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Antipenko, A., Himanen, J. - P., van Leyen, K., Nardi-Dei, V., Lesniak, J., Barton, W. A., Rajashankar, K. R., Lu, M., Hoemme, C., Püschel, A. W., and Nikolov, D. B. (2003) Structure of the semaphorin-3A receptor binding module. Neuron. 39, 589-98
Lou, X., Toresson, G., Benod, C., Suh, J. Ho, Philips, K. J., Webb, P., and Gustafsson, J. - Å. (2014) Structure of the retinoid X receptor α-liver X receptor β (RXRα-LXRβ) heterodimer on DNA.. Nat Struct Mol Biol. 21, 277-81
Rubin, S. M., Gall, A. - L., Zheng, N., and Pavletich, N. P. (2005) Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. Cell. 123, 1093-106
Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., M Manzini, C., Shapiro, L., and Mancia, F. (2016) Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun. 7, 10175
Yuan, P., Leonetti, M. D., Pico, A. R., Hsiung, Y., and MacKinnon, R. (2010) Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution. Science. 329, 182-6
Wang, Y., Sheng, G., Juranek, S., Tuschl, T., and Patel, D. J. (2008) Structure of the guide-strand-containing argonaute silencing complex. Nature. 456, 209-13
Chen, B., Liu, Z., Perry, K., and Jin, R. (2022) Structure of the glucosyltransferase domain of TcdA in complex with RhoA provides insights into substrate recognition. Sci Rep. 12, 9028
Chen, P., Lam, K. - H., Liu, Z., Mindlin, F. A., Chen, B., Gutierrez, C. B., Huang, L., Zhang, Y., Hamza, T., Feng, H., Matsui, T., Bowen, M. E., Perry, K., and Jin, R. (2019) Structure of the full-length Clostridium difficile toxin B. Nat Struct Mol Biol. 10.1038/s41594-019-0268-0
Tu, D., Graziano, B. R., Park, E., Zheng, W., Li, Y., Goode, B. L., and Eck, M. J. (2012) Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6. Proc Natl Acad Sci U S A. 109, E3424-33
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

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