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Sue, A. C. - H., Mannige, R. V., Deng, H., Cao, D., Wang, C., Gándara, F., J Stoddart, F., Whitelam, S., and Yaghi, O. M. (2015) Heterogeneity of functional groups in a metal-organic framework displays magic number ratios. Proc Natl Acad Sci U S A. 112, 5591-6
Sui, X., Zhang, J., Golczak, M., Palczewski, K., and Kiser, P. D. (2016) Key Residues for Catalytic Function and Metal Coordination in a Carotenoid Cleavage Dioxygenase. J Biol Chem. 291, 19401-12
Sui, X., Kiser, P. D., Che, T., Carey, P. R., Golczak, M., Shi, W., von Lintig, J., and Palczewski, K. (2014) Analysis of carotenoid isomerase activity in a prototypical carotenoid cleavage enzyme, apocarotenoid oxygenase (ACO). J Biol Chem. 289, 12286-99
Sui, X., Weitz, A. C., Farquhar, E. R., Badiee, M., Banerjee, S., von Lintig, J., Tochtrop, G. P., Palczewski, K., Hendrich, M. P., and Kiser, P. D. (2017) Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center. Biochemistry. 56, 2836-2852
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
Sui, X., Farquhar, E. R., Hill, H. E., von Lintig, J., Shi, W., and Kiser, P. D. (2018) Preparation and characterization of metal-substituted carotenoid cleavage oxygenases. J Biol Inorg Chem. 23, 887-901
Sukumar, N., Kurinov, I., Capel, M., Withrow, J., Sukumar, S., and Davidson, V. L. (2021) Ultra-high resolution and charge-density studies on type-I copper protein, amicyanin, from Paracoccus denitrificans. Biophysical Society Annual Meeting, February 22-26, 2021
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., 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. (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
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., 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. (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
Sullivan, J. R., Lupien, A., Kalthoff, E., Hamela, C., Taylor, L., Munro, K. A., T Schmeing, M., Kremer, L., and Behr, M. A. (2021) Efficacy of epetraborole against Mycobacterium abscessus is increased with norvaline. PLoS Pathog. 17, e1009965
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
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
Sun, T., Heiden, J. A. Vander, Gao, X., Yin, J., Uttarwar, S., Liang, W. - C., Jia, G., Yadav, R., Huang, Z., Mitra, M., Halpern, W., Bender, H. S., Brightbill, H. D., Wu, Y., Lupardus, P., Ramalingam, T., and Arron, J. R. (2024) Isoform-selective TGF-β3 inhibition for systemic sclerosis.. Med. 5, 132-147.e7
Sun, Z. - W., Waybright, J. M., Beldar, S., Chen, L., Foley, C. A., Norris-Drouin, J. L., Lyu, T. - J., Dong, A., Min, J., Wang, Y. - P., James, L. I., and Wang, Y. (2022) Cdyl Deficiency Brakes Neuronal Excitability and Nociception through Promoting Kcnb1 Transcription in Peripheral Sensory Neurons. Adv Sci (Weinh). 9, e2104317
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
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
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
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

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