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Shen, G., Li, S., Cui, W., Liu, S., Yang, Y., Gross, M., and Li, W. (2018) Membrane Protein Structure in Live Cells: Methodology for Studying Drug Interaction by Mass Spectrometry-Based Footprinting. Biochemistry. 57, 286-294
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
Sha, F., Kurosawa, K., Glasser, E., Ketavarapu, G., Albazzaz, S., Koide, A., and Koide, S. (2023) Monobody Inhibitor Selective to the Phosphatase Domain of SHP2 and its Use as a Probe for Quantifying SHP2 Allosteric Regulation. J Mol Biol. 435, 168010
Sever, N., Miličić, G., Bodnar, N. O., Wu, X., and Rapoport, T. A. (2020) Mechanism of Lamellar Body Formation by Lung Surfactant Protein B. Mol Cell. 10.1016/j.molcel.2020.10.042
Sekiyama, N., Arthanari, H., Papadopoulos, E., Rodriguez-Mias, R. A., Wagner, G., and Léger-Abraham, M. (2015) Molecular mechanism of the dual activity of 4EGI-1: Dissociating eIF4G from eIF4E but stabilizing the binding of unphosphorylated 4E-BP1. Proc Natl Acad Sci U S A. 112, E4036-45
Seely, S. M., Parajuli, N. P., De Tarafder, A., Ge, X., Sanyal, S., and Gagnon, M. G. (2023) Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome. Nat Commun. 14, 4666
Schnabl, J., Wang, J., Hohmann, U., Gehre, M., Batki, J., Andreev, V. I., Purkhauser, K., Fasching, N., Duchek, P., Novatchkova, M., Mechtler, K., Plaschka, C., Patel, D. J., and Brennecke, J. (2021) Molecular principles of Piwi-mediated cotranscriptional silencing through the dimeric SFiNX complex. Genes Dev. 35, 392-409
Schmitzberger, F., Richter, M. M., Gordiyenko, Y., Robinson, C. V., Dadlez, M., and Westermann, S. (2017) Molecular basis for inner kinetochore configuration through RWD domain-peptide interactions. EMBO J. 36, 3458-3482
Saxton, R. A., Chantranupong, L., Knockenhauer, K. E., Schwartz, T. U., and Sabatini, D. M. (2016) Mechanism of arginine sensing by CASTOR1 upstream of mTORC1. Nature. 536, 229-33
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Rubinstein, R., Thu, C. Aye, Goodman, K. Marie, Wolcott, H. Noelle, Bahna, F., Mannepalli, S., Ahlsen, G., Chevee, M., Halim, A., Clausen, H., Maniatis, T., Shapiro, L., and Honig, B. (2015) Molecular logic of neuronal self-recognition through protocadherin domain interactions. Cell. 163, 629-42
Ruangprasert, A., Maehigashi, T., Miles, S. J., Giridharan, N., Liu, J. X., and Dunham, C. M. (2014) Mechanisms of toxin inhibition and transcriptional repression by Escherichia coli DinJ-YafQ. J Biol Chem. 289, 20559-69
Roy, R. N., Lomakin, I. B., Gagnon, M. G., and Steitz, T. A. (2015) The mechanism of inhibition of protein synthesis by the proline-rich peptide oncocin. Nat Struct Mol Biol. 22, 466-9
Román-Hernández, G., Grant, R. A., Sauer, R. T., and Baker, T. A. (2009) Molecular basis of substrate selection by the N-end rule adaptor protein ClpS. Proc Natl Acad Sci U S A. 106, 8888-93
Reßing, N., Sönnichsen, M., Osko, J. D., Schöler, A., Schliehe-Diecks, J., Skerhut, A., Borkhardt, A., Hauer, J., Kassack, M. U., Christianson, D. W., Bhatia, S., and Hansen, F. K. (2020) Multicomponent Synthesis, Binding Mode, and Structure-Activity Relationship of Selective Histone Deacetylase 6 (HDAC6) Inhibitors with Bifurcated Capping Groups. J Med Chem. 63, 10339-10351
