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D
Dziedzic, P., Cisneros, J. A., Robertson, M. J., Hare, A. A., Danford, N. E., Baxter, R. H. G., and Jorgensen, W. L. (2015) Design, synthesis, and protein crystallography of biaryltriazoles as potent tautomerase inhibitors of macrophage migration inhibitory factor. J Am Chem Soc. 137, 2996-3003
Dutta, S., Gullá, S., T Chen, S., Fire, E., Grant, R. A., and Keating, A. E. (2010) Determinants of BH3 binding specificity for Mcl-1 versus Bcl-xL. J Mol Biol. 398, 747-62
Du, J., Zhong, X., Bernatavichute, Y. V., Stroud, H., Feng, S., Caro, E., Vashisht, A. A., Terragni, J., Chin, H. Gyeong, Tu, A., Hetzel, J., Wohlschlegel, J. A., Pradhan, S., Patel, D. J., and Jacobsen, S. E. (2012) Dual binding of chromomethylase domains to H3K9me2-containing nucleosomes directs DNA methylation in plants. Cell. 151, 167-80
Doamekpor, S. K., Grudzien-Nogalska, E., Mlynarska-Cieslak, A., Kowalska, J., Kiledjian, M., and Tong, L. (2020) DXO/Rai1 enzymes remove 5'-end FAD and dephospho-CoA caps on RNAs. Nucleic Acids Res. 48, 6136-6148
Do, T. D., Sangwan, S., de Almeida, N. E. C., Ilitchev, A. I., Giammona, M., Sawaya, M. R., Buratto, S. K., Eisenberg, D. S., and Bowers, M. T. (2018) Distal Amyloid β-Protein Fragments Template Amyloid Assembly.. Protein Sci. 10.1002/pro.3375
Decroos, C., and Christianson, D. W. (2015) Design, Synthesis, and Evaluation of Polyamine Deacetylase Inhibitors, and High-Resolution Crystal Structures of Their Complexes with Acetylpolyamine Amidohydrolase. Biochemistry. 54, 4692-703
de Miranda, R., Cuthbert, B. J., Klevorn, T., Chao, A., Mendoza, J., Arbing, M., Sieminski, P. J., Papavinasasundaram, K., Abdul-Hafiz, S., Chan, S., Sassetti, C. M., Ehrt, S., and Goulding, C. W. (2023) Differentiating the roles of Mycobacterium tuberculosis substrate binding proteins, FecB and FecB2, in iron uptake. PLoS Pathog. 19, e1011650
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
De Clercq, D. J. H., Heppner, D. E., To, C., Jang, J., Park, E., Yun, C. -hong, Mushajiang, M., Shin, B. Hee, Gero, T. W., Scott, D. A., Jänne, P. A., Eck, M. J., and Gray, N. S. (2019) Discovery and Optimization of Dibenzodiazepinones as Allosteric Mutant-Selective EGFR Inhibitors. ACS Med Chem Lett. 10, 1549-1553
Davila-Hernandez, F. A., Jin, B., Pyles, H., Zhang, S., Wang, Z., Huddy, T. F., Bera, A. K., Kang, A., Chen, C. - L., De Yoreo, J. J., and Baker, D. (2023) Directing polymorph specific calcium carbonate formation with de novo protein templates. Nat Commun. 14, 8191
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
C
Chu, B., Zhang, D., and Paukstelis, P. J. (2019) A DNA G-quadruplex/i-motif hybrid. Nucleic Acids Res. 10.1093/nar/gkz1008
Choi, P. H., Jo, J., Lin, Y. - C., Lin, M. - H., Chou, C. - Y., Dietrich, L. E. P., and Tong, L. (2016) A distinct holoenzyme organization for two-subunit pyruvate carboxylase. Nat Commun. 7, 12713
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
Chen, S., Wiewiora, R. P., Meng, F., Babault, N., Ma, A., Yu, W., Qian, K., Hu, H., Zou, H., Wang, J., Fan, S., Blum, G., Pittella-Silva, F., Beauchamp, K. A., Tempel, W., Jiang, H., Chen, K., Skene, R. J., Zheng, Y. George, Brown, P. J., Jin, J., Luo, C., Chodera, J. D., and Luo, M. (2019) The dynamic conformational landscape of the protein methyltransferase SETD8. Elife. 10.7554/eLife.45403
Chauleau, M., Jacewicz, A., and Shuman, S. (2015) DNA3'pp5'G de-capping activity of aprataxin: effect of cap nucleoside analogs and structural basis for guanosine recognition. Nucleic Acids Res. 43, 6075-83
Chase, D. H., Bebenek, A. M., Nie, P., Jaime-Figueroa, S., Butrin, A., Castro, D. A., Hines, J., Linhares, B. M., and Crews, C. M. (2024) Development of a Small Molecule Downmodulator for the Transcription Factor Brachyury. Angew Chem Int Ed Engl. 63, e202316496
Chana, C. K., Maisonneuve, P., Posternak, G., Grinberg, N. G. A., Poirson, J., Ona, S. M., Ceccarelli, D. F., Mader, P., St-Cyr, D. J., Pau, V., Kurinov, I., Tang, X., Deng, D., Cui, W., Su, W., Kuai, L., Soll, R., Tyers, M., Röst, H. L., Batey, R. A., Taipale, M., Gingras, A. - C., and Sicheri, F. (2022) Discovery and Structural Characterization of Small Molecule Binders of the Human CTLH E3 Ligase Subunit GID4. J Med Chem. 10.1021/acs.jmedchem.2c00509
Carter, Z. J., Hollander, K., Spasov, K. A., Anderson, K. S., and Jorgensen, W. L. (2023) Design, synthesis, and biological testing of biphenylmethyloxazole inhibitors targeting HIV-1 reverse transcriptase. Bioorg Med Chem Lett. 84, 129216
Cappadocia, L., Kochańczyk, T., and Lima, C. D. (2021) DNA asymmetry promotes SUMO modification of the single-stranded DNA-binding protein RPA. EMBO J. 10.15252/embj.2019103787
Cao, L., Coventry, B., Goreshnik, I., Huang, B., Park, J. Sung, Jude, K. M., Marković, I., Kadam, R. U., Verschueren, K. H. G., Verstraete, K., Walsh, S. Thomas Rus, Bennett, N., Phal, A., Yang, A., Kozodoy, L., DeWitt, M., Picton, L., Miller, L., Strauch, E. - M., DeBouver, N. D., Pires, A., Bera, A. K., Halabiya, S., Hammerson, B., Yang, W., Bernard, S., Stewart, L., Wilson, I. A., Ruohola-Baker, H., Schlessinger, J., Lee, S., Savvides, S. N., K Garcia, C., and Baker, D. (2022) Design of protein binding proteins from target structure alone. Nature. 10.1038/s41586-022-04654-9
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

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