Publications

Found 2870 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
Sharkey, M. A., Oliveira, T. F., Engel, P. C., and Khan, A. R. (2013) Structure of NADP(+)-dependent glutamate dehydrogenase from Escherichia coli--reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases. FEBS J. 280, 4681-92
Sharma, S., Yang, J., Doamekpor, S. K., Grudizen-Nogalska, E., Tong, L., and Kiledjian, M. (2022) Identification of a novel deFADding activity in human, yeast and bacterial 5' to 3' exoribonucleases. Nucleic Acids Res. 50, 8807-8817
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
Sharma, H., Yu, S., Kong, J., Wang, J., and Steitz, T. A. (2009) Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proc Natl Acad Sci U S A. 106, 16604-9
Sharon, I., Grogg, M., Hilvert, D., and T Schmeing, M. (2022) The structure of cyanophycinase in complex with a cyanophycin degradation intermediate. Biochim Biophys Acta Gen Subj. 1866, 130217
Sharon, I., McKay, G. A., Nguyen, D., and T Schmeing, M. (2023) Discovery of cyanophycin dipeptide hydrolase enzymes suggests widespread utility of the natural biopolymer cyanophycin. Proc Natl Acad Sci U S A. 120, e2216547120
Sharon, I., Haque, A. S., Grogg, M., Lahiri, I., Seebach, D., Leschziner, A. E., Hilvert, D., and T Schmeing, M. (2021) Structures and function of the amino acid polymerase cyanophycin synthetase. Nat Chem Biol. 17, 1101-1110
Shatalin, K., Nuthanakanti, A., Kaushik, A., Shishov, D., Peselis, A., Shamovsky, I., Pani, B., Lechpammer, M., Vasilyev, N., Shatalina, E., Rebatchouk, D., Mironov, A., Fedichev, P., Serganov, A., and Nudler, E. (2021) Inhibitors of bacterial HS biogenesis targeting antibiotic resistance and tolerance. Science. 372, 1169-1175
Shechner, D. M., and Bartel, D. P. (2011) The structural basis of RNA-catalyzed RNA polymerization. Nat Struct Mol Biol. 18, 1036-42
Shechner, D. M., Grant, R. A., Bagby, S. C., Koldobskaya, Y., Piccirilli, J. A., and Bartel, D. P. (2009) Crystal structure of the catalytic core of an RNA-polymerase ribozyme. Science. 326, 1271-5
Sheetz, J. B., Mathea, S., Karvonen, H., Malhotra, K., Chatterjee, D., Niininen, W., Perttilä, R., Preuss, F., Suresh, K., Stayrook, S. E., Tsutsui, Y., Radhakrishnan, R., Ungureanu, D., Knapp, S., and Lemmon, M. A. (2020) Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases. Mol Cell. 79, 390-405.e7
Shek, R., Dattmore, D. A., Stives, D. P., Jackson, A. L., Chatfield, C. H., Hicks, K. A., and French, J. B. (2017) Structural and functional basis for targeting Campylobacter jejuni agmatine deiminase to overcome antibiotic resistance. Biochemistry. 10.1021/acs.biochem.7b00982
Shek, R., Hilaire, T., Sim, J., and French, J. B. (2019) Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily. Biochemistry. 58, 3280-3292
Shelke, S. A., Shao, Y., Laski, A., Koirala, D., Weissman, B. P., Fuller, J. R., Tan, X., Constantin, T. P., Waggoner, A. S., Bruchez, M. P., Armitage, B. A., and Piccirilli, J. A. (2018) Structural basis for activation of fluorogenic dyes by an RNA aptamer lacking a G-quadruplex motif. Nat Commun. 9, 4542
Shelton, C. L., Conrady, D. G., and Herr, A. B. (2017) Functional consequences of B-repeat sequence variation in the staphylococcal biofilm protein Aap: deciphering the assembly code. Biochem J. 474, 427-443
Shen, J., Wu, G., Tsai, A. - L., and Zhou, M. (2020) Structure and Mechanism of a Unique Diiron Center in Mammalian Stearoyl-CoA Desaturase. J Mol Biol. 432, 5152-5161
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
Shen, Y., Li, F., Szewczyk, M. M., Halabelian, L., Chau, I., Eram, M. S., Seña, Cdela, Park, K. - S., Meng, F., Chen, H., Zeng, H., Dong, A., Wu, H., Trush, V. V., McLeod, D., Zepeda-Velázquez, C. A., Campbell, R. M., Mader, M. M., Watson, B. M., Schapira, M., Arrowsmith, C. H., Al-awar, R., Barsyte-Lovejoy, D., H Kaniskan, Ü., Brown, P. J., Vedadi, M., and Jin, J. (2021) A First-in-Class, Highly Selective and Cell-Active Allosteric Inhibitor of Protein Arginine Methyltransferase 6. J Med Chem. 64, 3697-3706
Shen, A., Higgins, D. E., and Panne, D. (2009) Recognition of AT-rich DNA binding sites by the MogR repressor. Structure. 17, 769-77
Shen, G., Cui, W., Zhang, H., Zhou, F., Huang, W., Liu, Q., Yang, Y., Li, S., Bowman, G. R., J Sadler, E., Gross, M. L., and Li, W. (2017) Warfarin traps human vitamin K epoxide reductase in an intermediate state during electron transfer. Nat Struct Mol Biol. 24, 69-76
Shen, C., Lu, A., Xie, W. Jun, Ruan, J., Negro, R., Egelman, E. H., Fu, T. - M., and Wu, H. (2019) Molecular mechanism for NLRP6 inflammasome assembly and activation. Proc Natl Acad Sci U S A. 10.1073/pnas.1817221116
Shen, G., Li, S., Cui, W., Liu, S., Liu, Q., Yang, Y., Gross, M., and Li, W. (2018) Stabilization of warfarin-binding pocket of VKORC1 and VKORL1 by a peripheral region determines their different sensitivity to warfarin inhibition. J Thromb Haemost. 16, 1164-1175
Sheng, G., Gogakos, T., Wang, J., Zhao, H., Serganov, A., Juranek, S., Tuschl, T., Patel, D. J., and Wang, Y. (2017) Structure/cleavage-based insights into helical perturbations at bulge sites within T. thermophilus Argonaute silencing complexes. Nucleic Acids Res. 45, 9149-9163
Sheng, Y., Gralla, E. Butler, Schumacher, M., Cascio, D., Cabelli, D. E., and Valentine, J. Selverston (2012) Six-coordinate manganese(3+) in catalysis by yeast manganese superoxide dismutase. Proc Natl Acad Sci U S A. 109, 14314-9
Sheng, G., Zhao, H., Wang, J., Rao, Y., Tian, W., Swarts, D. C., van der Oost, J., Patel, D. J., and Wang, Y. (2014) Structure-based cleavage mechanism of Thermus thermophilus Argonaute DNA guide strand-mediated DNA target cleavage. Proc Natl Acad Sci U S A. 111, 652-7

Pages