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Szulik, M. W., Pallan, P. S., Nocek, B., Voehler, M., Banerjee, S., Brooks, S., Joachimiak, A., Egli, M., Eichman, B. F., and Stone, M. P. (2015) Differential stabilities and sequence-dependent base pair opening dynamics of Watson-Crick base pairs with 5-hydroxymethylcytosine, 5-formylcytosine, or 5-carboxylcytosine. Biochemistry. 54, 1294-305
Szewczyk, M. M., Ishikawa, Y., Organ, S., Sakai, N., Li, F., Halabelian, L., Ackloo, S., Couzens, A. L., Eram, M., Dilworth, D., Fukushi, H., Harding, R., Seña, C. C. Dela, Sugo, T., Hayashi, K., McLeod, D., Zepeda, C., Aman, A., Sánchez-Osuna, M., Bonneil, E., Takagi, S., Al-awar, R., Tyers, M., Richard, S., Takizawa, M., Gingras, A. - C., Arrowsmith, C. H., Vedadi, M., Brown, P. J., Nara, H., and Barsyte-Lovejoy, D. (2020) Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response. Nat Commun. 11, 2396
Sysoeva, T. A., Bane, L. B., Xiao, D. Y., Bose, B., Chilton, S. S., Gaudet, R., and Burton, B. M. (2015) Structural characterization of the late competence protein ComFB from Bacillus subtilis. Biosci Rep. 10.1042/BSR20140174
Sydor, A. M., Jost, M., Ryan, K. S., Turo, K. E., Douglas, C. D., Drennan, C. L., and Zamble, D. B. (2013) Metal binding properties of Escherichia coli YjiA, a member of the metal homeostasis-associated COG0523 family of GTPases. Biochemistry. 52, 1788-1801
Svetlov, M. S., Plessa, E., Chen, C. - W., Bougas, A., Krokidis, M. G., Dinos, G. P., and Polikanov, Y. (2019) High-resolution crystal structures of ribosome-bound chloramphenicol and erythromycin provide the ultimate basis for their competition. RNA. 10.1261/rna.069260.118
Svetlov, M. S., Syroegin, E. A., Aleksandrova, E. V., Atkinson, G. C., Gregory, S. T., Mankin, A. S., and Polikanov, Y. S. (2021) Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance. Nat Chem Biol. 10.1038/s41589-020-00715-0
Suzuki, T., Miller, C., Guo, L. - T., Ho, J. M. L., Bryson, D. I., Wang, Y. - S., Liu, D. R., and Söll, D. (2017) Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase. Nat Chem Biol. 10.1038/nchembio.2497
Suzuki, C., Garces, R. G., Edmonds, K. A., Hiller, S., Hyberts, S. G., Marintchev, A., and Wagner, G. (2008) PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domains. Proc Natl Acad Sci U S A. 105, 3274-9
Suwa, Y., Gu, J., Baranovskiy, A. G., Babayeva, N. D., Pavlov, Y. I., and Tahirov, T. H. (2015) Crystal Structure of the Human Pol α B Subunit in Complex with the C-terminal Domain of the Catalytic Subunit.. J Biol Chem. 290, 14328-37
Suslov, N. B., DasGupta, S., Huang, H., Fuller, J. R., Lilley, D. M. J., Rice, P. A., and Piccirilli, J. A. (2015) Crystal structure of the Varkud satellite ribozyme. Nat Chem Biol. 11, 840-6
Susa, K. J., Seegar, T. Cm, Blacklow, S. C., and Kruse, A. C. (2020) A dynamic interaction between CD19 and the tetraspanin CD81 controls B cell co-receptor trafficking. Elife. 10.7554/eLife.52337
Sung, R. - J., Zhang, M., Qi, Y., and Verdine, G. L. (2013) Structural and biochemical analysis of DNA helix invasion by the bacterial 8-oxoguanine DNA glycosylase MutM. J Biol Chem. 288, 10012-23
Sung, R. - J., Zhang, M., Qi, Y., and Verdine, G. L. (2012) Sequence-dependent structural variation in DNA undergoing intrahelical inspection by the DNA glycosylase MutM. J Biol Chem. 287, 18044-54
Sun, J., Paduch, M., Kim, S. - A., Kramer, R. M., Barrios, A. F., Lu, V., Luke, J., Usatyuk, S., Kossiakoff, A. A., and Tan, S. (2018) Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2. Proc Natl Acad Sci U S A. 10.1073/pnas.1805343115
Sun, X. - J., Wang, Z., Wang, L., Jiang, Y., Kost, N., T Soong, D., Chen, W. - Y., Tang, Z., Nakadai, T., Elemento, O., Fischle, W., Melnick, A., Patel, D. J., Nimer, S. D., and Roeder, R. G. (2013) A stable transcription factor complex nucleated by oligomeric AML1-ETO controls leukaemogenesis. Nature. 500, 93-7
Summers, B. J., Digianantonio, K. M., Smaga, S. S., Huang, P. - T., Zhou, K., Gerber, E. E., Wang, W., and Xiong, Y. (2019) Modular HIV-1 Capsid Assemblies Reveal Diverse Host-Capsid Recognition Mechanisms. Cell Host Microbe. 26, 203-216.e6
Sukumar, N., Chen, Z. -wei, Ferrari, D., Merli, A., Rossi, G. Luigi, Bellamy, H. D., Chistoserdov, A., Davidson, V. L., and F Mathews, S. (2006) Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis. Biochemistry. 45, 13500-10
Sukumar, N., Mathews, F. S., Langan, P., and Davidson, V. L. (2010) A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transfer. Proc Natl Acad Sci U S A. 107, 6817-22
Sukumar, N., Liu, S., Li, W., Mathews, F. S., Mitra, B., and Kandavelu, P. (2018) Structure of the monotopic membrane protein (S)-mandelate dehydrogenase at 2.2Å resolution.. Biochimie. 10.1016/j.biochi.2018.07.017
Sukumar, N., Dewanti, A., Merli, A., Rossi, G. Luigi, Mitra, B., and F Mathews, S. (2009) Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates. Acta Crystallogr D Biol Crystallogr. 65, 543-52
Sukumar, N. (2013) Crystallographic studies on B12 binding proteins in eukaryotes and prokaryotes. Biochimie. 95, 976-88
Sukumar, N., Choi, M., and Davidson, V. L. (2011) Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper. J Inorg Biochem. 105, 1638-44
Sukumar, N., Langan, P., Mathews, F. S., Jones, L. H., Thiyagarajan, P., Schoenborn, B. P., and Davidson, V. L. (2005) A preliminary time-of-flight neutron diffraction study on amicyanin from Paracoccus denitrificans. Acta Crystallogr D Biol Crystallogr. 61, 640-2
Sukumar, N. (2014) A comparative analysis on X-ray structure of cobalamin binding proteins. 23rd International Union of Crystallography (IuCr) and General Assembly, August 5–12, 2014
Sui, X., Golczak, M., Zhang, J., Kleinberg, K. A., von Lintig, J., Palczewski, K., and Kiser, P. D. (2015) Utilization of Dioxygen by Carotenoid Cleavage Oxygenases. J Biol Chem. 290, 30212-23

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