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Geng, Y., Bush, M., Mosyak, L., Wang, F., and Fan, Q. R. (2013) Structural mechanism of ligand activation in human GABA(B) receptor. Nature. 504, 254-9
Geng, Y., Mosyak, L., Kurinov, I., Zuo, H., Sturchler, E., Cheng, T. Cheung, Subramanyam, P., Brown, A. P., Brennan, S. C., Mun, H. - C., Bush, M., Chen, Y., Nguyen, T. X., Cao, B., Chang, D. D., Quick, M., Conigrave, A. D., Colecraft, H. M., McDonald, P., and Fan, Q. R. (2016) Structural mechanism of ligand activation in human calcium-sensing receptor. Elife. 10.7554/eLife.13662
Ge, J., Elferich, J., Goehring, A., Zhao, H., Schuck, P., and Gouaux, E. (2018) Structure of mouse protocadherin 15 of the stereocilia tip link in complex with LHFPL5. Elife. 10.7554/eLife.38770
Gaynes, M. N., Osika, K. R., and Christianson, D. W. (2024) Structure and Function of Sabinene Synthase, a Monoterpene Cyclase That Generates a Highly Strained [3.1.0] Bicyclic Product. Biochemistry. 63, 3147-3159
Garg, A., Goldgur, Y., Sanchez, A. M., Schwer, B., and Shuman, S. (2019) Structure of fission yeast transcription factor Pho7 bound to promoter DNA and effect of Pho7 mutations on DNA binding and phosphate homeostasis. Mol Cell Biol. 10.1128/MCB.00132-19
Garg, P., Ceccarelli, D. F., Keszei, A. Fa, Kourinov, I., Sicheri, F., and Sidhu, S. S. (2019) Structural and Functional Analysis of Ubiquitin-based inhibitors that Target the Backsides of E2 Enzymes. J Mol Biol. 10.1016/j.jmb.2019.09.024
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, 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, 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., 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, A., and Serganov, A. (2014) Structural insights into recognition of c-di-AMP by the ydaO riboswitch. Nat Chem Biol. 10, 787-92
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
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
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, 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., Seetharaman, S. V., Bulkley, D., and Steitz, T. A. (2012) Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome. Science. 335, 1370-2
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Funk, M. A., Judd, E. T., E Marsh, N. G., Elliott, S. J., and Drennan, C. L. (2014) Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity. Proc Natl Acad Sci U S A. 111, 10161-6
Funk, M. A. (2015) Structural Studies of Radical Enzymes in Bacterial Central Metabolism. Ph.D. thesis, Massachusetts Institute of Technology, Cambridge, Massachusetts
Fribourgh, J. L., Nguyen, H. C., Matreyek, K. A., Alvarez, F. Joan D., Summers, B. J., Dewdney, T. G., Aiken, C., Zhang, P., Engelman, A., and Xiong, Y. (2014) Structural insight into HIV-1 restriction by MxB. Cell Host Microbe. 16, 627-638
Frey, K. M., Bertoletti, N., Chan, A. H., Ippolito, J. A., Bollini, M., Spasov, K. A., Jorgensen, W. L., and Anderson, K. S. (2022) Structural Studies and Structure Activity Relationships for Novel Computationally Designed Non-nucleoside Inhibitors and Their Interactions With HIV-1 Reverse Transcriptase. Front Mol Biosci. 9, 805187
French, J. B., and Ealick, S. E. (2011) Structural and kinetic insights into the mechanism of 5-hydroxyisourate hydrolase from Klebsiella pneumoniae. Acta Crystallogr D Biol Crystallogr. 67, 671-7
French, J. B., and Ealick, S. E. (2010) Structural and mechanistic studies on Klebsiella pneumoniae 2-Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase. J Biol Chem. 285, 35446-54
French, J. B., Begley, T. P., and Ealick, S. E. (2011) Structure of trifunctional THI20 from yeast. Acta Crystallogr D Biol Crystallogr. 67, 784-91
Fraser, B. J., Beldar, S., Seitova, A., Hutchinson, A., Mannar, D., Li, Y., Kwon, D., Tan, R., Wilson, R. P., Leopold, K., Subramaniam, S., Halabelian, L., Arrowsmith, C. H., and Bénard, F. (2022) Structure and activity of human TMPRSS2 protease implicated in SARS-CoV-2 activation. Nat Chem Biol. 10.1038/s41589-022-01059-7

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