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Eyler, D. E., Franco, M. K., Batool, Z., Wu, M. Z., Dubuke, M. L., Dobosz-Bartoszek, M., Jones, J. D., Polikanov, Y. S., Roy, B., and Koutmou, K. S. (2019) Pseudouridinylation of mRNA coding sequences alters translation. Proc Natl Acad Sci U S A. 116, 23068-23074
Everett, B. A., Litzau, L. A., Tompkins, K., Shi, K., Nelson, A., Aihara, H., Iii, R. L. Evans, and Gordon, W. R. (2019) Crystal structure of the Wheat dwarf virus Rep domain. Acta Crystallogr F Struct Biol Commun. 75, 744-749
Evans, R. N., Blaha, G., Bailey, S., and Steitz, T. A. (2008) The structure of LepA, the ribosomal back translocase. Proc Natl Acad Sci U S A. 105, 4673-8
Eser, B. E., Zhang, X., Chanani, P. K., Begley, T. P., and Ealick, S. E. (2016) From Suicide Enzyme to Catalyst: The Iron-Dependent Sulfide Transfer in Methanococcus jannaschii Thiamin Thiazole Biosynthesis. J Am Chem Soc. 138, 3639-42
Escobar-Alvarez, S., Goldgur, Y., Yang, G., Ouerfelli, O., Li, Y., and Scheinberg, D. A. (2009) Structure and activity of human mitochondrial peptide deformylase, a novel cancer target. J Mol Biol. 387, 1211-28
Ernst, A., Avvakumov, G., Tong, J., Fan, Y., Zhao, Y., Alberts, P., Persaud, A., Walker, J. R., Neculai, A. - M., Neculai, D., Vorobyov, A., Garg, P., Beatty, L., Chan, P. - K., Juang, Y. - C., Landry, M. - C., Yeh, C., Zeqiraj, E., Karamboulas, K., Allali-Hassani, A., Vedadi, M., Tyers, M., Moffat, J., Sicheri, F., Pelletier, L., Durocher, D., Raught, B., Rotin, D., Yang, J., Moran, M. F., Dhe-Paganon, S., and Sidhu, S. S. (2013) A strategy for modulation of enzymes in the ubiquitin system. Science. 339, 590-5
Erdmann, K. S., Mao, Y., McCrea, H. J., Zoncu, R., Lee, S., Paradise, S., Modregger, J., Biemesderfer, D., Toomre, D., and De Camilli, P. (2007) A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway. Dev Cell. 13, 377-90
Eram, M. S., Shen, Y., Szewczyk, M., Wu, H., Senisterra, G., Li, F., Butler, K. V., H Kaniskan, Ü., Speed, B. A., Seña, Cdela, Dong, A., Zeng, H., Schapira, M., Brown, P. J., Arrowsmith, C. H., Barsyte-Lovejoy, D., Liu, J., Vedadi, M., and Jin, J. (2016) A Potent, Selective, and Cell-Active Inhibitor of Human Type I Protein Arginine Methyltransferases. ACS Chem Biol. 11, 772-781
Englert, M., Nakamura, A., Wang, Y. - S., Eiler, D., Söll, D., and Guo, L. - T. (2015) Probing the active site tryptophan of Staphylococcus aureus thioredoxin with an analog. Nucleic Acids Res. 43, 11061-7
Englert, M., Xia, S., Okada, C., Nakamura, A., Tanavde, V., Yao, M., Eom, S. Hyun, Konigsberg, W. H., Söll, D., and Wang, J. (2012) Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3'-terminal phosphate and 5'-OH. Proc Natl Acad Sci U S A. 109, 15235-40
Emptage, R. P., Schoenberger, M. J., Ferguson, K. M., and Marmorstein, R. (2017) Intramolecular autoinhibition of checkpoint kinase 1 is mediated by conserved basic motifs of the C-terminal kinase-associated 1 domain. J Biol Chem. 292, 19024-19033
Emptage, R. P., Lemmon, M. A., Ferguson, K. M., and Marmorstein, R. (2018) Structural Basis for MARK1 Kinase Autoinhibition by Its KA1 Domain. Structure. 26, 1137-1143.e3
