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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
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
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., Wilson, J. R., Hosford, C. J., Adams, M. C., Preising, S. E., DeBlasio, S. L., MacLeod, H. J., Van Eck, J., Heck, M. L., and Chappie, J. S. (2022) Polerovirus N-terminal readthrough domain structures reveal molecular strategies for mitigating virus transmission by aphids. Nat Commun. 13, 6368
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
Schiltz, C. J., Adams, M. C., and Chappie, J. S. (2020) The full-length structure of Thermus scotoductus OLD defines the ATP hydrolysis properties and catalytic mechanism of Class 1 OLD family nucleases. Nucleic Acids Res. 48, 2762-2776
Schirle, N. T., Sheu-Gruttadauria, J., and MacRae, I. J. (2014) Structural basis for microRNA targeting. Science. 346, 608-13
Schirle, N. T., Sheu-Gruttadauria, J., Chandradoss, S. D., Joo, C., and MacRae, I. J. (2015) Water-mediated recognition of t1-adenosine anchors Argonaute2 to microRNA targets. Elife. 10.7554/eLife.07646
Schirle, N. T., and MacRae, I. J. (2012) The crystal structure of human Argonaute2. Science. 336, 1037-40
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
Schmandt, N., Velisetty, P., Chalamalasetti, S. V., Stein, R. A., Bonner, R., Talley, L., Parker, M. D., Mchaourab, H. S., Yee, V. C., Lodowski, D. T., and Chakrapani, S. (2015) A chimeric prokaryotic pentameric ligand-gated channel reveals distinct pathways of activation. J Gen Physiol. 146, 323-40
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
Schmidt, H. R., Zheng, S., Gurpinar, E., Koehl, A., Manglik, A., and Kruse, A. C. (2016) Crystal structure of the human σ1 receptor.. Nature. 532, 527-30
Schmidt, A. G., Therkelsen, M. D., Stewart, S., Kepler, T. B., Liao, H. - X., M Moody, A., Haynes, B. F., and Harrison, S. C. (2015) Viral receptor-binding site antibodies with diverse germline origins. Cell. 161, 1026-1034
Schmidt, A. G., Xu, H., Khan, A. R., O'Donnell, T., Khurana, S., King, L. R., Manischewitz, J., Golding, H., Suphaphiphat, P., Carfi, A., Settembre, E. C., Dormitzer, P. R., Kepler, T. B., Zhang, R., M Moody, A., Haynes, B. F., Liao, H. - X., Shaw, D. E., and Harrison, S. C. (2013) Preconfiguration of the antigen-binding site during affinity maturation of a broadly neutralizing influenza virus antibody. Proc Natl Acad Sci U S A. 110, 264-9
Schmier, B. J., Nelersa, C. M., and Malhotra, A. (2017) Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA. Sci Rep. 7, 11085
Schmitz, K. R., Carney, D. W., Sello, J. K., and Sauer, R. T. (2014) Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery. Proc Natl Acad Sci U S A. 111, E4587-95
Schmitzberger, F., and Harrison, S. C. (2012) RWD domain: a recurring module in kinetochore architecture shown by a Ctf19-Mcm21 complex structure. EMBO Rep. 13, 216-22
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
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
Schoeffler, A. J., May, A. P., and Berger, J. M. (2010) A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function. Nucleic Acids Res. 38, 7830-44
Schormann, N., Ayres, C. A., Fry, A., Green, T. J., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2016) Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes. PLoS One. 11, e0165917
Schormann, N., Campos, J., Motamed, R., Hayden, K. L., Gould, J. R., Green, T. J., Senkovich, O., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2020) Chlamydia trachomatis Glyceraldehyde 3-phosphate dehydrogenase: Enzyme Kinetics, High Resolution Crystal Structure and Plasminogen Binding. Protein Sci. 10.1002/pro.3975
Schormann, N., Hayden, K. L., Lee, P., Banerjee, S., and Chattopadhyay, D. (2019) An overview of structure, function, and regulation of pyruvate kinases. Protein Sci. 10.1002/pro.3691

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