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Bhattacharya, A., Alam, S. L., Fricke, T., Zadrozny, K., Sedzicki, J., Taylor, A. B., Demeler, B., Pornillos, O., Ganser-Pornillos, B. K., Diaz-Griffero, F., Ivanov, D. N., and Yeager, M. (2014) Structural basis of HIV-1 capsid recognition by PF74 and CPSF6. Proc Natl Acad Sci U S A. 111, 18625-30
Bhattacharya, S., Lou, X., Hwang, P., Rajashankar, K. R., Wang, X., Gustafsson, J. - Å., Fletterick, R. J., Jacobson, R. H., and Webb, P. (2014) Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D. Proc Natl Acad Sci U S A. 111, 9103-8
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. (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
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., 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., 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
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
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
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
Bogner, A. N., and Tanner, J. J. (2022) Structure-affinity relationships of reversible proline analog inhibitors targeting proline dehydrogenase. Org Biomol Chem. 10.1039/d1ob02328d
Bogner, A. N., Ji, J., and Tanner, J. J. (2022) Structure-based engineering of minimal Proline dehydrogenase domains for inhibitor discovery. Protein Eng Des Sel. 10.1093/protein/gzac016
Bogner, A. N., Stiers, K. M., McKay, C. M., Becker, D. F., and Tanner, J. J. (2021) Structural Basis for the Stereospecific Inhibition of the Dual Proline/Hydroxyproline Catabolic Enzyme ALDH4A1 by Trans-4-Hydroxy-L-Proline. Protein Sci. 10.1002/pro.4131
Bohl, T. E., Ieong, P., Lee, J. K., Lee, T., Kankanala, J., Shi, K., Demir, Ö., Kurahashi, K., Amaro, R. E., Wang, Z., and Aihara, H. (2018) The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem. 10.1074/jbc.RA118.002503
Bolla, J. Reddy, Do, S. V., Long, F., Dai, L., Su, C. - C., Lei, H. - T., Chen, X., Gerkey, J. E., Murphy, D. C., Rajashankar, K. R., Zhang, Q., and Yu, E. W. (2012) Structural and functional analysis of the transcriptional regulator Rv3066 of Mycobacterium tuberculosis. Nucleic Acids Res. 40, 9340-55
Bolon, D. N., Grant, R. A., Baker, T. A., and Sauer, R. T. (2005) Specificity versus stability in computational protein design. Proc Natl Acad Sci U S A. 102, 12724-9
Bonsignori, M., Kreider, E. F., Fera, D., R Meyerhoff, R., Bradley, T., Wiehe, K., S Alam, M., Aussedat, B., Walkowicz, W. E., Hwang, K. - K., Saunders, K. O., Zhang, R., Gladden, M. A., Monroe, A., Kumar, A., Xia, S. - M., Cooper, M., Louder, M. K., McKee, K., Bailer, R. T., Pier, B. W., Jette, C. A., Kelsoe, G., Williams, W. B., Morris, L., Kappes, J., Wagh, K., Kamanga, G., Cohen, M. S., Hraber, P. T., Montefiori, D. C., Trama, A., Liao, H. - X., Kepler, T. B., M Moody, A., Gao, F., Danishefsky, S. J., Mascola, J. R., Shaw, G. M., Hahn, B. H., Harrison, S. C., Korber, B. T., and Haynes, B. F. (2017) Staged induction of HIV-1 glycan-dependent broadly neutralizing antibodies. Sci Transl Med. 10.1126/scitranslmed.aai7514
Bonsor, D. A., Alexander, P., Snead, K., Hartig, N., Drew, M., Messing, S., Finci, L. I., Nissley, D. V., McCormick, F., Esposito, D., Rodriguez-Viciana, P., Stephen, A. G., and Simanshu, D. K. (2022) Structure of the SHOC2-MRAS-PP1C complex provides insights into RAF activation and Noonan syndrome. Nat Struct Mol Biol. 29, 966-977
Born, D. A., Ulrich, E. C., San Ju, K. -, Peck, S. C., van der Donk, W. A., and Drennan, C. L. (2017) Structural basis for methylphosphonate biosynthesis. Science. 358, 1336-1339
Borovinskaya, M. A., Pai, R. D., Zhang, W., Schuwirth, B. S., Holton, J. M., Hirokawa, G., Kaji, H., Kaji, A., and Cate, J. H. Doudna (2007) Structural basis for aminoglycoside inhibition of bacterial ribosome recycling. Nat Struct Mol Biol. 14, 727-32
Bowen, N. E., Temple, J., Shepard, C., Oo, A., Arizaga, F., Kapoor-Vazirani, P., Persaud, M., Yu, C. H., Kim, D. - H., Schinazi, R. F., Ivanov, D. N., Diaz-Griffero, F., Yu, D. S., Xiong, Y., and Kim, B. (2021) Structural and functional characterization explains loss of dNTPase activity of the cancer-specific R366C/H mutant SAMHD1 proteins. J Biol Chem. 10.1016/j.jbc.2021.101170
Bowman, B. R., Lee, S., Wang, S., and Verdine, G. L. (2010) Structure of Escherichia coli AlkA in complex with undamaged DNA. J Biol Chem. 285, 35783-91
Bowman, B. R., Lee, S., Wang, S., and Verdine, G. L. (2008) Structure of the E. coli DNA glycosylase AlkA bound to the ends of duplex DNA: a system for the structure determination of lesion-containing DNA. Structure. 16, 1166-74

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