Publications

Found 610 results
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Singer, J. M., Novotney, S., Strickland, D., Haddox, H. K., Leiby, N., Rocklin, G. J., Chow, C. M., Roy, A., Bera, A. K., Motta, F. C., Cao, L., Strauch, E. - M., Chidyausiku, T. M., Ford, A., Ho, E., Zaitzeff, A., Mackenzie, C. O., Eramian, H., DiMaio, F., Grigoryan, G., Vaughn, M., Stewart, L. J., Baker, D., and Klavins, E. (2022) Large-scale design and refinement of stable proteins using sequence-only models. PLoS One. 17, e0265020
Iketani, S., Forouhar, F., Liu, H., Hong, S. Jung, Lin, F. - Y., Nair, M. S., Zask, A., Huang, Y., Xing, L., Stockwell, B. R., Chavez, A., and Ho, D. D. (2021) Lead compounds for the development of SARS-CoV-2 3CL protease inhibitors. Nat Commun. 12, 2016
Zhang, Z., Fu, J., Rack, J. Gregor Mat, Li, C., Voorneveld, J., Filippov, D. V., Ahel, I., Luo, Z. - Q., and Das, C. (2024) Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain. Nat Commun. 15, 2452
Zhang, Z., Fu, J., Rack, J. Gregor Mat, Li, C., Voorneveld, J., Filippov, D. V., Ahel, I., Luo, Z. - Q., and Das, C. (2024) Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain. Nat Commun. 15, 2452
French, J. B., Yates, P. A., D Soysa, R., Boitz, J. M., Carter, N. S., Chang, B., Ullman, B., and Ealick, S. E. (2011) The Leishmania donovani UMP synthase is essential for promastigote viability and has an unusual tetrameric structure that exhibits substrate-controlled oligomerization. J Biol Chem. 286, 20930-41
Turlington, Z. R., de Macedo, S. Vaz Ferrei, Perry, K., Belsky, S. L., Faust, J. A., Snider, M. J., and Hicks, K. A. (2023) Ligand bound structure of a 6-hydroxynicotinic acid 3-monooxygenase provides mechanistic insights. Arch Biochem Biophys. 752, 109859
Münzker, L., Kimani, S. W., Fowkes, M. M., Dong, A., Zheng, H., Li, Y., Dasovich, M., Zak, K. M., Leung, A. K. L., Elkins, J. M., Kessler, D., Arrowsmith, C. H., Halabelian, L., and Böttcher, J. (2024) A ligand discovery toolbox for the WWE domain family of human E3 ligases. Commun Biol. 7, 901
Huang, W. Mun, DaGloria, J., Fox, H., Ruan, Q., Tillou, J., Shi, K., Aihara, H., Aron, J., and Casjens, S. (2012) Linear chromosome-generating system of Agrobacterium tumefaciens C58: protelomerase generates and protects hairpin ends. J Biol Chem. 287, 25551-63
Rivkin, E., Almeida, S. M., Ceccarelli, D. F., Juang, Y. - C., MacLean, T. A., Srikumar, T., Huang, H., Dunham, W. H., Fukumura, R., Xie, G., Gondo, Y., Raught, B., Gingras, A. - C., Sicheri, F., and Cordes, S. P. (2013) The linear ubiquitin-specific deubiquitinase gumby regulates angiogenesis. Nature. 498, 318-24
Berkovitch, F., Behshad, E., Tang, K. - H., Enns, E. A., Frey, P. A., and Drennan, C. L. (2004) A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase. Proc Natl Acad Sci U S A. 101, 15870-5
