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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
Germane, K. L., Ohi, R., Goldberg, M. B., and Spiller, B. W. (2008) Structural and functional studies indicate that Shigella VirA is not a protease and does not directly destabilize microtubules. Biochemistry. 47, 10241-3
Germane, K. L., and Spiller, B. W. (2011) Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase. Biochemistry. 50, 917-9
Ghosh, A., Shuman, S., and Lima, C. D. (2011) Structural insights to how mammalian capping enzyme reads the CTD code. Mol Cell. 43, 299-310
Gibson, M. I. (2015) Structures of Oxalate Oxidoreductase: C[2] Activation by a Microbial TPP-Dependent Ferredoxin Oxidoreductase. Ph.D. thesis, Massachusetts Institute of Technology, Cambridge, Massachusetts
Gibson, M. I., Brignole, E. J., Pierce, E., Can, M., Ragsdale, S. W., and Drennan, C. L. (2015) The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism. Biochemistry. 54, 4112-20
Gilbert, N. C., Gerstmeier, J., Schexnaydre, E. E., Börner, F., Garscha, U., Neau, D. B., Werz, O., and Newcomer, M. E. (2020) Structural and mechanistic insights into 5-lipoxygenase inhibition by natural products. Nat Chem Biol. 10.1038/s41589-020-0544-7
Gilbert, N. C., Bartlett, S. G., Waight, M. T., Neau, D. B., Boeglin, W. E., Brash, A. R., and Newcomer, M. E. (2011) The structure of human 5-lipoxygenase. Science. 331, 217-9
Gilleran, J. A., Ashraf, K., Delvillar, M., Eck, T., Fondekar, R., Miller, E. B., Hutchinson, A., Dong, A., Seitova, A., De Souza, M. Laureano, Augeri, D., Halabelian, L., Siekierka, J., Rotella, D. P., Gordon, J., Childers, W. E., Grier, M. C., Staker, B. L., Roberge, J. Y., and Bhanot, P. (2024) Structure-Activity Relationship of a Pyrrole Based Series of PfPKG Inhibitors as Anti-Malarials. J Med Chem. 67, 3467-3503
Golczak, M., Kiser, P. D., Sears, A. E., Lodowski, D. T., Blaner, W. S., and Palczewski, K. (2012) Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins. J Biol Chem. 287, 23790-807
Goodman, K. Marie, Rubinstein, R., Thu, C. Aye, Bahna, F., Mannepalli, S., Ahlsen, G., Rittenhouse, C., Maniatis, T., Honig, B., and Shapiro, L. (2016) Structural Basis of Diverse Homophilic Recognition by Clustered α- and β-Protocadherins.. Neuron. 90, 709-23
Gordon, W. R., Roy, M., Vardar-Ulu, D., Garfinkel, M., Mansour, M. R., Aster, J. C., and Blacklow, S. C. (2009) Structure of the Notch1-negative regulatory region: implications for normal activation and pathogenic signaling in T-ALL. Blood. 113, 4381-90
Gorelik, A., Illes, K., Mazhab-Jafari, M. T., and Nagar, B. (2023) Structure of the immunoregulatory sialidase NEU1. Sci Adv. 9, eadf8169
Gorelik, M., Manczyk, N., Pavlenco, A., Kurinov, I., Sidhu, S. S., and Sicheri, F. (2018) A Structure-Based Strategy for Engineering Selective Ubiquitin Variant Inhibitors of Skp1-Cul1-F-Box Ubiquitin Ligases. Structure. 10.1016/j.str.2018.06.004
Gorelik, A., Illes, K., Bui, K. Huy, and Nagar, B. (2022) Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase. Proc Natl Acad Sci U S A. 119, e2203518119
Goris, M., Magin, R. S., Foyn, H., Myklebust, L. M., Varland, S., Ree, R., Drazic, A., Bhambra, P., Støve, S. I., Baumann, M., Haug, B. Erik, Marmorstein, R., and Arnesen, T. (2018) Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80. Proc Natl Acad Sci U S A. 115, 4405-4410
Gottlieb, L., and Marmorstein, R. (2018) Structure of Human NatA and Its Regulation by the Huntingtin Interacting Protein HYPK. Structure. 10.1016/j.str.2018.04.003
Grasty, K. C., Guzik, C., D'Lauro, E. J., Padrick, S. B., Beld, J., and Loll, P. J. (2023) Structure of VanS from vancomycin-resistant enterococci: A sensor kinase with weak ATP binding.. J Biol Chem. 299, 103001
Green, M. N., Gangwar, S. Pal, Michard, E., Simon, A. A., Portes, M. Teresa, Barbosa-Caro, J., Wudick, M. M., Lizzio, M. A., Klykov, O., Yelshanskaya, M. V., Feijó, J. A., and Sobolevsky, A. I. (2021) Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4. Mol Cell. 10.1016/j.molcel.2021.05.025
Grell, T. A. J., Kincannon, W. M., Bruender, N. A., Blaesi, E. J., Krebs, C., Bandarian, V., and Drennan, C. L. (2018) Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. J Biol Chem. 10.1074/jbc.RA118.005369
Grigg, J. C., and Ke, A. (2013) Structural determinants for geometry and information decoding of tRNA by T box leader RNA. Structure. 21, 2025-32
Grudzien-Nogalska, E., Wu, Y., Jiao, X., Cui, H., Mateyak, M. K., Hart, R. P., Tong, L., and Kiledjian, M. (2019) Structural and mechanistic basis of mammalian Nudt12 RNA deNADding. Nat Chem Biol. 15, 575-582
Guan, R., Dai, H., Han, D., Harrison, S. C., and Kirchhausen, T. (2010) Structure of the PTEN-like region of auxilin, a detector of clathrin-coated vesicle budding. Structure. 18, 1191-8
Guettler, S., LaRose, J., Petsalaki, E., Gish, G., Scotter, A., Pawson, T., Rottapel, R., and Sicheri, F. (2011) Structural basis and sequence rules for substrate recognition by Tankyrase explain the basis for cherubism disease. Cell. 147, 1340-54
Guo, X., Schmiege, P., Assafa, T. E., Wang, R., Xu, Y., Donnelly, L., Fine, M., Ni, X., Jiang, J., Millhauser, G., Feng, L., and Li, X. (2022) Structure and mechanism of human cystine exporter cystinosin. Cell. 185, 3739-3752.e18

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