Publications

Found 699 results
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2012
Qi, Y., Nam, K., Spong, M. C., Banerjee, A., Sung, R. - J., Zhang, M., Karplus, M., and Verdine, G. L. (2012) Strandwise translocation of a DNA glycosylase on undamaged DNA. Proc Natl Acad Sci U S A. 109, 1086-91
Lai, M. - Y., Zhang, D., LaRonde-LeBlanc, N., and Fushman, D. (2012) Structural and biochemical studies of the open state of Lys48-linked diubiquitin. Biochim Biophys Acta. 1823, 2046-56
Bolla, J. Reddy, Do, S. V., Long, F., Dai, L., Su, C. - C., Lei, H. - T., Chen, X., Gerkey, J. E., Murphy, D. C., Rajashankar, K. R., Zhang, Q., and Yu, E. W. (2012) Structural and functional analysis of the transcriptional regulator Rv3066 of Mycobacterium tuberculosis. Nucleic Acids Res. 40, 9340-55
Li, X., Zhang, R., Draheim, K. M., Liu, W., Calderwood, D. A., and Boggon, T. J. (2012) Structural basis for small G protein effector interaction of Ras-related protein 1 (Rap1) and adaptor protein Krev interaction trapped 1 (KRIT1). J Biol Chem. 287, 22317-27
Ogunjimi, A. A., Zeqiraj, E., Ceccarelli, D. F., Sicheri, F., Wrana, J. L., and David, L. (2012) Structural basis for specificity of TGFβ family receptor small molecule inhibitors.. Cell Signal. 24, 476-83
Zong, Y., Zhang, B., Gu, S., Lee, K., Zhou, J., Yao, G., Figueiredo, D., Perry, K., Mei, L., and Jin, R. (2012) Structural basis of agrin-LRP4-MuSK signaling. Genes Dev. 26, 247-58
Zong, Y., Zhang, B., Gu, S., Lee, K., Zhou, J., Yao, G., Figueiredo, D., Perry, K., Mei, L., and Jin, R. (2012) Structural basis of agrin-LRP4-MuSK signaling. Genes Dev. 26, 247-58
Zong, Y., Zhang, B., Gu, S., Lee, K., Zhou, J., Yao, G., Figueiredo, D., Perry, K., Mei, L., and Jin, R. (2012) Structural basis of agrin-LRP4-MuSK signaling. Genes Dev. 26, 247-58
Dessanti, P., Zhang, Y., Allegrini, S., Tozzi, M. Grazia, Sgarrella, F., and Ealick, S. E. (2012) Structural basis of the substrate specificity of Bacillus cereus adenosine phosphorylase. Acta Crystallogr D Biol Crystallogr. 68, 239-48
Yang, H., Ji, X., Zhao, G., Ning, J., Zhao, Q., Aiken, C., Gronenborn, A. M., Zhang, P., and Xiong, Y. (2012) Structural insight into HIV-1 capsid recognition by rhesus TRIM5α.. Proc Natl Acad Sci U S A. 109, 18372-7
Yang, H., Ji, X., Zhao, G., Ning, J., Zhao, Q., Aiken, C., Gronenborn, A. M., Zhang, P., and Xiong, Y. (2012) Structural insight into HIV-1 capsid recognition by rhesus TRIM5α.. Proc Natl Acad Sci U S A. 109, 18372-7
Yang, H., Ji, X., Zhao, G., Ning, J., Zhao, Q., Aiken, C., Gronenborn, A. M., Zhang, P., and Xiong, Y. (2012) Structural insight into HIV-1 capsid recognition by rhesus TRIM5α.. Proc Natl Acad Sci U S A. 109, 18372-7
Dong, N., Zhu, Y., Lu, Q., Hu, L., Zheng, Y., and Shao, F. (2012) Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses. Cell. 150, 1029-41
Dong, N., Zhu, Y., Lu, Q., Hu, L., Zheng, Y., and Shao, F. (2012) Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses. Cell. 150, 1029-41
Levin, E. J., Cao, Y., Enkavi, G., Quick, M., Pan, Y., Tajkhorshid, E., and Zhou, M. (2012) Structure and permeation mechanism of a mammalian urea transporter. Proc Natl Acad Sci U S A. 109, 11194-9
Tu, D., Graziano, B. R., Park, E., Zheng, W., Li, Y., Goode, B. L., and Eck, M. J. (2012) Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6. Proc Natl Acad Sci U S A. 109, E3424-33
Zimanyi, C. M., Ando, N., Brignole, E. J., Asturias, F. J., Stubbe, J. A., and Drennan, C. L. (2012) Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase. Structure. 20, 1374-83
Lai, R. - Y., Huang, S., Fenwick, M. K., Hazra, A., Zhang, Y., Rajashankar, K., Philmus, B., Kinsland, C., Sanders, J. Mansell, Ealick, S. E., and Begley, T. P. (2012) Thiamin pyrimidine biosynthesis in Candida albicans : a remarkable reaction between histidine and pyridoxal phosphate. J Am Chem Soc. 134, 9157-9
Zhang, L., Lu, X., Lu, J., Liang, H., Dai, Q., Xu, G. - L., Luo, C., Jiang, H., and He, C. (2012) Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA. Nat Chem Biol. 8, 328-30
Ha, B. Hak, Davis, M. J., Chen, C., Lou, H. Jane, Gao, J., Zhang, R., Krauthammer, M., Halaban, R., Schlessinger, J., Turk, B. E., and Boggon, T. J. (2012) Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate. Proc Natl Acad Sci U S A. 109, 16107-12

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