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Shaban, N. M., Shi, K., Lauer, K. V., Carpenter, M. A., Richards, C. M., Salamango, D., Wang, J., Lopresti, M. W., Banerjee, S., Levin-Klein, R., Brown, W. L., Aihara, H., and Harris, R. S. (2018) The Antiviral and Cancer Genomic DNA Deaminase APOBEC3H Is Regulated by an RNA-Mediated Dimerization Mechanism. Mol Cell. 69, 75-86.e9
Shaban, N. M., Shi, K., Li, M., Aihara, H., and Harris, R. S. (2016) 1.92 Angstrom Zinc-Free APOBEC3F Catalytic Domain Crystal Structure. J Mol Biol. 428, 2307-16
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
Shah, M., Taylor, V. L., Bona, D., Tsao, Y., Stanley, S. Y., Pimentel-Elardo, S. M., McCallum, M., Bondy-Denomy, J., P Howell, L., Nodwell, J. R., Davidson, A. R., Moraes, T. F., and Maxwell, K. L. (2021) A phage-encoded anti-activator inhibits quorum sensing in Pseudomonas aeruginosa. Mol Cell. 81, 571-583.e6
Shan, C. - M., Wang, J., Xu, K., Chen, H., Yue, J. - X., Andrews, S., Moresco, J. J., Yates, J. R., Nagy, P. L., Tong, L., and Jia, S. (2016) A histone H3K9M mutation traps histone methyltransferase Clr4 to prevent heterochromatin spreading. Elife. 10.7554/eLife.17903
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., Ramachandran, S., Tulsian, N., Radhakrishnan, S., Jobichen, C., and Sivaraman, J. (2022) A novel allosteric site employs a conserved inhibition mechanism in human kidney-type glutaminase. FEBS J. 10.1111/febs.16658
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
Shanmugam, G., Minko, I. G., Banerjee, S., Christov, P. P., Kozekov, I. D., Rizzo, C. J., R Lloyd, S., Egli, M., and Stone, M. P. (2013) Ring-opening of the γ-OH-PdG adduct promotes error-free bypass by the Sulfolobus solfataricus DNA polymerase Dpo4.. Chem Res Toxicol. 26, 1348-60
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, S., Grudzien-Nogalska, E., Hamilton, K., Jiao, X., Yang, J., Tong, L., and Kiledjian, M. (2020) Mammalian Nudix proteins cleave nucleotide metabolite caps on RNAs. Nucleic Acids Res. 10.1093/nar/gkaa402
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
Sharma, S., Yang, J., Doamekpor, S. K., Grudizen-Nogalska, E., Tong, L., and Kiledjian, M. (2022) Identification of a novel deFADding activity in human, yeast and bacterial 5' to 3' exoribonucleases. Nucleic Acids Res. 50, 8807-8817
Sharon, I., McKay, G. A., Nguyen, D., and T Schmeing, M. (2023) Discovery of cyanophycin dipeptide hydrolase enzymes suggests widespread utility of the natural biopolymer cyanophycin. Proc Natl Acad Sci U S A. 120, e2216547120
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
Shatalin, K., Nuthanakanti, A., Kaushik, A., Shishov, D., Peselis, A., Shamovsky, I., Pani, B., Lechpammer, M., Vasilyev, N., Shatalina, E., Rebatchouk, D., Mironov, A., Fedichev, P., Serganov, A., and Nudler, E. (2021) Inhibitors of bacterial HS biogenesis targeting antibiotic resistance and tolerance. Science. 372, 1169-1175
Shechner, D. M., Grant, R. A., Bagby, S. C., Koldobskaya, Y., Piccirilli, J. A., and Bartel, D. P. (2009) Crystal structure of the catalytic core of an RNA-polymerase ribozyme. Science. 326, 1271-5
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
Shek, R., Dattmore, D. A., Stives, D. P., Jackson, A. L., Chatfield, C. H., Hicks, K. A., and French, J. B. (2017) Structural and functional basis for targeting Campylobacter jejuni agmatine deiminase to overcome antibiotic resistance. Biochemistry. 10.1021/acs.biochem.7b00982
Shelke, S. A., Shao, Y., Laski, A., Koirala, D., Weissman, B. P., Fuller, J. R., Tan, X., Constantin, T. P., Waggoner, A. S., Bruchez, M. P., Armitage, B. A., and Piccirilli, J. A. (2018) Structural basis for activation of fluorogenic dyes by an RNA aptamer lacking a G-quadruplex motif. Nat Commun. 9, 4542
Shelton, C. L., Conrady, D. G., and Herr, A. B. (2017) Functional consequences of B-repeat sequence variation in the staphylococcal biofilm protein Aap: deciphering the assembly code. Biochem J. 474, 427-443

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