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Schreiter, E. R., Sintchak, M. D., Guo, Y., Chivers, P. T., Sauer, R. T., and Drennan, C. L. (2003) Crystal structure of the nickel-responsive transcription factor NikR. Nat Struct Biol. 10, 794-9
Schuermann, J. P., Tan, A., Tanner, J. J., and Henzl, M. T. (2010) Structure of avian thymic hormone, a high-affinity avian beta-parvalbumin, in the Ca2+-free and Ca2+-bound states. J Mol Biol. 397, 991-1002
Schuermann, J. (2022) Data Flow at NE-CAT. 2022 Workshop on High Data Rate Macromolecular Crystallography (HDRMX)
Schuhmacher, M. Kirstin, Beldar, S., Khella, M. S., Bröhm, A., Ludwig, J., Tempel, W., Weirich, S., Min, J., and Jeltsch, A. (2020) Sequence specificity analysis of the SETD2 protein lysine methyltransferase and discovery of a SETD2 super-substrate. Commun Biol. 3, 511
Schureck, M. A. (2016) Structural and Functional Studies of a Toxin-Antitoxin System Involved in Translational Inhibition. Ph.D. thesis, Emory University, Atlanta, Georgia, PhD, 273
Schureck, M. A., Dunkle, J. A., Maehigashi, T., Miles, S. J., and Dunham, C. M. (2015) Defining the mRNA recognition signature of a bacterial toxin protein. Proc Natl Acad Sci U S A. 112, 13862-7
Schureck, M. A., Meisner, J., Hoffer, E. D., Wang, D., Onuoha, N., Cho, S. Ei, Lollar, P., and Dunham, C. M. (2019) Structural basis of transcriptional regulation by the HigA antitoxin. Mol Microbiol. 10.1111/mmi.14229
Schureck, M. A., Maehigashi, T., Miles, S. J., Marquez, J., Cho, S. Ei, Erdman, R., and Dunham, C. M. (2014) Structure of the Proteus vulgaris HigB-(HigA)2-HigB toxin-antitoxin complex. J Biol Chem. 289, 1060-70
Schürpf, T., Chen, Q., Liu, J. -huan, Wang, R., Springer, T. A., and Wang, J. -huai (2012) The RGD finger of Del-1 is a unique structural feature critical for integrin binding. FASEB J. 26, 3412-20
Schwartz, J., Son, J., Brugger, C., and Deaconescu, A. M. (2021) Phospho-dependent signaling during the general stress response by the atypical response regulator and ClpXP adaptor RssB. Protein Sci. 10.1002/pro.4047
Schwer, B., Garg, A., Jacewicz, A., and Shuman, S. (2021) Genetic screen for suppression of transcriptional interference identifies a gain-of-function mutation in Pol2 termination factor Seb1. Proc Natl Acad Sci U S A. 10.1073/pnas.2108105118
Schwer, B., Ghosh, A., Sanchez, A. M., Lima, C. D., and Shuman, S. (2015) Genetic and structural analysis of the essential fission yeast RNA polymerase II CTD phosphatase Fcp1. RNA. 21, 1135-46
Sciara, G., Clarke, O. B., Tomasek, D., Kloss, B., Tabuso, S., Byfield, R., Cohn, R., Banerjee, S., Rajashankar, K. R., Slavkovic, V., Graziano, J. H., Shapiro, L., and Mancia, F. (2014) Structural basis for catalysis in a CDP-alcohol phosphotransferase. Nat Commun. 5, 4068
Scott, D. C., Monda, J. K., Bennett, E. J., J Harper, W., and Schulman, B. A. (2011) N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex. Science. 334, 674-8
Scott, D. C., Sviderskiy, V. O., Monda, J. K., Lydeard, J. R., Cho, S. Ei, J Harper, W., and Schulman, B. A. (2014) Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8. Cell. 157, 1671-84
Scott, D. C., Monda, J. K., Grace, C. R. R., Duda, D. M., Kriwacki, R. W., Kurz, T., and Schulman, B. A. (2010) A dual E3 mechanism for Rub1 ligation to Cdc53. Mol Cell. 39, 784-96
Scrima, A., Konícková, R., Czyzewski, B. K., Kawasaki, Y., Jeffrey, P. D., Groisman, R., Nakatani, Y., Iwai, S., Pavletich, N. P., and Thomä, N. H. (2008) Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex. Cell. 135, 1213-23
Sea, K. W., Taylor, A. B., Thomas, S. T., Liba, A., Bergman, I. B., Holloway, S. P., Cao, X., Gralla, E. B., Valentine, J. S., P Hart, J., and Galaleldeen, A. (2021) A pH Switch Controls Zinc Binding in Tomato Copper-Zinc Superoxide Dismutase. Biochemistry. 60, 1597-1608
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
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
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
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
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
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
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

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