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Journal Article
Settembre, E. C., Dorrestein, P. C., Park, J. - H., Augustine, A. M., Begley, T. P., and Ealick, S. E. (2003) Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis. Biochemistry. 42, 2971-81
Ho, M. - C., Cassera, M. B., Madrid, D. C., Ting, L. - M., Tyler, P. C., Kim, K., Almo, S. C., and Schramm, V. L. (2009) Structural and metabolic specificity of methylthiocoformycin for malarial adenosine deaminases. Biochemistry. 48, 9618-26
Kudalkar, S. N., Ullah, I., Bertoletti, N., Mandl, H. K., Cisneros, J. A., Beloor, J., Chan, A. H., Quijano, E., W Saltzman, M., Jorgensen, W. L., Kumar, P., and Anderson, K. S. (2019) Structural and pharmacological evaluation of a novel non-nucleoside reverse transcriptase inhibitor as a promising long acting nanoformulation for treating HIV. Antiviral Res. 167, 110-116
Maiti, A., Buffalo, C. Z., Saurabh, S., Montecinos-Franjola, F., Hachey, J. S., Conlon, W. J., Tran, G. N., Hassan, B., Walters, K. J., Drobizhev, M., Moerner, W. E., Ghosh, P., Matsuo, H., Tsien, R. Y., Lin, J. Y., and Rodriguez, E. A. (2023) Structural and photophysical characterization of the small ultra-red fluorescent protein. Nat Commun. 14, 4155
Custodio, J. M., Ayres, C. M., Rosales, T. J., Brambley, C. A., Arbuiso, A. G., Landau, L. M., Keller, G. L. J., Srivastava, P. K., and Baker, B. M. (2023) Structural and physical features that distinguish tumor-controlling from inactive cancer neoepitopes. Proc Natl Acad Sci U S A. 120, e2312057120
Kudalkar, S. N., Beloor, J., Chan, A. H., Lee, W. - G., Jorgensen, W. L., Kumar, P., and Anderson, K. S. (2017) Structural and Preclinical Studies of Computationally Designed Non-Nucleoside Reverse Transcriptase Inhibitors for Treating HIV infection. Mol Pharmacol. 91, 383-391
Olenginski, G. M., Piacentini, J., Harris, D. R., Runko, N. A., Papoutsis, B. M., Alter, J. R., Hess, K. R., Brewer, S. H., and Phillips-Piro, C. M. (2021) Structural and spectrophotometric investigation of two unnatural amino-acid altered chromophores in the superfolder green fluorescent protein. Acta Crystallogr D Struct Biol. 77, 1010-1018
Grell, T. A. J., Kincannon, W. M., Bruender, N. A., Blaesi, E. J., Krebs, C., Bandarian, V., and Drennan, C. L. (2018) Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. J Biol Chem. 10.1074/jbc.RA118.005369
Niu, Y., Suzuki, H., Hosford, C. J., Walz, T., and Chappie, J. S. (2020) Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes. Nat Commun. 11, 5907
Chen, L., Shi, K., Yin, Z., and Aihara, H. (2013) Structural asymmetry in the Thermus thermophilus RuvC dimer suggests a basis for sequential strand cleavages during Holliday junction resolution. Nucleic Acids Res. 41, 648-56
Yelshanskaya, M. V., Singh, A. K., Sampson, J. M., Narangoda, C., Kurnikova, M., and Sobolevsky, A. I. (2016) Structural Bases of Noncompetitive Inhibition of AMPA-Subtype Ionotropic Glutamate Receptors by Antiepileptic Drugs. Neuron. 91, 1305-15
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
Guettler, S., LaRose, J., Petsalaki, E., Gish, G., Scotter, A., Pawson, T., Rottapel, R., and Sicheri, F. (2011) Structural basis and sequence rules for substrate recognition by Tankyrase explain the basis for cherubism disease. Cell. 147, 1340-54
Wilker, E. W., Grant, R. A., Artim, S. C., and Yaffe, M. B. (2005) A structural basis for 14-3-3sigma functional specificity. J Biol Chem. 280, 18891-8
Wang, H., Goehring, A., Wang, K. H., Penmatsa, A., Ressler, R., and Gouaux, E. (2013) Structural basis for action by diverse antidepressants on biogenic amine transporters. Nature. 503, 141-5
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
Sun, J., Paduch, M., Kim, S. - A., Kramer, R. M., Barrios, A. F., Lu, V., Luke, J., Usatyuk, S., Kossiakoff, A. A., and Tan, S. (2018) Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2. Proc Natl Acad Sci U S A. 10.1073/pnas.1805343115
Malakhova, M., Tereshko, V., Lee, S. - Y., Yao, K., Cho, Y. - Y., Bode, A., and Dong, Z. (2008) Structural basis for activation of the autoinhibitory C-terminal kinase domain of p90 RSK2. Nat Struct Mol Biol. 15, 112-3
Cai, Y., Chin, H. F., Lazarova, D., Menon, S., Fu, C., Cai, H., Sclafani, A., Rodgers, D. W., De La Cruz, E. M., Ferro-Novick, S., and Reinisch, K. M. (2008) The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes. Cell. 133, 1202-13
Warner, K. Deigan, Chen, M. C., Song, W., Strack, R. L., Thorn, A., Jaffrey, S. R., and Ferré-D'Amaré, A. R. (2014) Structural basis for activity of highly efficient RNA mimics of green fluorescent protein. Nat Struct Mol Biol. 21, 658-63
Wang, X. - H., Su, M., Gao, F., Xie, W., Zeng, Y., Li, D. - L., Liu, X. - L., Zhao, H., Qin, L., Li, F., Liu, Q., Clarke, O. B., Lam, S. Man, Shui, G. - H., Hendrickson, W. A., and Chen, Y. - H. (2019) Structural basis for activity of TRIC counter-ion channels in calcium release. Proc Natl Acad Sci U S A. 10.1073/pnas.1817271116
Hann, Z. S., Ji, C., Olsen, S. K., Lu, X., Lux, M. C., Tan, D. S., and Lima, C. D. (2019) Structural basis for adenylation and thioester bond formation in the ubiquitin E1. Proc Natl Acad Sci U S A. 116, 15475-15484
Fairman, J. Wesley, Wijerathna, S. Ranjan, Ahmad, M. Faiz, Xu, H., Nakano, R., Jha, S., Prendergast, J., R Welin, M., Flodin, S., Roos, A., Nordlund, P., Li, Z., Walz, T., and Dealwis, C. Godfrey (2011) Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nat Struct Mol Biol. 18, 316-22
Xiao, T., Takagi, J., Coller, B. S., Wang, J. -huai, and Springer, T. A. (2004) Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature. 432, 59-67
Borovinskaya, M. A., Pai, R. D., Zhang, W., Schuwirth, B. S., Holton, J. M., Hirokawa, G., Kaji, H., Kaji, A., and Cate, J. H. Doudna (2007) Structural basis for aminoglycoside inhibition of bacterial ribosome recycling. Nat Struct Mol Biol. 14, 727-32