Publications

Found 1065 results
Filters: First Letter Of Last Name is W  [Clear All Filters]
2009
Jin, L., Wei, W., Jiang, Y., Peng, H., Cai, J., Mao, C., Dai, H., Choy, W., Bemis, J. E., Jirousek, M. R., Milne, J. C., Westphal, C. H., and Perni, R. B. (2009) Crystal structures of human SIRT3 displaying substrate-induced conformational changes. J Biol Chem. 284, 24394-405
Jin, L., Wei, W., Jiang, Y., Peng, H., Cai, J., Mao, C., Dai, H., Choy, W., Bemis, J. E., Jirousek, M. R., Milne, J. C., Westphal, C. H., and Perni, R. B. (2009) Crystal structures of human SIRT3 displaying substrate-induced conformational changes. J Biol Chem. 284, 24394-405
Wang, G. G., Song, J., Wang, Z., Dormann, H. L., Casadio, F., Li, H., Luo, J. - L., Patel, D. J., and C Allis, D. (2009) Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger. Nature. 459, 847-51
Wang, G. G., Song, J., Wang, Z., Dormann, H. L., Casadio, F., Li, H., Luo, J. - L., Patel, D. J., and C Allis, D. (2009) Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger. Nature. 459, 847-51
Regni, C. A., Roush, R. F., Miller, D. J., Nourse, A., Walsh, C. T., and Schulman, B. A. (2009) How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic. EMBO J. 28, 1953-64
Wang, J., Dye, B. T., Rajashankar, K. R., Kurinov, I., and Schulman, B. A. (2009) Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure. Nat Struct Mol Biol. 16, 987-9
Dong, G., Wearsch, P. A., Peaper, D. R., Cresswell, P., and Reinisch, K. M. (2009) Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity. 30, 21-32
Himanen, J. P., Goldgur, Y., Miao, H., Myshkin, E., Guo, H., Buck, M., Nguyen, M., Rajashankar, K. R., Wang, B., and Nikolov, D. B. (2009) Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex. EMBO Rep. 10, 722-8
Ivanova, M. I., Sievers, S. A., Sawaya, M. R., Wall, J. S., and Eisenberg, D. (2009) Molecular basis for insulin fibril assembly. Proc Natl Acad Sci U S A. 106, 18990-5
Dias, S. M. G., Wilson, K. F., Rojas, K. S., Ambrosio, A. L. B., and Cerione, R. A. (2009) The molecular basis for the regulation of the cap-binding complex by the importins. Nat Struct Mol Biol. 16, 930-7
Wang, Q., Navarro, M. V. A. S., Peng, G., Molinelli, E., Goh, S. Lin, Judson, B. L., Rajashankar, K. R., and Sondermann, H. (2009) Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin. Proc Natl Acad Sci U S A. 106, 12700-5
Wiltzius, J. J. W., Landau, M., Nelson, R., Sawaya, M. R., Apostol, M. I., Goldschmidt, L., Soriaga, A. B., Cascio, D., Rajashankar, K., and Eisenberg, D. (2009) Molecular mechanisms for protein-encoded inheritance. Nat Struct Mol Biol. 16, 973-8
Zhou, W., Ercan, D., Chen, L., Yun, C. -hong, Li, D., Capelletti, M., Cortot, A. B., Chirieac, L., Iacob, R. E., Padera, R., Engen, J. R., Wong, K. - K., Eck, M. J., Gray, N. S., and Jänne, P. A. (2009) Novel mutant-selective EGFR kinase inhibitors against EGFR T790M. Nature. 462, 1070-4
Wang, Y., Juranek, S., Li, H., Sheng, G., Wardle, G. S., Tuschl, T., and Patel, D. J. (2009) Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes. Nature. 461, 754-61
Wang, Y., Juranek, S., Li, H., Sheng, G., Wardle, G. S., Tuschl, T., and Patel, D. J. (2009) Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes. Nature. 461, 754-61
Joh, N. H., Oberai, A., Yang, D., Whitelegge, J. P., and Bowie, J. U. (2009) Similar energetic contributions of packing in the core of membrane and water-soluble proteins. J Am Chem Soc. 131, 10846-7
Wong, C., Fujimori, D. Galonić, Walsh, C. T., and Drennan, C. L. (2009) Structural analysis of an open active site conformation of nonheme iron halogenase CytC3. J Am Chem Soc. 131, 4872-9
Wong, C., Fujimori, D. Galonić, Walsh, C. T., and Drennan, C. L. (2009) Structural analysis of an open active site conformation of nonheme iron halogenase CytC3. J Am Chem Soc. 131, 4872-9
Aranda, R., Cai, H., Worley, C. E., Levin, E. J., Li, R., Olson, J. S., Phillips, G. N., and Richards, M. P. (2009) Structural analysis of fish versus mammalian hemoglobins: effect of the heme pocket environment on autooxidation and hemin loss. Proteins. 75, 217-30
Yun, S. - M., Moulaei, T., Lim, D., Bang, J. K., Park, J. - E., Shenoy, S. R., Liu, F., Kang, Y. H., Liao, C., Soung, N. - K., Lee, S., Yoon, D. - Y., Lim, Y., Lee, D. - H., Otaka, A., Appella, E., McMahon, J. B., Nicklaus, M. C., Burke, T. R., Yaffe, M. B., Wlodawer, A., and Lee, K. S. (2009) Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1. Nat Struct Mol Biol. 16, 876-82
Lo, Y. - C., Lin, S. - C., Rospigliosi, C. C., Conze, D. B., Wu, C. - J., Ashwell, J. D., Eliezer, D., and Wu, H. (2009) Structural basis for recognition of diubiquitins by NEMO. Mol Cell. 33, 602-15
Lo, Y. - C., Lin, S. - C., Rospigliosi, C. C., Conze, D. B., Wu, C. - J., Ashwell, J. D., Eliezer, D., and Wu, H. (2009) Structural basis for recognition of diubiquitins by NEMO. Mol Cell. 33, 602-15
Sharma, H., Yu, S., Kong, J., Wang, J., and Steitz, T. A. (2009) Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proc Natl Acad Sci U S A. 106, 16604-9
Zhuang, M., Calabrese, M. F., Liu, J., M Waddell, B., Nourse, A., Hammel, M., Miller, D. J., Walden, H., Duda, D. M., Seyedin, S. N., Hoggard, T., J Harper, W., White, K. P., and Schulman, B. A. (2009) Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. Mol Cell. 36, 39-50
Zhuang, M., Calabrese, M. F., Liu, J., M Waddell, B., Nourse, A., Hammel, M., Miller, D. J., Walden, H., Duda, D. M., Seyedin, S. N., Hoggard, T., J Harper, W., White, K. P., and Schulman, B. A. (2009) Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. Mol Cell. 36, 39-50

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