Publications

Found 2721 results
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Shi, K., Moeller, N. H., Banerjee, S., McCann, J. L., Carpenter, M. A., Yin, L., Moorthy, R., Orellana, K., Harki, D. A., Harris, R. S., and Aihara, H. (2021) Structural basis for recognition of distinct deaminated DNA lesions by endonuclease Q. Proc Natl Acad Sci U S A. 10.1073/pnas.2021120118
Shi, F., Mendrola, J. M., Sheetz, J. B., Wu, N., Sommer, A., Speer, K. F., Noordermeer, J. N., Kan, Z. - Y., Perry, K., S Englander, W., Stayrook, S. E., Fradkin, L. G., and Lemmon, M. A. (2021) ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes. Cell Rep. 37, 109834
Shi, K., Pandey, K. K., Bera, S., Vora, A. C., Grandgenett, D. P., and Aihara, H. (2013) A possible role for the asymmetric C-terminal domain dimer of Rous sarcoma virus integrase in viral DNA binding. PLoS One. 8, e56892
Shi, K., Oakland, J. T., Kurniawan, F., Moeller, N. H., Banerjee, S., and Aihara, H. (2020) Structural basis of superinfection exclusion by bacteriophage T4 Spackle. Commun Biol. 3, 691
Shi, K., Kurahashi, K., Gao, R., Tsutakawa, S. E., Tainer, J. A., Pommier, Y., and Aihara, H. (2012) Structural basis for recognition of 5'-phosphotyrosine adducts by Tdp2. Nat Struct Mol Biol. 19, 1372-7
Shigdel, U. K., Ovchinnikov, V., Lee, S. - J., Shih, J. A., Karplus, M., Nam, K., and Verdine, G. L. (2020) The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase. Nat Commun. 11, 4437
Shnitsar, V., Li, J., Li, X., Calmettes, C., Basu, A., Casey, J. R., Moraes, T. F., and Reithmeier, R. A. F. (2013) A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters. J Biol Chem. 288, 33848-60
Shoffner, G. M., Wang, R., Podell, E., Cech, T. R., and Guo, F. (2018) In Crystallo Selection to Establish New RNA Crystal Contacts.. Structure. 26, 1275-1283.e3
Shrivastava, T., Mino, K., Babayeva, N. D., Baranovskaya, O. I., Rizzino, A., and Tahirov, T. H. (2014) Structural basis of Ets1 activation by Runx1. Leukemia. 28, 2040-8
Siegel, S. D., Amer, B. R., Wu, C., Sawaya, M. R., Gosschalk, J. E., Clubb, R. T., and Ton-That, H. (2019) Structure and Mechanism of LcpA, a Phosphotransferase That Mediates Glycosylation of a Gram-Positive Bacterial Cell Wall-Anchored Protein. MBio. 10.1128/mBio.01580-18
Sievers, S. A., Karanicolas, J., Chang, H. W., Zhao, A., Jiang, L., Zirafi, O., Stevens, J. T., Münch, J., Baker, D., and Eisenberg, D. (2011) Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation. Nature. 475, 96-100
Sikowitz, M. D., Shome, B., Zhang, Y., Begley, T. P., and Ealick, S. E. (2013) Structure of a Clostridium botulinum C143S thiaminase I/thiamin complex reveals active site architecture . Biochemistry. 52, 7830-9
Sikowitz, M. D., Cooper, L. E., Begley, T. P., Kaminski, P. Alexandre, and Ealick, S. E. (2013) Reversal of the substrate specificity of CMP N-glycosidase to dCMP. Biochemistry. 52, 4037-47
Silvaroli, J. A., Plau, J., Adams, C. H., Banerjee, S., Widjaja-Adhi, M. Airanthi K., Blaner, W. S., and Golczak, M. (2021) Molecular basis for the interaction of cellular retinol-binding protein 2 (CRBP2) with non-retinoid ligands. J Lipid Res. 10.1016/j.jlr.2021.100054
Silvaroli, J. A., Pleshinger, M. J., Banerjee, S., Kiser, P. D., and Golczak, M. (2017) Enzyme That Makes You Cry-Crystal Structure of Lachrymatory Factor Synthase from Allium cepa. ACS Chem Biol. 10.1021/acschembio.7b00336
Silvaroli, J. A., Widjaja-Adhi, M. Airanthi K., Trischman, T., Chelstowska, S., Horwitz, S., Banerjee, S., Kiser, P. D., Blaner, W. S., and Golczak, M. (2019) Abnormal Cannabidiol Modulates Vitamin A Metabolism by Acting as a Competitive Inhibitor of CRBP1. ACS Chem Biol. 10.1021/acschembio.8b01070
Silvaroli, J. A., Arne, J. M., Chelstowska, S., Kiser, P. D., Banerjee, S., and Golczak, M. (2016) Ligand Binding Induces Conformational Changes in Human Cellular Retinol-binding Protein 1 (CRBP1) Revealed by Atomic Resolution Crystal Structures. J Biol Chem. 291, 8528-40
Silvers, M. A., Pakhomova, S., Neau, D. B., Silvers, W. C., Anzalone, N., Taylor, C. M., and Waldrop, G. L. (2016) Crystal Structure of Carboxyltransferase from Staphylococcus aureus Bound to the Antibacterial Agent Moiramide B. Biochemistry. 55, 4666-74
Silverstein, T. D., Johnson, R. E., Jain, R., Prakash, L., Prakash, S., and Aggarwal, A. K. (2010) Structural basis for the suppression of skin cancers by DNA polymerase eta. Nature. 465, 1039-43
Silverstein, T. D., Jain, R., Johnson, R. E., Prakash, L., Prakash, S., and Aggarwal, A. K. (2010) Structural basis for error-free replication of oxidatively damaged DNA by yeast DNA polymerase η.. Structure. 18, 1463-70
Simanshu, D. K., Zhai, X., Munch, D., Hofius, D., Markham, J. E., Bielawski, J., Bielawska, A., Malinina, L., Molotkovsky, J. G., Mundy, J. W., Patel, D. J., and Brown, R. E. (2014) Arabidopsis accelerated cell death 11, ACD11, is a ceramide-1-phosphate transfer protein and intermediary regulator of phytoceramide levels. Cell Rep. 6, 388-99
Simanshu, D. K., Yamaguchi, Y., Park, J. - H., Inouye, M., and Patel, D. J. (2013) Structural basis of mRNA recognition and cleavage by toxin MazF and its regulation by antitoxin MazE in Bacillus subtilis. Mol Cell. 52, 447-58
Simanshu, D. K., Kamlekar, R. Kanth, Wijesinghe, D. S., Zou, X., Zhai, X., Mishra, S. K., Molotkovsky, J. G., Malinina, L., Hinchcliffe, E. H., Chalfant, C. E., Brown, R. E., and Patel, D. J. (2013) Non-vesicular trafficking by a ceramide-1-phosphate transfer protein regulates eicosanoids. Nature. 500, 463-7
Simmons, H. C., Watanabe, A., Iii, T. H. Oguin, Van Itallie, E. S., Wiehe, K. J., Sempowski, G. D., Kuraoka, M., Kelsoe, G., and McCarthy, K. R. (2023) A new class of antibodies that overcomes a steric barrier to cross-group neutralization of influenza viruses. PLoS Biol. 21, e3002415
Simon, B., Lou, H. Jane, Huet-Calderwood, C., Shi, G., Boggon, T. J., Turk, B. E., and Calderwood, D. A. (2022) Tousled-like kinase 2 targets ASF1 histone chaperones through client mimicry. Nat Commun. 13, 749

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