Publications

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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
Fuse, S., Tsukamoto, H., Yuan, Y., Wang, T. - S. Andrew, Zhang, Y., Bolla, M., Walker, S., Sliz, P., and Kahne, D. (2010) Functional and structural analysis of a key region of the cell wall inhibitor moenomycin. ACS Chem Biol. 5, 701-11
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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
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
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
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
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
Gallant, J. P., Hicks, D., Shi, K., Moeller, N. H., Hoppe, B., Lake, E. W., Baehr, C., Pravetoni, M., Aihara, H., and LeBeau, A. M. (2024) Identification and biophysical characterization of a novel domain-swapped camelid antibody specific for fentanyl. J Biol Chem. 300, 107502
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
Gama, F. H. de Souza, Dutra, L. A., Hawgood, M., Reis, C. Vinícius, Serafim, R. A. M., Ferreira, M. A., Teodoro, B. V. M., Takarada, J. Emi, Santiago, A. S., Balourdas, D. - I., Nilsson, A. - S., Urien, B., Almeida, V. M., Gileadi, C., Ramos, P. Z., Salmazo, A., Vasconcelos, S. N. S., Cunha, M. R., Mueller, S., Knapp, S., Massirer, K. B., Elkins, J. M., Gileadi, O., Mascarello, A., Lemmens, B. B. L. G., Guimarães, C. R. W., Azevedo, H., and Couñago, R. M. (2024) Novel Dihydropteridinone Derivatives As Potent Inhibitors of the Understudied Human Kinases Vaccinia-Related Kinase 1 and Casein Kinase 1δ/ε.. J Med Chem. 67, 8609-8629
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
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
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
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
Gao, A., Vasilyev, N., Kaushik, A., Duan, W., and Serganov, A. (2020) Principles of RNA and nucleotide discrimination by the RNA processing enzyme RppH. Nucleic Acids Res. 10.1093/nar/gkaa024
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

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