Publications

Found 2704 results
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
S
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
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., 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
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
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
Simonovic, M., and Steitz, T. A. (2008) Peptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3'-hydroxyl group of A76 of the unacylated A-site tRNA. RNA. 14, 2372-8
Simpson, B. W., Pahil, K. S., Owens, T. W., Lundstedt, E. A., Davis, R. M., Kahne, D., and Ruiz, N. (2019) Combining Mutations That Inhibit Two Distinct Steps of the ATP Hydrolysis Cycle Restores Wild-Type Function in the Lipopolysaccharide Transporter and Shows that ATP Binding Triggers Transport. MBio. 10.1128/mBio.01931-19
Sinatra, L., Vogelmann, A., Friedrich, F., Tararina, M. A., Neuwirt, E., Colcerasa, A., König, P., Toy, L., Yesiloglu, T. Z., Hilscher, S., Gaitzsch, L., Papenkordt, N., Zhai, S., Zhang, L., Romier, C., Einsle, O., Sippl, W., Schutkowski, M., Gross, O., Bendas, G., Christianson, D. W., Hansen, F. K., Jung, M., and Schiedel, M. (2023) Development of First-in-Class Dual Sirt2/HDAC6 Inhibitors as Molecular Tools for Dual Inhibition of Tubulin Deacetylation. J Med Chem. 66, 14787-14814
Singer, J. M., Novotney, S., Strickland, D., Haddox, H. K., Leiby, N., Rocklin, G. J., Chow, C. M., Roy, A., Bera, A. K., Motta, F. C., Cao, L., Strauch, E. - M., Chidyausiku, T. M., Ford, A., Ho, E., Zaitzeff, A., Mackenzie, C. O., Eramian, H., DiMaio, F., Grigoryan, G., Vaughn, M., Stewart, L. J., Baker, D., and Klavins, E. (2022) Large-scale design and refinement of stable proteins using sequence-only models. PLoS One. 17, e0265020
Singh, S., Ng, J., Nayak, D., and Sivaraman, J. (2019) Structural insights into a HECT-type E3 ligase AREL1 and its ubiquitination activities . J Biol Chem. 294, 19934-19949
Singh, S., and Sivaraman, J. (2020) Crystal structure of HECT domain of UBE3C E3 ligase and its ubiquitination activity. Biochem J. 477, 905-923
Singh, M., Wang, Z., Cascio, D., and Feigon, J. (2015) Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1. J Mol Biol. 427, 807-23
Singh, H., Schuermann, J. P., Reilly, T. J., Calcutt, M. J., and Tanner, J. J. (2010) Recognition of nucleoside monophosphate substrates by Haemophilus influenzae class C acid phosphatase. J Mol Biol. 404, 639-49
Singh, A. K., Saotome, K., and Sobolevsky, A. I. (2017) Swapping of transmembrane domains in the epithelial calcium channel TRPV6. Sci Rep. 7, 10669
Singh, A. K., Saotome, K., McGoldrick, L. L., and Sobolevsky, A. I. (2018) Structural bases of TRP channel TRPV6 allosteric modulation by 2-APB. Nat Commun. 9, 2465
Singh, H., Reilly, T. J., and Tanner, J. J. (2011) Structural basis of the inhibition of class C acid phosphatases by adenosine 5'-phosphorothioate. FEBS J. 278, 4374-81
Singh, M., Wang, Z., Koo, B. - K., Patel, A., Cascio, D., Collins, K., and Feigon, J. (2012) Structural basis for telomerase RNA recognition and RNP assembly by the holoenzyme La family protein p65. Mol Cell. 47, 16-26
Singh, M., Gonzales, F. A., Cascio, D., Heckmann, N., Chanfreau, G., and Feigon, J. (2009) Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1. J Biol Chem. 284, 1906-16
Singh, H., Arentson, B. W., Becker, D. F., and Tanner, J. J. (2014) Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proc Natl Acad Sci U S A. 111, 3389-94
Singh, H., Felts, R. L., Schuermann, J. P., Reilly, T. J., and Tanner, J. J. (2009) Crystal Structures of the histidine acid phosphatase from Francisella tularensis provide insight into substrate recognition. J Mol Biol. 394, 893-904

Pages