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Bick, M. J., Banik, J. J., Darst, S. A., and Brady, S. F. (2010) Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone. Biochemistry. 49, 4159-68
Bick, M. J., Lamour, V., Rajashankar, K. R., Gordiyenko, Y., Robinson, C. V., and Darst, S. A. (2009) How to switch off a histidine kinase: crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda. J Mol Biol. 386, 163-77
Biester, A., Dementin, S., and Drennan, C. L. (2022) Visualizing the gas channel of a monofunctional carbon monoxide dehydrogenase. J Inorg Biochem. 230, 111774
Bigalke, J. M., and Heldwein, E. E. (2015) Structural basis of membrane budding by the nuclear egress complex of herpesviruses. EMBO J. 34, 2921-36
Bilokapic, S., and Schwartz, T. U. (2012) Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex. Proc Natl Acad Sci U S A. 109, 15241-6
Bilokapic, S., and Schwartz, T. U. (2013) Structural and functional studies of the 252 kDa nucleoporin ELYS reveal distinct roles for its three tethered domains. Structure. 21, 572-80
Bitto, E., Bingman, C. A., Wesenberg, G. E., McCoy, J. G., and Phillips, G. N. (2006) Structure of pyrimidine 5'-nucleotidase type 1. Insight into mechanism of action and inhibition during lead poisoning. J Biol Chem. 281, 20521-9
Blaha, G., Stanley, R. E., and Steitz, T. A. (2009) Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome. Science. 325, 966-70
Blaha, G., Gürel, G., Schroeder, S. J., Moore, P. B., and Steitz, T. A. (2008) Mutations outside the anisomycin-binding site can make ribosomes drug-resistant. J Mol Biol. 379, 505-19
Blair, J. A., Rauh, D., Kung, C., Yun, C. -hong, Fan, Q. - W., Rode, H., Zhang, C., Eck, M. J., Weiss, W. A., and Shokat, K. M. (2007) Structure-guided development of affinity probes for tyrosine kinases using chemical genetics. Nat Chem Biol. 3, 229-38
Blank, P. N., Barrow, G. H., and Christianson, D. W. (2019) Crystal structure of F95Q epi-isozizaene synthase, an engineered sesquiterpene cyclase that generates biofuel precursors β- and γ-curcumene.. J Struct Biol. 207, 218-224
Blank, P. N., Shinsky, S. A., and Christianson, D. W. (2019) Structure of Sesquisabinene Synthase 1, a Terpenoid Cyclase That Generates a Strained [3.1.0] Bridged-Bicyclic Product. ACS Chem Biol. 10.1021/acschembio.9b00218
Blank, P. N., Barrow, G. H., Chou, W. K. W., Duan, L., Cane, D. E., and Christianson, D. W. (2017) Substitution of Aromatic Residues with Polar Residues in the Active Site Pocket of epi-Isozizaene Synthase Leads to the Generation of New Cyclic Sesquiterpenes. Biochemistry. 10.1021/acs.biochem.7b00895
Blank, P. N., Pemberton, T. A., Chow, J. - Y., C Poulter, D., and Christianson, D. W. (2018) Crystal Structure of Cucumene Synthase, a Terpenoid Cyclase That Generates a Linear Triquinane Sesquiterpene. Biochemistry. 57, 6326-6335
Blankenchip, C. L., Nguyen, J. V., Lau, R. K., Ye, Q., Gu, Y., and Corbett, K. D. (2022) Control of bacterial immune signaling by a WYL domain transcription factor. Nucleic Acids Res. 50, 5239-5250
Blankenship, E., Vukoti, K., Miyagi, M., and Lodowski, D. T. (2014) Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state. Acta Crystallogr D Biol Crystallogr. 70, 833-40
Blankenship, E., Vahedi-Faridi, A., and Lodowski, D. T. (2015) The High-Resolution Structure of Activated Opsin Reveals a Conserved Solvent Network in the Transmembrane Region Essential for Activation. Structure. 23, 2358-2364
Blobaum, A. L., Xu, S., Rowlinson, S. W., Duggan, K. C., Banerjee, S., Kudalkar, S. N., Birmingham, W. R., Ghebreselasie, K., and Marnett, L. J. (2015) Action at a distance: mutations of peripheral residues transform rapid reversible inhibitors to slow, tight binders of cyclooxygenase-2. J Biol Chem. 290, 12793-803
Bloch, J. S., Mukherjee, S., Kowal, J., Filippova, E. V., Niederer, M., Pardon, E., Steyaert, J., Kossiakoff, A. A., and Locher, K. P. (2021) Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins. Proc Natl Acad Sci U S A. 10.1073/pnas.2115435118
Blower, T. R., Williamson, B. H., Kerns, R. J., and Berger, J. M. (2016) Crystal structure and stability of gyrase-fluoroquinolone cleaved complexes from Mycobacterium tuberculosis. Proc Natl Acad Sci U S A. 113, 1706-13
Blum, E., Zhang, J., Zaluski, J., Einstein, D. E., Korshin, E. E., Kubas, A., Gruzman, A., Tochtrop, G. P., Kiser, P. D., and Palczewski, K. (2021) Rational Alteration of Pharmacokinetics of Chiral Fluorinated and Deuterated Derivatives of Emixustat for Retinal Therapy. J Med Chem. 10.1021/acs.jmedchem.1c00279
Blumberg, L. J., Humphries, J. E., Jones, S. D., Pearce, L. B., Holgate, R., Hearn, A., Cheung, J., Mahmood, A., Del Tito, B., Graydon, J. S., Stolz, L. E., Bitonti, A., Purohit, S., de Graaf, D., Kacena, K., Andersen, J. T., Christianson, G. J., Roopenian, D. C., Hubbard, J. J., Gandhi, A. K., Lasseter, K., Pyzik, M., and Blumberg, R. S. (2019) Blocking FcRn in humans reduces circulating IgG levels and inhibits IgG immune complex-mediated immune responses. Sci Adv. 5, eaax9586
Blus, B. J., Hashimoto, H., Seo, H. - S., Krolak, A., and Debler, E. W. (2019) Substrate Affinity and Specificity of the ScSth1p Bromodomain Are Fine-Tuned for Versatile Histone Recognition. Structure. 27, 1460-1468.e3
Bobik, T. A., Morales, E. J., Shin, A., Cascio, D., Sawaya, M. R., Arbing, M., Yeates, T. O., and Rasche, M. E. (2014) Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii. Acta Crystallogr F Struct Biol Commun. 70, 1472-9
Bodea, S., Funk, M. A., Balskus, E. P., and Drennan, C. L. (2016) Molecular Basis of C-N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase. Cell Chem Biol. 23, 1206-1216

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