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Wittlinger, F., Heppner, D. E., To, C., Günther, M., Shin, B. Hee, Rana, J. K., Schmoker, A. M., Beyett, T. S., Berger, L. M., Berger, B. - T., Bauer, N., Vasta, J. D., Corona, C. R., Robers, M. B., Knapp, S., Jänne, P. A., Eck, M. J., and Laufer, S. A. (2021) Design of a "Two-in-One" Mutant-Selective Epidermal Growth Factor Receptor Inhibitor That Spans the Orthosteric and Allosteric Sites. J Med Chem. 10.1021/acs.jmedchem.1c00848
Matsushita, T., Sati, G., Kondasinghe, N., Pirrone, M., Kato, T., Waduge, P., Kumar, H., Sanchon, A., Dobosz-Bartoszek, M., Shcherbakov, D., Juhas, M., Hobbie, S. N., Schrepfer, T., Chow, C. S., Polikanov, Y., Schacht, J., Vasella, A., Böttger, E. C., and Crich, D. (2019) Design, Multigram Synthesis, and in Vitro and in Vivo Evaluation of Propylamycin: A Semisynthetic 4,5-Deoxystreptamine Class Aminoglycoside for the Treatment of Drug-Resistant Enterobacteriaceae and Other Gram-Negative Pathogens. J Am Chem Soc. 10.1021/jacs.9b01693
Lee, W. - G., Chan, A. H., Spasov, K. A., Anderson, K. S., and Jorgensen, W. L. (2016) Design, Conformation, and Crystallography of 2-Naphthyl Phenyl Ethers as Potent Anti-HIV Agents. ACS Med Chem Lett. 7, 1156-1160
Miller, A. Kern, Morgen, M., Steimbach, R. R., Géraldy, M., Hellweg, L., Sehr, P., Ridinger, J., Witt, O., Oehme, I., Herbst-Gervasoni, C. J., Osko, J. D., Porter, N. J., Christianson, D. W., and Gunkel, N. (2020) Design and Synthesis of Dihydroxamic Acids as HDAC6/8/10 Inhibitors. ChemMedChem. 10.1002/cmdc.202000149
Hymel, D., Tsuji, K., Grant, R. A., Chingle, R. M., Kunciw, D. L., Yaffe, M. B., and Burke, T. R. (2021) Design and synthesis of a new orthogonally protected glutamic acid analog and its use in the preparation of high affinity polo-like kinase 1 polo-box domain - binding peptide macrocycles. Org Biomol Chem. 19, 7843-7854
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
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
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
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
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
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

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