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Boekhout, M., Karasu, M. E., Wang, J., Acquaviva, L., Pratto, F., Brick, K., Eng, D. Y., Xu, J., R Camerini-Otero, D., Patel, D. J., and Keeney, S. (2019) REC114 Partner ANKRD31 Controls Number, Timing, and Location of Meiotic DNA Breaks. Mol Cell. 10.1016/j.molcel.2019.03.023
Boehmer, T., Jeudy, S., Berke, I. C., and Schwartz, T. U. (2008) Structural and functional studies of Nup107/Nup133 interaction and its implications for the architecture of the nuclear pore complex. Mol Cell. 30, 721-31
Boehmer, T., and Schwartz, T. U. (2007) Purification, crystallization and preliminary X-ray analysis of a Nup107-Nup133 heterodimeric nucleoporin complex. Acta Crystallogr Sect F Struct Biol Cryst Commun. 63, 816-8
Bodnar, N. (2018) Mechanism and Structure of the Cdc48 ATPase Complex. Ph.D. thesis, Harvard University, Cambridge, Massachusetts
Bodnar, N. O., Kim, K. H., Ji, Z., Wales, T. E., Svetlov, V., Nudler, E., Engen, J. R., Walz, T., and Rapoport, T. A. (2018) Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4. Nat Struct Mol Biol. 25, 616-622
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
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
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
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
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
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
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
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
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
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
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
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., 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
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
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
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
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

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