Publications

Found 2717 results
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Gao, P., Yang, H., Rajashankar, K. R., Huang, Z., and Patel, D. J. (2016) Type V CRISPR-Cas Cpf1 endonuclease employs a unique mechanism for crRNA-mediated target DNA recognition. Cell Res. 26, 901-13
Gao, A., and Serganov, A. (2014) Structural insights into recognition of c-di-AMP by the ydaO riboswitch. Nat Chem Biol. 10, 787-92
Gao, A., Vasilyev, N., Luciano, D. J., Levenson-Palmer, R., Richards, J., Marsiglia, W. M., Traaseth, N. J., Belasco, J. G., and Serganov, A. (2018) Structural and kinetic insights into stimulation of RppH-dependent RNA degradation by the metabolic enzyme DapF. Nucleic Acids Res. 10.1093/nar/gky327
Gao, T., Cho, E. - A., Zhang, P., and Wu, J. (2023) Inhibition of talin-induced integrin activation by a double-hit stapled peptide. Structure. 31, 948-957.e3
Gao, X., Xie, X., Pashkov, I., Sawaya, M. R., Laidman, J., Zhang, W., Cacho, R., Yeates, T. O., and Tang, Y. (2009) Directed evolution and structural characterization of a simvastatin synthase. Chem Biol. 16, 1064-74
Gao, P., Ascano, M., Zillinger, T., Wang, W., Dai, P., Serganov, A. A., Gaffney, B. L., Shuman, S., Jones, R. A., Deng, L., Hartmann, G., Barchet, W., Tuschl, T., and Patel, D. J. (2013) Structure-function analysis of STING activation by c[G(2',5')pA(3',5')p] and targeting by antiviral DMXAA. Cell. 154, 748-62
Gao, P., Ascano, M., Wu, Y., Barchet, W., Gaffney, B. L., Zillinger, T., Serganov, A. A., Liu, Y., Jones, R. A., Hartmann, G., Tuschl, T., and Patel, D. J. (2013) Cyclic [G(2',5')pA(3',5')p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase. Cell. 153, 1094-107
Gao, L., Lam, K. - H., Liu, S., Przykopanski, A., Lübke, J., Qi, R., Krüger, M., Nowakowska, M. B., Selby, K., Douillard, F. P., Dorner, M. B., Perry, K., Lindström, M., Dorner, B. G., Rummel, A., and Jin, R. (2023) Crystal structures of OrfX1, OrfX2 and the OrfX1-OrfX3 complex from the orfX gene cluster of botulinum neurotoxin E1. FEBS Lett. 597, 524-537
Gao, J., Ha, B. Hak, Lou, H. Jane, Morse, E. M., Zhang, R., Calderwood, D. A., Turk, B. E., and Boggon, T. J. (2013) Substrate and inhibitor specificity of the type II p21-activated kinase, PAK6. PLoS One. 8, e77818
Gao, L., Guo, Y., Biswal, M., Lu, J., Yin, J., Fang, J., Chen, X., Shao, Z., Huang, M., Wang, Y., Wang, G. Greg, and Song, J. (2022) Structure of DNMT3B homo-oligomer reveals vulnerability to impairment by ICF mutations. Nat Commun. 13, 4249
Gao, P., Zillinger, T., Wang, W., Ascano, M., Dai, P., Hartmann, G., Tuschl, T., Deng, L., Barchet, W., and Patel, D. J. (2014) Binding-pocket and lid-region substitutions render human STING sensitive to the species-specific drug DMXAA. Cell Rep. 8, 1668-1676
Gantt, S. M. Lucy, Decroos, C., Lee, M. S., Gullett, L. E., Bowman, C. M., Christianson, D. W., and Fierke, C. A. (2016) General Base-General Acid Catalysis in Human Histone Deacetylase 8. Biochemistry. 55, 820-32
