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D
Ketcham, J. M., Haling, J., Khare, S., Bowcut, V., Briere, D. M., Burns, A. C., Gunn, R. J., Ivetac, A., Kuehler, J., Kulyk, S., Laguer, J., J Lawson, D., Moya, K., Nguyen, N., Rahbaek, L., Saechao, B., Smith, C. R., Sudhakar, N., Thomas, N. C., Vegar, L., Vanderpool, D., Wang, X., Yan, L., Olson, P., Christensen, J. G., and Marx, M. A. (2022) Design and Discovery of MRTX0902, a Potent, Selective, Brain-Penetrant, and Orally Bioavailable Inhibitor of the SOS1:KRAS Protein-Protein Interaction. J Med Chem. 65, 9678-9690
Zhan, C., Patskovsky, Y., Yan, Q., Li, Z., Ramagopal, U., Cheng, H., Brenowitz, M., Hui, X., Nathenson, S. G., and Almo, S. C. (2011) Decoy strategies: the structure of TL1A:DcR3 complex. Structure. 19, 162-71
Anishchenko, I., Pellock, S. J., Chidyausiku, T. M., Ramelot, T. A., Ovchinnikov, S., Hao, J., Bafna, K., Norn, C., Kang, A., Bera, A. K., DiMaio, F., Carter, L., Chow, C. M., Montelione, G. T., and Baker, D. (2021) De novo protein design by deep network hallucination. Nature. 10.1038/s41586-021-04184-w
de Haas, R. J., Tas, R. P., van den Broek, D., Zheng, C., Nguyen, H., Kang, A., Bera, A. K., King, N. P., Voets, I. K., and de Vries, R. (2023) De novo designed ice-binding proteins from twist-constrained helices. Proc Natl Acad Sci U S A. 120, e2220380120
Kim, D. E., Jensen, D. R., Feldman, D., Tischer, D., Saleem, A., Chow, C. M., Li, X., Carter, L., Milles, L., Nguyen, H., Kang, A., Bera, A. K., Peterson, F. C., Volkman, B. F., Ovchinnikov, S., and Baker, D. (2023) De novo design of small beta barrel proteins. Proc Natl Acad Sci U S A. 120, e2207974120
Torres, S. Vázquez, J Y Leung, P., Venkatesh, P., Lutz, I. D., Hink, F., Huynh, H. - H., Becker, J., Yeh, A. Hsien- Wei, Juergens, D., Bennett, N. R., Hoofnagle, A. N., Huang, E., MacCoss, M. J., Expòsit, M., Lee, G. Rie, Bera, A. K., Kang, A., De La Cruz, J., Levine, P. M., Li, X., Lamb, M., Gerben, S. R., Murray, A., Heine, P., Korkmaz, E. Nihal, Nivala, J., Stewart, L., Watson, J. L., Rogers, J. M., and Baker, D. (2023) De novo design of high-affinity binders of bioactive helical peptides. Nature. 10.1038/s41586-023-06953-1
Meyer, P. A., Socias, S., Key, J., Ransey, E., Tjon, E. C., Buschiazzo, A., Lei, M., Botka, C., Withrow, J., Neau, D., Rajashankar, K., Anderson, K. S., Baxter, R. H., Blacklow, S. C., Boggon, T. J., Bonvin, A. M. J. J., Borek, D., Brett, T. J., Caflisch, A., Chang, C. - I., Chazin, W. J., Corbett, K. D., Cosgrove, M. S., Crosson, S., Dhe-Paganon, S., Di Cera, E., Drennan, C. L., Eck, M. J., Eichman, B. F., Fan, Q. R., Ferré-D'Amaré, A. R., J Fromme, C., K Garcia, C., Gaudet, R., Gong, P., Harrison, S. C., Heldwein, E. E., Jia, Z., Keenan, R. J., Kruse, A. C., Kvansakul, M., McLellan, J. S., Modis, Y., Nam, Y., Otwinowski, Z., Pai, E. F., Pereira, P. José Barb, Petosa, C., Raman, C. S., Rapoport, T. A., Roll-Mecak, A., Rosen, M. K., Rudenko, G., Schlessinger, J., Schwartz, T. U., Shamoo, Y., Sondermann, H., Tao, Y. J., Tolia, N. H., Tsodikov, O. V., Westover, K. D., Wu, H., Foster, I., Fraser, J. S., Maia, F. R. N. C., Gonen, T., Kirchhausen, T., Diederichs, K., Crosas, M., and Sliz, P. (2016) Data publication with the structural biology data grid supports live analysis. Nat Commun. 7, 10882
