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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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
Seo, M., and Lee, Y. - H. (2014) PFKFB3 regulates oxidative stress homeostasis via its S-glutathionylation in cancer. J Mol Biol. 426, 830-42
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
Semavina, M., Saha, N., Kolev, M. V., Goldgur, Y., Giger, R. J., Himanen, J. P., and Nikolov, D. B. (2011) Crystal structure of the Nogo-receptor-2. Protein Sci. 20, 684-9
Sekiyama, N., Arthanari, H., Papadopoulos, E., Rodriguez-Mias, R. A., Wagner, G., and Léger-Abraham, M. (2015) Molecular mechanism of the dual activity of 4EGI-1: Dissociating eIF4G from eIF4E but stabilizing the binding of unphosphorylated 4E-BP1. Proc Natl Acad Sci U S A. 112, E4036-45
Seidler, P. Matthew, Boyer, D. R., Murray, K. A., Yang, T. P., Bentzel, M., Sawaya, M. R., Rosenberg, G., Cascio, D., Williams, C. Kazu, Newell, K. L., Ghetti, B., DeTure, M. A., Dickson, D. W., Vinters, H. V., and Eisenberg, D. S. (2019) Structure-based inhibitors halt prion-like seeding by Alzheimer's disease-and tauopathy-derived brain tissue samples. J Biol Chem. 294, 16451-16464
Seetharaman, S. V., Taylor, A. B., Holloway, S., and P Hart, J. (2010) Structures of mouse SOD1 and human/mouse SOD1 chimeras. Arch Biochem Biophys. 503, 183-90
Seely, S. M., Parajuli, N. P., De Tarafder, A., Ge, X., Sanyal, S., and Gagnon, M. G. (2023) Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome. Nat Commun. 14, 4666
Seegar, T. C. M., Killingsworth, L. B., Saha, N., Meyer, P. A., Patra, D., Zimmerman, B., Janes, P. W., Rubinstein, E., Nikolov, D. B., Skiniotis, G., Kruse, A. C., and Blacklow, S. C. (2017) Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10.. Cell. 171, 1638-1648.e7
Seckute, J., McCloskey, D. E., H Thomas, J., Secrist, J. A., Pegg, A. E., and Ealick, S. E. (2011) Binding and inhibition of human spermidine synthase by decarboxylated S-adenosylhomocysteine. Protein Sci. 20, 1836-44

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