Publications

Found 2668 results
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2010
Freeman, M. M., Seaman, M. S., Rits-Volloch, S., Hong, X., Kao, C. - Y., Ho, D. D., and Chen, B. (2010) Crystal structure of HIV-1 primary receptor CD4 in complex with a potent antiviral antibody. Structure. 18, 1632-41
Tahirov, T. H., Babayeva, N. D., Varzavand, K., Cooper, J. J., Sedore, S. C., and Price, D. H. (2010) Crystal structure of HIV-1 Tat complexed with human P-TEFb. Nature. 465, 747-51
Bacik, J. - P., Walker, J. R., Ali, M., Schimmer, A. D., and Dhe-Paganon, S. (2010) Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5) bound to ATP: mechanistic insights into a minimalistic E1 enzyme. J Biol Chem. 285, 20273-80
Singla, N., Goldgur, Y., Xu, K., Paavilainen, S., Nikolov, D. B., and Himanen, J. P. (2010) Crystal structure of the ligand-binding domain of the promiscuous EphA4 receptor reveals two distinct conformations. Biochem Biophys Res Commun. 399, 555-9
Mehboob, S., Song, Y., Witek, M., Long, F., Santarsiero, B. D., Johnson, M. E., and Fung, L. W. - M. (2010) Crystal structure of the nonerythroid alpha-spectrin tetramerization site reveals differences between erythroid and nonerythroid spectrin tetramer formation. J Biol Chem. 285, 14572-84
Mehboob, S., Song, Y., Witek, M., Long, F., Santarsiero, B. D., Johnson, M. E., and Fung, L. W. - M. (2010) Crystal structure of the nonerythroid alpha-spectrin tetramerization site reveals differences between erythroid and nonerythroid spectrin tetramer formation. J Biol Chem. 285, 14572-84
Arbing, M. A., Handelman, S. K., Kuzin, A. P., Verdon, G., Wang, C., Su, M., Rothenbacher, F. P., Abashidze, M., Liu, M., Hurley, J. M., Xiao, R., Acton, T., Inouye, M., Montelione, G. T., Woychik, N. A., and Hunt, J. F. (2010) Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems. Structure. 18, 996-1010
Long, F., Su, C. - C., Zimmermann, M. T., Boyken, S. E., Rajashankar, K. R., Jernigan, R. L., and Yu, E. W. (2010) Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport. Nature. 467, 484-8
Laganowsky, A., Benesch, J. L. P., Landau, M., Ding, L., Sawaya, M. R., Cascio, D., Huang, Q., Robinson, C. V., Horwitz, J., and Eisenberg, D. (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci. 19, 1031-43
Apostol, M. I., Sawaya, M. R., Cascio, D., and Eisenberg, D. (2010) Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J Biol Chem. 285, 29671-5
Banigan, J. R., Mandal, K., Sawaya, M. R., Thammavongsa, V., Hendrickx, A. P. A., Schneewind, O., Yeates, T. O., and Kent, S. B. H. (2010) Determination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography. Protein Sci. 19, 1840-9
Banigan, J. R., Mandal, K., Sawaya, M. R., Thammavongsa, V., Hendrickx, A. P. A., Schneewind, O., Yeates, T. O., and Kent, S. B. H. (2010) Determination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography. Protein Sci. 19, 1840-9
Schoeffler, A. J., May, A. P., and Berger, J. M. (2010) A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function. Nucleic Acids Res. 38, 7830-44
Scott, D. C., Monda, J. K., Grace, C. R. R., Duda, D. M., Kriwacki, R. W., Kurz, T., and Schulman, B. A. (2010) A dual E3 mechanism for Rub1 ligation to Cdc53. Mol Cell. 39, 784-96
Scott, D. C., Monda, J. K., Grace, C. R. R., Duda, D. M., Kriwacki, R. W., Kurz, T., and Schulman, B. A. (2010) A dual E3 mechanism for Rub1 ligation to Cdc53. Mol Cell. 39, 784-96
Wang, L., Yang, J. Kuk, Kabaleeswaran, V., Rice, A. J., Cruz, A. C., Park, A. Young, Yin, Q., Damko, E., Jang, S. Bok, Raunser, S., Robinson, C. V., Siegel, R. M., Walz, T., and Wu, H. (2010) The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat Struct Mol Biol. 17, 1324-9
R Wiseman, L., Zhang, Y., Lee, K. P. K., Harding, H. P., Haynes, C. M., Price, J., Sicheri, F., and Ron, D. (2010) Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Mol Cell. 38, 291-304
Fuse, S., Tsukamoto, H., Yuan, Y., Wang, T. - S. Andrew, Zhang, Y., Bolla, M., Walker, S., Sliz, P., and Kahne, D. (2010) Functional and structural analysis of a key region of the cell wall inhibitor moenomycin. ACS Chem Biol. 5, 701-11
Paul, D., O'Leary, S. E., Rajashankar, K., Bu, W., Toms, A., Settembre, E. C., Sanders, J. M., Begley, T. P., and Ealick, S. E. (2010) Glycal formation in crystals of uridine phosphorylase. Biochemistry. 49, 3499-509
Paul, D., O'Leary, S. E., Rajashankar, K., Bu, W., Toms, A., Settembre, E. C., Sanders, J. M., Begley, T. P., and Ealick, S. E. (2010) Glycal formation in crystals of uridine phosphorylase. Biochemistry. 49, 3499-509
Mueser, T. C., Griffith, W. P., Kovalevsky, A. Y., Guo, J., Seaver, S., Langan, P., and B Hanson, L. (2010) Hemoglobin redux: combining neutron and X-ray diffraction with mass spectrometry to analyse the quaternary state of oxidized hemoglobins. Acta Crystallogr D Biol Crystallogr. 66, 1249-56
French, J. B., Cen, Y., Sauve, A. A., and Ealick, S. E. (2010) High-resolution crystal structures of Streptococcus pneumoniae nicotinamidase with trapped intermediates provide insights into the catalytic mechanism and inhibition by aldehydes . Biochemistry. 49, 8803-12
Subramanian, R., Wilson-Kubalek, E. M., Arthur, C. P., Bick, M. J., Campbell, E. A., Darst, S. A., Milligan, R. A., and Kapoor, T. M. (2010) Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein. Cell. 142, 433-43
Sukumar, N., Mathews, F. S., Langan, P., and Davidson, V. L. (2010) A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transfer. Proc Natl Acad Sci U S A. 107, 6817-22
Stewart, M. L., Fire, E., Keating, A. E., and Walensky, L. D. (2010) The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer. Nat Chem Biol. 6, 595-601

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