Meyer, P. A., Socias, S., Key, J., Ransey, E., Tjon, E. C., Buschiazzo, A., Lei, M., Botka, C., Withrow, J., Neau, D., Rajashankar, K., Anderson, K. S., Baxter, R. H., Blacklow, S. C., Boggon, T. J., Bonvin, A. M. J. J., Borek, D., Brett, T. J., Caflisch, A., Chang, C. - I., Chazin, W. J., Corbett, K. D., Cosgrove, M. S., Crosson, S., Dhe-Paganon, S., Di Cera, E., Drennan, C. L., Eck, M. J., Eichman, B. F., Fan, Q. R., Ferré-D'Amaré, A. R., J Fromme, C., K Garcia, C., Gaudet, R., Gong, P., Harrison, S. C., Heldwein, E. E., Jia, Z., Keenan, R. J., Kruse, A. C., Kvansakul, M., McLellan, J. S., Modis, Y., Nam, Y., Otwinowski, Z., Pai, E. F., Pereira, P. José Barb, Petosa, C., Raman, C. S., Rapoport, T. A., Roll-Mecak, A., Rosen, M. K., Rudenko, G., Schlessinger, J., Schwartz, T. U., Shamoo, Y., Sondermann, H., Tao, Y. J., Tolia, N. H., Tsodikov, O. V., Westover, K. D., Wu, H., Foster, I., Fraser, J. S., Maia, F. R. N. C., Gonen, T., Kirchhausen, T., Diederichs, K., Crosas, M., and Sliz, P. (2016) Data publication with the structural biology data grid supports live analysis. Nat Commun. 7, 10882
Murphy, F., Schuermann, J., Neau, D., Perry, K., and Rajashankar, K. R. (2019) Data Analysis in Real Time with RAPDv2.0. 2019 Annual Meeting of the American Crystallographic Association, July 20-24, 2019
C
Wang, Y., Sosinowski, T., Novikov, A., Crawford, F., Neau, D. B., Yang, J., Kwok, W. W., Marrack, P., Kappler, J. W., and Dai, S. (2018) C-terminal modification of the insulin B:11-23 peptide creates superagonists in mouse and human type 1 diabetes. Proc Natl Acad Sci U S A. 115, 162-167
Wang, Y., Sosinowski, T., Novikov, A., Crawford, F., Neau, D. B., Yang, J., Kwok, W. W., Marrack, P., Kappler, J. W., and Dai, S. (2018) C-terminal modification of the insulin B:11-23 peptide creates superagonists in mouse and human type 1 diabetes. Proc Natl Acad Sci U S A. 115, 162-167
Perera, Y. R., Enriquez, K. T., Rodriguez, A., Garcia, V., Akizuki, T., Naretto, A., Togashi, M., Guillen, R., Skaar, E. P., and Chazin, W. J. (2025) The C-terminal extension of calprotectin mediates zinc chelation and modulates Staphylococcus aureus biomass accumulation. Protein Sci. 34, e70294
Meeks, K. R., Bogner, A. N., Nix, J. C., and Tanner, J. J. (2024) Crystallographic Fragment Screening of a Bifunctional Proline Catabolic Enzyme Reveals New Inhibitor Templates for Proline Dehydrogenase and L-Glutamate-γ-semialdehyde Dehydrogenase.. Molecules. 10.3390/molecules29225408
Young, T., Niks, D., Hakopian, S., Tam, T. K., Yu, X., Hille, R., and Blaha, G. M. (2020) Crystallographic and kinetic analyses of the FdsBG subcomplex of the cytosolic formate dehydrogenase FdsABG from Cupriavidus necator. J Biol Chem. 10.1074/jbc.RA120.013264
