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A Saraswati, P., Relitti, N., Brindisi, M., Osko, J. D., Chemi, G., Federico, S., Grillo, A., Brogi, S., McCabe, N. H., Turkington, R. C., Ibrahim, O., O'Sullivan, J., Lamponi, S., Ghanim, M., Kelly, V. P., Zisterer, D., Amet, R., Barroeta, P. Hannon, Vanni, F., Ulivieri, C., Herp, D., Sarno, F., Di Costanzo, A., Saccoccia, F., Ruberti, G., Jung, M., Altucci, L., Gemma, S., Butini, S., Christianson, D. W., and Campiani, G. (2020) Spiroindoline-Capped Selective HDAC6 Inhibitors: Design, Synthesis, Structural Analysis, and Biological Evaluation. ACS Med Chem Lett. 11, 2268-2276
Saxton, R. A., Knockenhauer, K. E., Wolfson, R. L., Chantranupong, L., Pacold, M. E., Wang, T., Schwartz, T. U., and Sabatini, D. M. (2016) Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. Science. 351, 53-8
Schaefer, K., Owens, T. W., Page, J. E., Santiago, M., Kahne, D., and Walker, S. (2020) Structure and reconstitution of a hydrolase complex that may release peptidoglycan from the membrane after polymerization. Nat Microbiol. 10.1038/s41564-020-00808-5
Schaefer, K., Owens, T. W., Kahne, D., and Walker, S. (2018) Substrate Preferences Establish the Order of Cell Wall Assembly in Staphylococcus aureus. J Am Chem Soc. 140, 2442-2445
Schauder, C. M., Wu, X., Saheki, Y., Narayanaswamy, P., Torta, F., Wenk, M. R., De Camilli, P., and Reinisch, K. M. (2014) Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. Nature. 510, 552-5
Schiltz, C. J., Lee, A., Partlow, E. A., Hosford, C. J., and Chappie, J. S. (2019) Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage. Nucleic Acids Res. 47, 9448-9463
Schirle, N. T., Sheu-Gruttadauria, J., and MacRae, I. J. (2014) Structural basis for microRNA targeting. Science. 346, 608-13
Schlieker, C., Weihofen, W. A., Frijns, E., Kattenhorn, L. M., Gaudet, R., and Ploegh, H. L. (2007) Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes. Mol Cell. 25, 677-87
T Schmeing, M., Moore, P. B., and Steitz, T. A. (2003) Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. RNA. 9, 1345-52
Schmidt, F. I., Lu, A., Chen, J. W., Ruan, J., Tang, C., Wu, H., and Ploegh, H. L. (2016) A single domain antibody fragment that recognizes the adaptor ASC defines the role of ASC domains in inflammasome assembly. J Exp Med. 213, 771-90
Schmier, B. J., Nelersa, C. M., and Malhotra, A. (2017) Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA. Sci Rep. 7, 11085
Schormann, N., Banerjee, S., Ricciardi, R., and Chattopadhyay, D. (2013) Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 69, 1328-34
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
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., 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
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
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
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

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