Found 2750 results
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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, 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
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, 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
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
Sherkhanov, S., Korman, T. P., Chan, S., Faham, S., Liu, H., Sawaya, M. R., Hsu, W. - T., Vikram, E., Cheng, T., and Bowie, J. U. (2020) Isobutanol production freed from biological limits using synthetic biochemistry. Nat Commun. 11, 4292
Sherman, D. J., Lazarus, M. B., Murphy, L., Liu, C., Walker, S., Ruiz, N., and Kahne, D. (2014) Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport. Proc Natl Acad Sci U S A. 111, 4982-7
Sherwood, L. Jo, Taylor, A. Bryan, Hart, P. John, and Hayhurst, A. (2019) Paratope duality and gullying are among the atypical recognition mechanisms employed by a trio of nanobodies to differentiate ebolavirus nucleoproteins. J Mol Biol. 10.1016/j.jmb.2019.10.005
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., Demir, Ö., Carpenter, M. A., Wagner, J., Kurahashi, K., Harris, R. S., Amaro, R. E., and Aihara, H. (2017) Conformational Switch Regulates the DNA Cytosine Deaminase Activity of Human APOBEC3B. Sci Rep. 7, 17415
Shi, K., Carpenter, M. A., Banerjee, S., Shaban, N. M., Kurahashi, K., Salamango, D. J., McCann, J. L., Starrett, G. J., Duffy, J. V., Demir, Ö., Amaro, R. E., Harki, D. A., Harris, R. S., and Aihara, H. (2017) Structural basis for targeted DNA cytosine deamination and mutagenesis by APOBEC3A and APOBEC3B. Nat Struct Mol Biol. 24, 131-139
Shi, K., Kurniawan, F., Banerjee, S., Moeller, N. H., and Aihara, H. (2020) Crystal structure of bacteriophage T4 Spackle as determined by native SAD phasing. Acta Crystallogr D Struct Biol. 76, 899-904
Shi, K., Demir, Ö., Carpenter, M. A., Banerjee, S., Harki, D. A., Amaro, R. E., Harris, R. S., and Aihara, H. (2020) Active site plasticity and possible modes of chemical inhibition of the human DNA deaminase APOBEC3B. FASEB Bioadv. 2, 49-58
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., 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, K., Huang, W. Mun, and Aihara, H. (2013) An enzyme-catalyzed multistep DNA refolding mechanism in hairpin telomere formation. PLoS Biol. 11, e1001472
Shi, K., Carpenter, M. A., Kurahashi, K., Harris, R. S., and Aihara, H. (2015) Crystal Structure of the DNA Deaminase APOBEC3B Catalytic Domain. J Biol Chem. 290, 28120-30
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., Cho, S., Aukema, K. G., Lee, T., Bera, A. K., Seffernick, J. L., Wackett, L. P., and Aihara, H. (2019) Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis. PLoS One. 14, e0216979