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
Ellis-Guardiola, K., Rui, H., Beckner, R. L., Srivastava, P., Sukumar, N., Roux, B., and Lewis, J. C. (2019) Crystal Structure and Conformational Dynamics of Pyrococcus furiosus Prolyl Oligopeptidase. Biochemistry. 10.1021/acs.biochem.9b00031
Eldirany, S. A., Ho, M., Hinbest, A. J., Lomakin, I. B., and Bunick, C. G. (2019) Human keratin 1/10-1B tetramer structures reveal a knob-pocket mechanism in intermediate filament assembly. EMBO J. 10.15252/embj.2018100741
Ekworomadu, M. C. T., Poor, C. B., Owens, C. P., Balderas, M. A., Fabian, M., Olson, J. S., Murphy, F., Bakkalbasi, E., Balkabasi, E., Honsa, E. S., He, C., Goulding, C. W., and Maresso, A. W. (2012) Differential function of lip residues in the mechanism and biology of an anthrax hemophore. PLoS Pathog. 8, e1002559
Ejaz, A., Ordonez, H., Jacewicz, A., Ferrao, R., and Shuman, S. (2017) Structure of mycobacterial 3'-to-5' RNA:DNA helicase Lhr bound to a ssDNA tracking strand highlights distinctive features of a novel family of bacterial helicases. Nucleic Acids Res. 10.1093/nar/gkx1163
Ejaz, A., Goldgur, Y., and Shuman, S. (2019) Activity and structure of MPE, a manganese-dependent single-strand DNA endonuclease encoded in a nucleic acid repair gene cluster. J Biol Chem. 10.1074/jbc.RA119.008049
Eiler, D., Lin, J., Simonetti, A., Klaholz, B. P., and Steitz, T. A. (2013) Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases. Proc Natl Acad Sci U S A. 110, 15662-7
Eiler, D., Wang, J., and Steitz, T. A. (2014) Structural basis for the fast self-cleavage reaction catalyzed by the twister ribozyme. Proc Natl Acad Sci U S A. 111, 13028-33
Eichhorn, C. D., Yang, Y., Repeta, L., and Feigon, J. (2018) Structural basis for recognition of human 7SK long noncoding RNA by the La-related protein Larp7. Proc Natl Acad Sci U S A. 115, E6457-E6466
Eek, P., Järving, R., Järving, I., Gilbert, N. C., Newcomer, M. E., and Samel, N. (2012) Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2+ regulation. J Biol Chem. 287, 22377-86
Eduful, B. J., O'Byrne, S. N., Temme, L., Asquith, C. R. M., Liang, Y., Picado, A., Pilotte, J. R., Hossain, M. Anwar, Wells, C. I., Zuercher, W. J., Catta-Preta, C. M. C., Ramos, P. Zonzini, Santiago, Ade S., Couñago, R. M., Langendorf, C. G., Nay, K., Oakhill, J. S., Pulliam, T. L., Lin, C., Awad, D., Willson, T. M., Frigo, D. E., Scott, J. W., and Drewry, D. H. (2021) Hinge Binder Scaffold Hopping Identifies Potent Calcium/Calmodulin-Dependent Protein Kinase Kinase 2 (CAMKK2) Inhibitor Chemotypes. J Med Chem. 64, 10849-10877
Edani, B. H., Grabińska, K. A., Zhang, R., Park, E. Joo, Siciliano, B., Surmacz, L., Ha, Y., and Sessa, W. C. (2020) Structural elucidation of the -prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation. Proc Natl Acad Sci U S A. 10.1073/pnas.2008381117
Economou, N. J., Zentner, I. J., Lazo, E., Jakoncic, J., Stojanoff, V., Weeks, S. D., Grasty, K. C., Cocklin, S., and Loll, P. J. (2013) Structure of the complex between teicoplanin and a bacterial cell-wall peptide: use of a carrier-protein approach. Acta Crystallogr D Biol Crystallogr. 69, 520-33

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