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Lu, J., Meng, W., Poy, F., Maiti, S., Goode, B. L., and Eck, M. J. (2007) Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly. J Mol Biol. 369, 1258-69
Joo, W., Xu, G., Persky, N. S., Smogorzewska, A., Rudge, D. G., Buzovetsky, O., Elledge, S. J., and Pavletich, N. P. (2011) Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway. Science. 333, 312-6
Joo, W., Xu, G., Persky, N. S., Smogorzewska, A., Rudge, D. G., Buzovetsky, O., Elledge, S. J., and Pavletich, N. P. (2011) Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway. Science. 333, 312-6
Papadopoulos, E., Jenni, S., Kabha, E., Takrouri, K. J., Yi, T., Salvi, N., Luna, R. E., Gavathiotis, E., Mahalingam, P., Arthanari, H., Rodriguez-Mias, R., Yefidoff-Freedman, R., Aktas, B. H., Chorev, M., Halperin, J. A., and Wagner, G. (2014) Structure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G. Proc Natl Acad Sci U S A. 111, E3187-95
Green, M. N., Gangwar, S. Pal, Michard, E., Simon, A. A., Portes, M. Teresa, Barbosa-Caro, J., Wudick, M. M., Lizzio, M. A., Klykov, O., Yelshanskaya, M. V., Feijó, J. A., and Sobolevsky, A. I. (2021) Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4. Mol Cell. 10.1016/j.molcel.2021.05.025
Basu, R., Eichhorn, C. D., Cheng, R., Peterson, R. D., and Feigon, J. (2020) Structure of telomerase protein Pof8 C-terminal domain is an xRRM conserved among LARP7 proteins. RNA Biol. 10.1080/15476286.2020.1836891
Jobichen, C., Chong, T. Ying, Prabhakar, M. Tirumuru, Nayak, D., Biswas, D., Pannu, N. Singh, Hanski, E., and Sivaraman, J. (2018) Structure of ScpC, a virulence protease from , reveal the functional domains and maturation mechanism. Biochem J. 10.1042/BCJ20180145
Jobichen, C., Chong, T. Ying, Prabhakar, M. Tirumuru, Nayak, D., Biswas, D., Pannu, N. Singh, Hanski, E., and Sivaraman, J. (2018) Structure of ScpC, a virulence protease from , reveal the functional domains and maturation mechanism. Biochem J. 10.1042/BCJ20180145
Kiser, P. D., Farquhar, E. R., Shi, W., Sui, X., Chance, M. R., and Palczewski, K. (2012) Structure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis. Proc Natl Acad Sci U S A. 109, E2747-56
Bitto, E., Bingman, C. A., Wesenberg, G. E., McCoy, J. G., and Phillips, G. N. (2006) Structure of pyrimidine 5'-nucleotidase type 1. Insight into mechanism of action and inhibition during lead poisoning. J Biol Chem. 281, 20521-9
Chen, E., Trajkovski, M., Lee, H. Kyung, Nyovanie, S., Martin, K. N., Dean, W. L., Tahiliani, M., Plavec, J., and Yatsunyk, L. A. (2024) Structure of native four-repeat satellite III sequence with non-canonical base interactions. Nucleic Acids Res. 52, 3390-3405
Tabackman, A. A., Frankson, R., Marsan, E. S., Perry, K., and Cole, K. E. (2016) Structure of 'linkerless' hydroxamic acid inhibitor-HDAC8 complex confirms the formation of an isoform-specific subpocket. J Struct Biol. 195, 373-378
Pourfarjam, Y., Ventura, J., Kurinov, I., Cho, A., Moss, J., and Kim, I. - K. (2018) Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. J Biol Chem. 293, 12350-12359
Svetlov, M. S., Syroegin, E. A., Aleksandrova, E. V., Atkinson, G. C., Gregory, S. T., Mankin, A. S., and Polikanov, Y. S. (2021) Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance. Nat Chem Biol. 10.1038/s41589-020-00715-0
Song, J., Rechkoblit, O., Bestor, T. H., and Patel, D. J. (2011) Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation. Science. 331, 1036-40
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Becker, A., Kannan, T. R., Taylor, A. B., Pakhomova, O. N., Zhang, Y., Somarajan, S. R., Galaleldeen, A., Holloway, S. P., Baseman, J. B., and P Hart, J. (2015) Structure of CARDS toxin, a unique ADP-ribosylating and vacuolating cytotoxin from Mycoplasma pneumoniae. Proc Natl Acad Sci U S A. 112, 5165-70
Tyler, R. C., Bitto, E., Berndsen, C. E., Bingman, C. A., Singh, S., Lee, M. S., Wesenberg, G. E., Denu, J. M., Phillips, G. N., and Markley, J. L. (2006) Structure of Arabidopsis thaliana At1g77540 protein, a minimal acetyltransferase from the COG2388 family. Biochemistry. 45, 14325-36
Gibson, M. I., Brignole, E. J., Pierce, E., Can, M., Ragsdale, S. W., and Drennan, C. L. (2015) The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism. Biochemistry. 54, 4112-20
Wang, Y., Juranek, S., Li, H., Sheng, G., Tuschl, T., and Patel, D. J. (2008) Structure of an argonaute silencing complex with a seed-containing guide DNA and target RNA duplex. Nature. 456, 921-6
Yamaguchi, M., Yu, S., Qiao, R., Weissmann, F., Miller, D. J., VanderLinden, R., Brown, N. G., Frye, J. J., Peters, J. - M., and Schulman, B. A. (2015) Structure of an APC3-APC16 complex: insights into assembly of the anaphase-promoting complex/cyclosome. J Mol Biol. 427, 1748-64
Rudolph, M. J., Davis, S. A., Haque, H. M. Emranul, Ejemel, M., Cavacini, L. A., Vance, D. J., Willsey, G. G., Piazza, C. Lyn, Weis, D. D., Wang, Y., and Mantis, N. J. (2023) Structure of a transmission blocking antibody in complex with Outer surface protein A from the Lyme disease spirochete, Borreliella burgdorferi. Proteins. 10.1002/prot.26549
McCoy, J. G., Ren, Z., Stanevich, V., Lee, J., Mitra, S., Levin, E. J., Poget, S., Quick, M., Im, W., and Zhou, M. (2016) The Structure of a Sugar Transporter of the Glucose EIIC Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport. Structure. 24, 956-64
Pollard, A. M., Bilwes, A. M., and Crane, B. R. (2009) The structure of a soluble chemoreceptor suggests a mechanism for propagating conformational signals. Biochemistry. 48, 1936-44

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