Publications

Found 943 results
Filters: First Letter Of Title is S  [Clear All Filters]
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
S
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., 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
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
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., 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
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
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
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
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., 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
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
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
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
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., Chew, T. Weng, Chichili, V. Priyanka R., Low, B. Chuan, and Sivaraman, J. (2024) Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP. Cell Mol Life Sci. 81, 216
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
Sharma, H., Yu, S., Kong, J., Wang, J., and Steitz, T. A. (2009) Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proc Natl Acad Sci U S A. 106, 16604-9
Sharon, I., Haque, A. S., Grogg, M., Lahiri, I., Seebach, D., Leschziner, A. E., Hilvert, D., and T Schmeing, M. (2021) Structures and function of the amino acid polymerase cyanophycin synthetase. Nat Chem Biol. 17, 1101-1110
Sharon, I., Grogg, M., Hilvert, D., and T Schmeing, M. (2022) The structure of cyanophycinase in complex with a cyanophycin degradation intermediate. Biochim Biophys Acta Gen Subj. 1866, 130217
Shechner, D. M., and Bartel, D. P. (2011) The structural basis of RNA-catalyzed RNA polymerization. Nat Struct Mol Biol. 18, 1036-42
Sheetz, J. B., Mathea, S., Karvonen, H., Malhotra, K., Chatterjee, D., Niininen, W., Perttilä, R., Preuss, F., Suresh, K., Stayrook, S. E., Tsutsui, Y., Radhakrishnan, R., Ungureanu, D., Knapp, S., and Lemmon, M. A. (2020) Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases. Mol Cell. 79, 390-405.e7
Shek, R., Hilaire, T., Sim, J., and French, J. B. (2019) Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily. Biochemistry. 58, 3280-3292

Pages