A. (2011) Structural basis of cooperative ligand binding by the glycine riboswitch. Chem Biol. 18, 293-8
Shechner, D. M., and Bartel, D. P. (2011) The structural basis of RNA-catalyzed RNA polymerization. Nat Struct Mol Biol. 18, 1036-42
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
Singh, H., Reilly, T. J., and Tanner, J. J. (2011) Structural basis of the inhibition of class C acid phosphatases by adenosine 5'-phosphorothioate. FEBS J. 278, 4374-81
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
Ghosh, A., Shuman, S., and Lima, C. D. (2011) Structural insights to how mammalian capping enzyme reads the CTD code. Mol Cell. 43, 299-310
Song, J., Rechkoblit, O., Bestor, T. H., and Patel, D. J. (2011) Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation. Science. 331, 1036-40
Lazarus, M. B., Nam, Y., Jiang, J., Sliz, P., and Walker, S. (2011) Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature. 469, 564-7
Reha-Krantz, L. J., Hariharan, C., Subuddhi, U., Xia, S., Zhao, C., Beckman, J., Christian, T., and Konigsberg, W. (2011) Structure of the 2-aminopurine-cytosine base pair formed in the polymerase active site of the RB69 Y567A-DNA polymerase. Biochemistry. 50, 10136-49
Joo, W., Xu, G., Persky, N. S., Smogorzewska, A., Rudge, D. G., Buzovetsky, O., Elledge, S. J., and Pavletich, N. P. (2011) Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway. Science. 333, 312-6
Sievers, S. A., Karanicolas, J., Chang, H. W., Zhao, A., Jiang, L., Zirafi, O., Stevens, J. T., Münch, J., Baker, D., and Eisenberg, D. (2011) Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation. Nature. 475, 96-100
Sievers, S. A., Karanicolas, J., Chang, H. W., Zhao, A., Jiang, L., Zirafi, O., Stevens, J. T., Münch, J., Baker, D., and Eisenberg, D. (2011) Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation. Nature. 475, 96-100

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