Publications

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Soragni, A., Yousefi, S., Stoeckle, C., Soriaga, A. B., Sawaya, M. R., Kozlowski, E., Schmid, I., Radonjic-Hoesli, S., Boutet, S., Williams, G. J., Messerschmidt, M., M Seibert, M., Cascio, D., Zatsepin, N. A., Burghammer, M., Riekel, C., Colletier, J. - P., Riek, R., Eisenberg, D. S., and Simon, H. - U. (2015) Toxicity of eosinophil MBP is repressed by intracellular crystallization and promoted by extracellular aggregation. Mol Cell. 57, 1011-21
Soragni, A., Janzen, D. M., Johnson, L. M., Lindgren, A. G., Nguyen, A. Thai- Quynh, Tiourin, E., Soriaga, A. B., Lu, J., Jiang, L., Faull, K. F., Pellegrini, M., Memarzadeh, S., and Eisenberg, D. S. (2016) A Designed Inhibitor of p53 Aggregation Rescues p53 Tumor Suppression in Ovarian Carcinomas. Cancer Cell. 29, 90-103
Soriaga, A. B., Sangwan, S., Macdonald, R., Sawaya, M. R., and Eisenberg, D. (2016) Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets. J Phys Chem B. 120, 5810-6
Soriano, E. V., Zhang, Y., Colabroy, K. L., Sanders, J. M., Settembre, E. C., Dorrestein, P. C., Begley, T. P., and Ealick, S. E. (2013) Active-site models for complexes of quinolinate synthase with substrates and intermediates. Acta Crystallogr D Biol Crystallogr. 69, 1685-96
Soriano, E. V., Rajashankar, K. R., Hanes, J. W., Bale, S., Begley, T. P., and Ealick, S. E. (2008) Structural similarities between thiamin-binding protein and thiaminase-I suggest a common ancestor. Biochemistry. 47, 1346-57
Soriano, E. V., Clark, V. C., and Ealick, S. E. (2007) Structures of human deoxycytidine kinase product complexes. Acta Crystallogr D Biol Crystallogr. 63, 1201-7
Sosa, B. A., Rothballer, A., Kutay, U., and Schwartz, T. U. (2012) LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins. Cell. 149, 1035-47
Sosa, B. A., F Demircioglu, E., Chen, J. Z., Ingram, J., Ploegh, H. L., and Schwartz, T. U. (2014) How lamina-associated polypeptide 1 (LAP1) activates Torsin. Elife. 3, e03239
Sotomayor, M., Weihofen, W. A., Gaudet, R., and Corey, D. P. (2012) Structure of a force-conveying cadherin bond essential for inner-ear mechanotransduction. Nature. 492, 128-32
Sotomayor, M., Weihofen, W. A., Gaudet, R., and Corey, D. P. (2010) Structural determinants of cadherin-23 function in hearing and deafness. Neuron. 66, 85-100
Soule, J., Gnann, A. D., Gonzalez, R., Parker, M. J., McKenna, K. C., Nguyen, S. V., Phan, N. T., Wicht, D. K., and Dowling, D. P. (2019) Structure and function of the two-component flavin-dependent methanesulfinate monooxygenase within bacterial sulfur assimilation. Biochem Biophys Res Commun. 10.1016/j.bbrc.2019.11.008
Spicer, T. P., Jiang, J., Taylor, A. B., Choi, J. Yong, P Hart, J., Roush, W. R., Fields, G. B., Hodder, P. S., and Minond, D. (2014) Characterization of selective exosite-binding inhibitors of matrix metalloproteinase 13 that prevent articular cartilage degradation in vitro. J Med Chem. 57, 9598-611
Spiegelman, L., Bahn-Suh, A., Montaño, E. T., Zhang, L., Hura, G. L., Patras, K. A., Kumar, A., F Tezcan, A., Nizet, V., Tsutakawa, S. E., and Ghosh, P. (2022) Strengthening of enterococcal biofilms by Esp. PLoS Pathog. 18, e1010829
Srivastava, D., Gowribidanur-Chinnaswamy, P., Gaur, P., Spies, M., Swaroop, A., and Artemyev, N. O. (2024) Molecular basis of CRX/DNA recognition and stoichiometry at the Ret4 response element. Structure. 10.1016/j.str.2024.07.004
Srivastava, D., Singh, R. K., Moxley, M. A., Henzl, M. T., Becker, D. F., and Tanner, J. J. (2012) The three-dimensional structural basis of type II hyperprolinemia. J Mol Biol. 420, 176-89
St-Cyr, D., Ceccarelli, D. F., Orlicky, S., van der Sloot, A. M., Tang, X., Kelso, S., Moore, S., James, C., Posternak, G., Coulombe-Huntington, J., Bertomeu, T., Marinier, A., Sicheri, F., and Tyers, M. (2021) Identification and optimization of molecular glue compounds that inhibit a noncovalent E2 enzyme-ubiquitin complex. Sci Adv. 7, eabi5797
Stabach, P. R., Simonović, I., Ranieri, M. A., Aboodi, M. S., Steitz, T. A., Simonovic, M., and Morrow, J. S. (2009) The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties. Blood. 113, 5377-84
Stafford, R. L., Tang, M. - Y., Sawaya, M. R., Phillips, M. L., and Bowie, J. U. (2011) Crystal structure of the central coiled-coil domain from human liprin-β2.. Biochemistry. 50, 3807-15
Stafford, R. L., Hinde, E., Knight, M. Jane, Pennella, M. A., Ear, J., Digman, M. A., Gratton, E., and Bowie, J. U. (2011) Tandem SAM domain structure of human Caskin1: a presynaptic, self-assembling scaffold for CASK. Structure. 19, 1826-36
Stanek, K. A., Patterson-West, J., Randolph, P. S., and Mura, C. (2017) Crystal structure and RNA-binding properties of an Hfq homolog from the deep-branching Aquificae: conservation of the lateral RNA-binding mode. Acta Crystallogr D Struct Biol. 73, 294-315
Stanley, B. J., Ehrlich, E. S., Short, L., Yu, Y., Xiao, Z., Yu, X. - F., and Xiong, Y. (2008) Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. J Virol. 82, 8656-63
Stanley, R. E., Blaha, G., Grodzicki, R. L., Strickler, M. D., and Steitz, T. A. (2010) The structures of the anti-tuberculosis antibiotics viomycin and capreomycin bound to the 70S ribosome. Nat Struct Mol Biol. 17, 289-93
Steimbach, R. R., Herbst-Gervasoni, C. J., Lechner, S., Stewart, T. Murray, Klinke, G., Ridinger, J., Géraldy, M. N. E., Tihanyi, G., Foley, J. R., Uhrig, U., Kuster, B., Poschet, G., Casero, R. A., Médard, G., Oehme, I., Christianson, D. W., Gunkel, N., and Miller, A. K. (2022) Aza-SAHA Derivatives Are Selective Histone Deacetylase 10 Chemical Probes That Inhibit Polyamine Deacetylation and Phenocopy HDAC10 Knockout. J Am Chem Soc. 144, 18861-18875
Stein, B. J., Grant, R. A., Sauer, R. T., and Baker, T. A. (2016) Structural Basis of an N-Degron Adaptor with More Stringent Specificity. Structure. 24, 232-42
Stella, S., Cascio, D., and Johnson, R. C. (2010) The shape of the DNA minor groove directs binding by the DNA-bending protein Fis. Genes Dev. 24, 814-26

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