Gannam, Z. T. K., Min, K., Shillingford, S. R., Zhang, L., Herrington, J., Abriola, L., Gareiss, P. C., Pantouris, G., Tzouvelekis, A., Kaminski, N., Zhang, X., Yu, J., Jamali, H., Ellman, J. A., Lolis, E., Anderson, K. S., and Bennett, A. M. (2020) An allosteric site on MKP5 reveals a strategy for small-molecule inhibition. Sci Signal. 10.1126/scisignal.aba3043
Gannam, Z. T. K., Jamali, H., Kweon, O. Sang, Herrington, J., Shillingford, S. R., Papini, C., Gentzel, E., Lolis, E., Bennett, A. M., Ellman, J. A., and Anderson, K. S. (2022) Defining the structure-activity relationship for a novel class of allosteric MKP5 inhibitors. Eur J Med Chem. 243, 114712
Gangwar, S. Pal, Green, M. N., Michard, E., Simon, A. A., Feijó, J. A., and Sobolevsky, A. I. (2020) Structure of the Arabidopsis Glutamate Receptor-like Channel GLR3.2 Ligand-Binding Domain. Structure. 10.1016/j.str.2020.09.006
Gándara, F., Furukawa, H., Lee, S., and Yaghi, O. M. (2014) High methane storage capacity in aluminum metal-organic frameworks. J Am Chem Soc. 136, 5271-4
Gallegos, E. M., Reed, T. D., Mathes, F. A., Guevara, N. V., Neau, D. B., Huang, W., Newcomer, M. E., and Gilbert, N. C. (2022) Helical remodeling augments 5-lipoxygenase activity in the synthesis of pro-inflammatory mediators. J Biol Chem. 10.1016/j.jbc.2022.102282
Gallagher-Jones, M., Glynn, C., Boyer, D. R., Martynowycz, M. W., Hernandez, E., Miao, J., Zee, C. - T., Novikova, I. V., Goldschmidt, L., McFarlane, H. T., Helguera, G. F., Evans, J. E., Sawaya, M. R., Cascio, D., Eisenberg, D. S., Gonen, T., and Rodriguez, J. A. (2018) Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.. Nat Struct Mol Biol. 10.1038/s41594-017-0018-0
D Gallagher, T., Smith, N., Kim, S. - K., Robinson, H., and Reddy, P. T. (2009) Profound asymmetry in the structure of the cAMP-free cAMP Receptor Protein (CRP) from Mycobacterium tuberculosis. J Biol Chem. 284, 8228-32
Gallagher, T., Ruan, B., London, M., Bryan, M. A., and Bryan, P. N. (2009) Structure of a switchable subtilisin complexed with a substrate and with the activator azide. Biochemistry. 48, 10389-94
Galaleldeen, A., Taylor, A. B., Chen, D., Schuermann, J. P., Holloway, S. P., Hou, S., Gong, S., Zhong, G., and P Hart, J. (2013) Structure of the Chlamydia trachomatis immunodominant antigen Pgp3. J Biol Chem. 288, 22068-79
Gagnon, D. M., Brophy, M. Brunjes, Bowman, S. E. J., Stich, T. A., Drennan, C. L., R Britt, D., and Nolan, E. M. (2015) Manganese binding properties of human calprotectin under conditions of high and low calcium: X-ray crystallographic and advanced electron paramagnetic resonance spectroscopic analysis. J Am Chem Soc. 137, 3004-16
Gagnon, M. G., Lin, J., and Steitz, T. A. (2016) Elongation factor 4 remodels the A-site tRNA on the ribosome. Proc Natl Acad Sci U S A. 113, 4994-9
Gagnon, M. G., Roy, R. N., Lomakin, I. B., Florin, T., Mankin, A. S., and Steitz, T. A. (2016) Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Nucleic Acids Res. 44, 2439-50
Gagnon, M. G., Lin, J., Bulkley, D., and Steitz, T. A. (2014) Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. Science. 345, 684-7

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