Publications

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Senturia, R., Faller, M., Yin, S., Loo, J. A., Cascio, D., Sawaya, M. R., Hwang, D., Clubb, R. T., and Guo, F. (2010) Structure of the dimerization domain of DiGeorge critical region 8. Protein Sci. 19, 1354-65
Seo, M., and Lee, Y. - H. (2014) PFKFB3 regulates oxidative stress homeostasis via its S-glutathionylation in cancer. J Mol Biol. 426, 830-42
Seo, M., Kim, J. - D., Neau, D., Sehgal, I., and Lee, Y. - H. (2011) Structure-based development of small molecule PFKFB3 inhibitors: a framework for potential cancer therapeutic agents targeting the Warburg effect. PLoS One. 6, e24179
Serafim, R. A. M., Santiago, Ada Silva, Schwalm, M. P., Hu, Z., Reis, C. V. Dos, Takarada, J. E., Mezzomo, P., Massirer, K. B., Kudolo, M., Gerstenecker, S., Chaikuad, A., Zender, L., Knapp, S., Laufer, S., Couñago, R. M., and Gehringer, M. (2022) Development of the First Covalent Monopolar Spindle Kinase 1 (MPS1/TTK) Inhibitor. J Med Chem. 65, 3173-3192
Serafim, R. A. M., Gama, F. H. de Souza, Dutra, L. A., Reis, C. V. Dos, Vasconcelos, S. N. S., Santiago, Ada Silva, Takarada, J. E., Di Pillo, F., Azevedo, H., Mascarello, A., Elkins, J. M., Massirer, K. B., Gileadi, O., Guimarães, C. R. W., and Couñago, R. M. (2019) Development of Pyridine-based Inhibitors for the Human Vaccinia-related Kinases 1 and 2. ACS Med Chem Lett. 10, 1266-1271
Serganov, A., Huang, L., and Patel, D. J. (2009) Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch. Nature. 458, 233-7
Serganov, A., Huang, L., and Patel, D. J. (2008) Structural insights into amino acid binding and gene control by a lysine riboswitch. Nature. 455, 1263-7
Sethi, D. K., Gordo, S., Schubert, D. A., and Wucherpfennig, K. W. (2013) Crossreactivity of a human autoimmune TCR is dominated by a single TCR loop. Nat Commun. 4, 2623
Setser, J. W., Heemstra, J. R., Walsh, C. T., and Drennan, C. L. (2014) Crystallographic evidence of drastic conformational changes in the active site of a flavin-dependent N-hydroxylase. Biochemistry. 53, 6063-77
Setser, J. Wayne (2014) Conformational Dynamics Control Catalysis in Disparate Systems: Structural Insights from DNA Repair and Antibiotic Biosynthetic Enzymes. Ph.D. thesis, Massachusetts Institute of Technology, Cambridge, MA
Settembre, E. C., Dorrestein, P. C., Zhai, H., Chatterjee, A., McLafferty, F. W., Begley, T. P., and Ealick, S. E. (2004) Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex. Biochemistry. 43, 11647-57
Settembre, E. C., Dorrestein, P. C., Park, J. - H., Augustine, A. M., Begley, T. P., and Ealick, S. E. (2003) Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis. Biochemistry. 42, 2971-81
Sever, N., Miličić, G., Bodnar, N. O., Wu, X., and Rapoport, T. A. (2020) Mechanism of Lamellar Body Formation by Lung Surfactant Protein B. Mol Cell. 10.1016/j.molcel.2020.10.042
Sha, F., Gencer, E. Basak, Georgeon, S., Koide, A., Yasui, N., Koide, S., and Hantschel, O. (2013) Dissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domains. Proc Natl Acad Sci U S A. 110, 14924-9
Sha, F., Kurosawa, K., Glasser, E., Ketavarapu, G., Albazzaz, S., Koide, A., and Koide, S. (2023) Monobody Inhibitor Selective to the Phosphatase Domain of SHP2 and its Use as a Probe for Quantifying SHP2 Allosteric Regulation. J Mol Biol. 435, 168010
Shaban, N. M., Shi, K., Lauer, K. V., Carpenter, M. A., Richards, C. M., Salamango, D., Wang, J., Lopresti, M. W., Banerjee, S., Levin-Klein, R., Brown, W. L., Aihara, H., and Harris, R. S. (2018) The Antiviral and Cancer Genomic DNA Deaminase APOBEC3H Is Regulated by an RNA-Mediated Dimerization Mechanism. Mol Cell. 69, 75-86.e9
Shaban, N. M., Shi, K., Li, M., Aihara, H., and Harris, R. S. (2016) 1.92 Angstrom Zinc-Free APOBEC3F Catalytic Domain Crystal Structure. J Mol Biol. 428, 2307-16
Shabdar, S., Anaclet, B., Castineiras, A. Garcia, Desir, N., Choe, N., Crane, E. J., and Sazinsky, M. H. (2021) Structural and Kinetic Characterization of Hyperthermophilic NADH-Dependent Persulfide Reductase from . Archaea. 2021, 8817136
Shah, M., Taylor, V. L., Bona, D., Tsao, Y., Stanley, S. Y., Pimentel-Elardo, S. M., McCallum, M., Bondy-Denomy, J., P Howell, L., Nodwell, J. R., Davidson, A. R., Moraes, T. F., and Maxwell, K. L. (2021) A phage-encoded anti-activator inhibits quorum sensing in Pseudomonas aeruginosa. Mol Cell. 81, 571-583.e6
Shan, C. - M., Wang, J., Xu, K., Chen, H., Yue, J. - X., Andrews, S., Moresco, J. J., Yates, J. R., Nagy, P. L., Tong, L., and Jia, S. (2016) A histone H3K9M mutation traps histone methyltransferase Clr4 to prevent heterochromatin spreading. Elife. 10.7554/eLife.17903
Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., and Li, F. (2020) Structural basis of receptor recognition by SARS-CoV-2. Nature. 10.1038/s41586-020-2179-y
Shankar, S., Ramachandran, S., Tulsian, N., Radhakrishnan, S., Jobichen, C., and Sivaraman, J. (2022) A novel allosteric site employs a conserved inhibition mechanism in human kidney-type glutaminase. FEBS J. 10.1111/febs.16658
Shanmugam, G., Minko, I. G., Banerjee, S., Christov, P. P., Kozekov, I. D., Rizzo, C. J., R Lloyd, S., Egli, M., and Stone, M. P. (2013) Ring-opening of the γ-OH-PdG adduct promotes error-free bypass by the Sulfolobus solfataricus DNA polymerase Dpo4.. Chem Res Toxicol. 26, 1348-60
Shao, Y., Huang, H., Qin, D., Li, N. - S., Koide, A., Staley, J. P., Koide, S., Kossiakoff, A. A., and Piccirilli, J. A. (2016) Specific Recognition of a Single-Stranded RNA Sequence by a Synthetic Antibody Fragment. J Mol Biol. 428, 4100-4114
Sharkey, M. A., Oliveira, T. F., Engel, P. C., and Khan, A. R. (2013) Structure of NADP(+)-dependent glutamate dehydrogenase from Escherichia coli--reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases. FEBS J. 280, 4681-92

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