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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
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
Rajashankar, K., and Dauter, Z. (2014) Data collection for crystallographic structure determination. Methods Mol Biol. 1140, 211-37
Schuermann, J. (2022) Data Flow at NE-CAT. 2022 Workshop on High Data Rate Macromolecular Crystallography (HDRMX)
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
Gannam, Z. T. K., Jamali, H., Kweon, O. Sang, Herrington, J., Shillingford, S. R., Papini, C., Gentzel, E., Lolis, E., Bennett, A. M., Ellman, J. A., and Anderson, K. S. (2022) Defining the structure-activity relationship for a novel class of allosteric MKP5 inhibitors. Eur J Med Chem. 243, 114712
Remillard, D., Buckley, D. L., Paulk, J., Brien, G. L., Sonnett, M., Seo, H. - S., Dastjerdi, S., Wühr, M., Dhe-Paganon, S., Armstrong, S. A., and Bradner, J. E. (2017) Degradation of the BAF Complex Factor BRD9 by Heterobifunctional Ligands. Angew Chem Int Ed Engl. 56, 5738-5743
Darabedian, N., Ji, W., Fan, M., Lin, S., Seo, H. - S., Vinogradova, E. V., Yaron, T. M., Mills, E. L., Xiao, H., Senkane, K., Huntsman, E. M., Johnson, J. L., Che, J., Cantley, L. C., Cravatt, B. F., Dhe-Paganon, S., Stegmaier, K., Zhang, T., Gray, N. S., and Chouchani, E. T. (2023) Depletion of creatine phosphagen energetics with a covalent creatine kinase inhibitor. Nat Chem Biol. 10.1038/s41589-023-01273-x
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
Cannon, K. A., Park, R. U., Boyken, S. E., Nattermann, U., Yi, S., Baker, D., King, N. P., and Yeates, T. O. (2019) Design and structure of two new protein cages illustrate successes and ongoing challenges in protein engineering. Protein Sci. 10.1002/pro.3802