Sartmatova, D., Nash, T., Schormann, N., Nuth, M., Ricciardi, R., Banerjee, S., and Chattopadhyay, D. (2013) Crystallization and preliminary X-ray diffraction analysis of three recombinant mutants of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 69, 295-301
Sartmatova, D., Nash, T., Schormann, N., Nuth, M., Ricciardi, R., Banerjee, S., and Chattopadhyay, D. (2013) Crystallization and preliminary X-ray diffraction analysis of three recombinant mutants of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 69, 295-301
Yuan, L., Gao, F., Lv, Z., Nayak, D., Nayak, A., Bury, P. Dos Santos, Cano, K. E., Jia, L., Oleinik, N., Atilgan, F. Cansu, Ogretmen, B., Williams, K. M., Davies, C., Oualid, F. El, Wasmuth, E. V., and Olsen, S. K. (2022) Crystal structures reveal catalytic and regulatory mechanisms of the dual-specificity ubiquitin/FAT10 E1 enzyme Uba6. Nat Commun. 13, 4880
Yuan, L., Gao, F., Lv, Z., Nayak, D., Nayak, A., Bury, P. Dos Santos, Cano, K. E., Jia, L., Oleinik, N., Atilgan, F. Cansu, Ogretmen, B., Williams, K. M., Davies, C., Oualid, F. El, Wasmuth, E. V., and Olsen, S. K. (2022) Crystal structures reveal catalytic and regulatory mechanisms of the dual-specificity ubiquitin/FAT10 E1 enzyme Uba6. Nat Commun. 13, 4880
Barton, W. A., Tzvetkova-Robev, D., Miranda, E. P., Kolev, M. V., Rajashankar, K. R., Himanen, J. P., and Nikolov, D. B. (2006) Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex. Nat Struct Mol Biol. 13, 524-32
Gao, L., Lam, K. - H., Liu, S., Przykopanski, A., Lübke, J., Qi, R., Krüger, M., Nowakowska, M. B., Selby, K., Douillard, F. P., Dorner, M. B., Perry, K., Lindström, M., Dorner, B. G., Rummel, A., and Jin, R. (2023) Crystal structures of OrfX1, OrfX2 and the OrfX1-OrfX3 complex from the orfX gene cluster of botulinum neurotoxin E1. FEBS Lett. 597, 524-537
Xu, K., Xu, Y., Rajashankar, K. R., Robev, D., and Nikolov, D. B. (2013) Crystal structures of Lgr4 and its complex with R-spondin1. Structure. 21, 1683-9
Feliciano, P. R., Drennan, C. L., and Nonato, M. Cristina (2019) Crystal structures of fumarate hydratases from Leishmania major in a complex with inhibitor 2-thiomalate. ACS Chem Biol. 10.1021/acschembio.8b00972
Pierce, C. T., Tan, P., Greenberg, L. R., Walsh, M. E., Shi, K., Nguyen, A. H., Meixner, E. L., Sarak, S., Aihara, H., Evans, R. L., and Kazlauskas, R. J. (2025) Crystal structures of 40- and 71-substitution variants of hydroxynitrile lyase from rubber tree. Acta Crystallogr D Struct Biol. 81, 511-523
Dhatwalia, R., Singh, H., Oppenheimer, M., Karr, D. B., Nix, J. C., Sobrado, P., and Tanner, J. J. (2012) Crystal structures and small-angle x-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus. J Biol Chem. 287, 9041-51
Everett, B. A., Litzau, L. A., Tompkins, K., Shi, K., Nelson, A., Aihara, H., Iii, R. L. Evans, and Gordon, W. R. (2019) Crystal structure of the Wheat dwarf virus Rep domain. Acta Crystallogr F Struct Biol Commun. 75, 744-749

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