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Bajic, G., Maron, M. J., Adachi, Y., Onodera, T., McCarthy, K. R., McGee, C. E., Sempowski, G. D., Takahashi, Y., Kelsoe, G., Kuraoka, M., and Schmidt, A. G. (2019) Influenza Antigen Engineering Focuses Immune Responses to a Subdominant but Broadly Protective Viral Epitope. Cell Host Microbe. 25, 827-835.e6
R Bajaj, A., Arbing, M. A., Shin, A., Cascio, D., and Miallau, L. (2016) Crystal structure of the toxin Msmeg_6760, the structural homolog of Mycobacterium tuberculosis Rv2035, a novel type II toxin involved in the hypoxic response. Acta Crystallogr F Struct Biol Commun. 72, 863-869
Bailey, S., Wing, R. A., and Steitz, T. A. (2006) The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases. Cell. 126, 893-904
Bailey, S., Eliason, W. K., and Steitz, T. A. (2007) Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science. 318, 459-63
Bailey, L. J., Sheehy, K. M., Dominik, P. K., Liang, W. G., Rui, H., Clark, M., Jaskolowski, M., Kim, Y., Deneka, D., Tang, W. - J., and Kossiakoff, A. A. (2018) Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination. J Mol Biol. 430, 337-347
Baidin, V., Owens, T. W., Lazarus, M. B., and Kahne, D. (2021) Simple Secondary Amines Inhibit Growth of Gram-Negative Bacteria through Highly Selective Binding to Phenylalanyl-tRNA Synthetase. J Am Chem Soc. 143, 623-627
Bai, Y., McCoy, J. G., Levin, E. J., Sobrado, P., Rajashankar, K. R., Fox, B. G., and Zhou, M. (2015) X-ray structure of a mammalian stearoyl-CoA desaturase. Nature. 524, 252-6
Bae, B., Feklistov, A., Lass-Napiorkowska, A., Landick, R., and Darst, S. A. (2015) Structure of a bacterial RNA polymerase holoenzyme open promoter complex. Elife. 10.7554/eLife.08504
Bae, B., Davis, E., Brown, D., Campbell, E. A., Wigneshweraraj, S., and Darst, S. A. (2013) Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of σ70 domain 1.1.. Proc Natl Acad Sci U S A. 110, 19772-7
Baconguis, I., and Gouaux, E. (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature. 489, 400-5
Backman, L. Rf, Huang, Y. Y., Andorfer, M. C., Gold, B., Raines, R. T., Balskus, E. P., and Drennan, C. L. (2020) Molecular basis for catabolism of the abundant metabolite -4-hydroxy-L-proline by a microbial glycyl radical enzyme. Elife. 10.7554/eLife.51420
Babayeva, N. D., Wilder, P. J., Shiina, M., Mino, K., Desler, M., Ogata, K., Rizzino, A., and Tahirov, T. H. (2010) Structural basis of Ets1 cooperative binding to palindromic sequences on stromelysin-1 promoter DNA. Cell Cycle. 9, 3054-62
Babayeva, N. D., Baranovskaya, O. I., and Tahirov, T. H. (2012) Structural basis of Ets1 cooperative binding to widely separated sites on promoter DNA. PLoS One. 7, e33698
Babault, N., Allali-Hassani, A., Li, F., Fan, J., Yue, A., Ju, K., Liu, F., Vedadi, M., Liu, J., and Jin, J. (2018) Discovery of Bisubstrate Inhibitors of Nicotinamide N-Methyltransferase (NNMT). J Med Chem. 61, 1541-1551