Publications

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Schormann, N., Campos, J., Motamed, R., Hayden, K. L., Gould, J. R., Green, T. J., Senkovich, O., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2020) Chlamydia trachomatis Glyceraldehyde 3-phosphate dehydrogenase: Enzyme Kinetics, High Resolution Crystal Structure and Plasminogen Binding. Protein Sci. 10.1002/pro.3975
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., 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
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
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
Schwartze, T. A., Morosky, S. A., Rosato, T. L., Henrickson, A., Lin, G., Hinck, C. S., Taylor, A. B., Olsen, S. K., Calero, G., Demeler, B., Roman, B. L., and Hinck, A. P. (2025) Molecular Basis of Interchain Disulfide Bond Formation in BMP-9 and BMP-10. J Mol Biol. 437, 168935
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., Dharuman, S., Griffith, E., Chai, S. C., Ronnebaum, J., King, M. T., Tangallapally, R., Lee, C., Gee, C. T., Yang, L., Li, Y., Loudon, V. C., Lee, H. Won, Ochoada, J., Miller, D. J., Jayasinghe, T., Paulo, J. A., Elledge, S. J., J Harper, W., Chen, T., Lee, R. E., and Schulman, B. A. (2024) Principles of paralog-specific targeted protein degradation engaging the C-degron E3 KLHDC2. Nat Commun. 15, 8829
Scott, D. C., Chittori, S., Purser, N., King, M. T., Maiwald, S. A., Churion, K., Nourse, A., Lee, C., Paulo, J. A., Miller, D. J., Elledge, S. J., J Harper, W., Kleiger, G., and Schulman, B. A. (2024) Structural basis for C-degron selectivity across KLHDCX family E3 ubiquitin ligases. Nat Commun. 15, 9899
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
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., King, M. T., Baek, K., Gee, C. T., Kalathur, R., Li, J., Purser, N., Nourse, A., Chai, S. C., Vaithiyalingam, S., Chen, T., Lee, R. E., Elledge, S. J., Kleiger, G., and Schulman, B. A. (2023) E3 ligase autoinhibition by C-degron mimicry maintains C-degron substrate fidelity. Mol Cell. 83, 770-786.e9
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

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