Rechkoblit, O., Kolbanovskiy, A., Malinina, L., Geacintov, N. E., Broyde, S., and Patel, D. J. (2010) Mechanism of error-free and semitargeted mutagenic bypass of an aromatic amine lesion by Y-family polymerase Dpo4. Nat Struct Mol Biol. 17, 379-88
Ray, L. C., Das, D., Entova, S., Lukose, V., Lynch, A. J., Imperiali, B., and Allen, K. N. (2018) Membrane association of monotopic phosphoglycosyl transferase underpins function. Nat Chem Biol. 10.1038/s41589-018-0054-z
Rapp, M., Guo, Y., Reddem, E. R., Yu, J., Liu, L., Wang, P., Cerutti, G., Katsamba, P., Bimela, J. S., Bahna, F. A., Mannepalli, S. M., Zhang, B., Kwong, P. D., Huang, Y., Ho, D. D., Shapiro, L., and Sheng, Z. (2021) Modular basis for potent SARS-CoV-2 neutralization by a prevalent VH1-2-derived antibody class. Cell Rep. 10.1016/j.celrep.2021.108950
Raghuraman, H., Cordero-Morales, J. F., Jogini, V., Pan, A. C., Kollewe, A., Roux, B., and Perozo, E. (2012) Mechanism of Cd2+ coordination during slow inactivation in potassium channels. Structure. 20, 1332-42
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Price, I. R., Gaballa, A., Ding, F., Helmann, J. D., and Ke, A. (2015) Mn(2+)-sensing mechanisms of yybP-ykoY orphan riboswitches. Mol Cell. 57, 1110-1123
Porter, N. J., Shen, S., Barinka, C., Kozikowski, A. P., and Christianson, D. W. (2018) Molecular Basis for the Selective Inhibition of Histone Deacetylase 6 by a Mercaptoacetamide Inhibitor. ACS Med Chem Lett. 9, 1301-1305
Poor, C. B., Wegner, S. V., Li, H., Dlouhy, A. C., Schuermann, J. P., Sanishvili, R., Hinshaw, J. R., Riggs-Gelasco, P. J., Outten, C. E., and He, C. (2014) Molecular mechanism and structure of the Saccharomyces cerevisiae iron regulator Aft2. Proc Natl Acad Sci U S A. 111, 4043-8
Pavelich, I. J., Maehigashi, T., Hoffer, E. D., Ruangprasert, A., Miles, S. J., and Dunham, C. M. (2019) Monomeric YoeB toxin retains RNase activity but adopts an obligate dimeric form for thermal stability. Nucleic Acids Res. 10.1093/nar/gkz760
Patchett, S., Lv, Z., Rut, W., Békés, M., Drag, M., Olsen, S. K., and Huang, T. T. (2021) A molecular sensor determines the ubiquitin substrate specificity of SARS-CoV-2 papain-like protease. Cell Rep. 36, 109754
Park, M. Seul, Araya-Secchi, R., Brackbill, J. A., Phan, H. - D., Kehling, A. C., El-Wahab, E. W. Abd, Dayeh, D. M., Sotomayor, M., and Nakanishi, K. (2019) Multidomain Convergence of Argonaute during RISC Assembly Correlates with the Formation of Internal Water Clusters. Mol Cell. 75, 725-740.e6
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Osterman, I. A., Khabibullina, N. F., Komarova, E. S., Kasatsky, P., Kartsev, V. G., Bogdanov, A. A., Dontsova, O. A., Konevega, A. L., Sergiev, P. V., and Polikanov, Y. S. (2017) Madumycin II inhibits peptide bond formation by forcing the peptidyl transferase center into an inactive state. Nucleic Acids Res. 10.1093/nar/gkx413

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