Publications

Found 2727 results
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D
Choi, M., Sukumar, N., Liu, A., and Davidson, V. L. (2009) Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine. Biochemistry. 48, 9174-84
Schureck, M. A., Dunkle, J. A., Maehigashi, T., Miles, S. J., and Dunham, C. M. (2015) Defining the mRNA recognition signature of a bacterial toxin protein. Proc Natl Acad Sci U S A. 112, 13862-7
Kohlway, A., Luo, D., Rawling, D. C., Ding, S. C., and Pyle, A. Marie (2013) Defining the functional determinants for RNA surveillance by RIG-I. EMBO Rep. 14, 772-9
Polizzi, N. F., and DeGrado, W. F. (2020) A defined structural unit enables de novo design of small-molecule-binding proteins. Science. 369, 1227-1233
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
Papadaki, G. F., Ani, O., Florio, T. J., Young, M. C., Danon, J. N., Sun, Y., Dersh, D., and Sgourakis, N. G. (2023) Decoupling peptide binding from T cell receptor recognition with engineered chimeric MHC-I molecules. Front Immunol. 14, 1116906
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
Park, H. Ho, Logette, E., Raunser, S., Cuenin, S., Walz, T., Tschopp, J., and Wu, H. (2007) Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex. Cell. 128, 533-46
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
Vorobieva, A. A., White, P., Liang, B., Horne, J. E., Bera, A. K., Chow, C. M., Gerben, S., Marx, S., Kang, A., Stiving, A. Q., Harvey, S. R., Marx, D. C., G Khan, N., Fleming, K. G., Wysocki, V. H., Brockwell, D. J., Tamm, L. K., Radford, S. E., and Baker, D. (2021) De novo design of transmembrane β barrels.. Science. 10.1126/science.abc8182
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
Joh, N. H., Wang, T., Bhate, M. P., Acharya, R., Wu, Y., Grabe, M., Hong, M., Grigoryan, G., and DeGrado, W. F. (2014) De novo design of a transmembrane Zn²⁺-transporting four-helix bundle.. Science. 346, 1520-4
Kurz, T., Chou, Y. - C., Willems, A. R., Meyer-Schaller, N., Hecht, M. - L., Tyers, M., Peter, M., and Sicheri, F. (2008) Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation. Mol Cell. 29, 23-35
Elsässer, S. J., Huang, H., Lewis, P. W., Chin, J. W., C Allis, D., and Patel, D. J. (2012) DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition. Nature. 491, 560-5
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
Schuermann, J. (2022) Data Flow at NE-CAT. 2022 Workshop on High Data Rate Macromolecular Crystallography (HDRMX)
Rajashankar, K., and Dauter, Z. (2014) Data collection for crystallographic structure determination. Methods Mol Biol. 1140, 211-37
Murphy, F. (2018) Data Collection and Quality. CCP4/APS School in Macromolecular Crystallography: From data collection to structure refinement and beyond, June 18 - 25, 2018
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

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