Tayeb-Fligelman, E., Bowler, J. T., Tai, C. E., Sawaya, M. R., Jiang, Y. Xiao, Garcia, G., Griner, S. L., Cheng, X., Salwinski, L., Lutter, L., Seidler, P. M., Lu, J., Rosenberg, G. M., Hou, K., Abskharon, R., Pan, H., Zee, C. - T., Boyer, D. R., Li, Y., Anderson, D. H., Murray, K. A., Falcon, G., Cascio, D., Saelices, L., Damoiseaux, R., Arumugaswami, V., Guo, F., and Eisenberg, D. S. (2023) Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils. Nat Commun. 14, 2379
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Amrhein, J. A., Beyett, T. S., Feng, W. W., Krämer, A., Weckesser, J., Schaeffner, I. K., Rana, J. K., Jänne, P. A., Eck, M. J., Knapp, S., and Hanke, T. (2022) Macrocyclization of Quinazoline-Based EGFR Inhibitors Leads to Exclusive Mutant Selectivity for EGFR L858R and Del19. J Med Chem. 65, 15679-15697
Washington, A. Z., Benicewicz, D. B., Canzoneri, J. C., Fagan, C. E., Mwakwari, S. C., Maehigashi, T., Dunham, C. M., and Oyelere, A. K. (2014) Macrolide-peptide conjugates as probes of the path of travel of the nascent peptides through the ribosome. ACS Chem Biol. 9, 2621-31
Chevalier, A., Silva, D. - A., Rocklin, G. J., Hicks, D. R., Vergara, R., Murapa, P., Bernard, S. M., Zhang, L., Lam, K. - H., Yao, G., Bahl, C. D., Miyashita, S. - I., Goreshnik, I., Fuller, J. T., Koday, M. T., Jenkins, C. M., Colvin, T., Carter, L., Bohn, A., Bryan, C. M., D Fernández-Velasco, A., Stewart, L., Dong, M., Huang, X., Jin, R., Wilson, I. A., Fuller, D. H., and Baker, D. (2017) Massively parallel de novo protein design for targeted therapeutics. Nature. 550, 74-79
Chevalier, A., Silva, D. - A., Rocklin, G. J., Hicks, D. R., Vergara, R., Murapa, P., Bernard, S. M., Zhang, L., Lam, K. - H., Yao, G., Bahl, C. D., Miyashita, S. - I., Goreshnik, I., Fuller, J. T., Koday, M. T., Jenkins, C. M., Colvin, T., Carter, L., Bohn, A., Bryan, C. M., D Fernández-Velasco, A., Stewart, L., Dong, M., Huang, X., Jin, R., Wilson, I. A., Fuller, D. H., and Baker, D. (2017) Massively parallel de novo protein design for targeted therapeutics. Nature. 550, 74-79
Chevalier, A., Silva, D. - A., Rocklin, G. J., Hicks, D. R., Vergara, R., Murapa, P., Bernard, S. M., Zhang, L., Lam, K. - H., Yao, G., Bahl, C. D., Miyashita, S. - I., Goreshnik, I., Fuller, J. T., Koday, M. T., Jenkins, C. M., Colvin, T., Carter, L., Bohn, A., Bryan, C. M., D Fernández-Velasco, A., Stewart, L., Dong, M., Huang, X., Jin, R., Wilson, I. A., Fuller, D. H., and Baker, D. (2017) Massively parallel de novo protein design for targeted therapeutics. Nature. 550, 74-79
Stewart, M. L., Fire, E., Keating, A. E., and Walensky, L. D. (2010) The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer. Nat Chem Biol. 6, 595-601
Fire, E., Gullá, S. V., Grant, R. A., and Keating, A. E. (2010) Mcl-1-Bim complexes accommodate surprising point mutations via minor structural changes. Protein Sci. 19, 507-19
Zhao, H., Xu, L., Bombardi, R., Nargi, R., Deng, Z., Errico, J. M., Nelson, C. A., Dowd, K. A., Pierson, T. C., Crowe, J. E., Diamond, M. S., and Fremont, D. H. (2020) Mechanism of differential Zika and dengue virus neutralization by a public antibody lineage targeting the DIII lateral ridge. J Exp Med. 10.1084/jem.20191792

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