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Brohawn, S. G., del Mármol, J., and MacKinnon, R. (2012) Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive K+ ion channel. Science. 335, 436-41
Brosey, C. A., Houl, J. H., Katsonis, P., Balapiti-Modarage, L. P. F., Bommagani, S., Arvai, A., Moiani, D., Bacolla, A., Link, T., Warden, L. S., Lichtarge, O., Jones, D. E., Ahmed, Z., and Tainer, J. A. (2021) Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors. Prog Biophys Mol Biol. 10.1016/j.pbiomolbio.2021.02.002
Broussard, T. C., Pakhomova, S., Neau, D. B., Bonnot, R., and Waldrop, G. L. (2015) Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase. Biochemistry. 54, 3860-70
Broussard, T. C., Kobe, M. J., Pakhomova, S., Neau, D. B., Price, A. E., Champion, T. S., and Waldrop, G. L. (2013) The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase. Structure. 21, 650-7
Brown, N. G., VanderLinden, R., Watson, E. R., Qiao, R., Grace, C. R. R., Yamaguchi, M., Weissmann, F., Frye, J. J., Dube, P., Cho, S. Ei, Actis, M. L., Rodrigues, P., Fujii, N., Peters, J. - M., Stark, H., and Schulman, B. A. (2015) RING E3 mechanism for ubiquitin ligation to a disordered substrate visualized for human anaphase-promoting complex. Proc Natl Acad Sci U S A. 112, 5272-9
Brown, K. L., Banerjee, S., Feigley, A., Abe, H., Blackwell, T. S., Pozzi, A., Hudson, B. G., and Zent, R. (2018) Salt-bridge modulates differential calcium-mediated ligand binding to integrin α1- and α2-I domains.. Sci Rep. 8, 2916
Brown, N. G., Watson, E. R., Weissmann, F., Jarvis, M. A., VanderLinden, R., Grace, C. R. R., Frye, J. J., Qiao, R., Dube, P., Petzold, G., Cho, S. Ei, Alsharif, O., Bao, J., Davidson, I. F., Zheng, J. J., Nourse, A., Kurinov, I., Peters, J. - M., Stark, H., and Schulman, B. A. (2014) Mechanism of polyubiquitination by human anaphase-promoting complex: RING repurposing for ubiquitin chain assembly. Mol Cell. 56, 246-260
Brown, N. G., VanderLinden, R., Watson, E. R., Weissmann, F., Ordureau, A., Wu, K. - P., Zhang, W., Yu, S., Mercredi, P. Y., Harrison, J. S., Davidson, I. F., Qiao, R., Lu, Y., Dube, P., Brunner, M. R., Grace, C. R. R., Miller, D. J., Haselbach, D., Jarvis, M. A., Yamaguchi, M., Yanishevski, D., Petzold, G., Sidhu, S. S., Kuhlman, B., Kirschner, M. W., J Harper, W., Peters, J. - M., Stark, H., and Schulman, B. A. (2016) Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. Cell. 165, 1440-1453
Brown, B. L., Kardon, J. R., Sauer, R. T., and Baker, T. A. (2018) Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. Structure. 10.1016/j.str.2018.02.012
Brown, J. A., Bulkley, D., Wang, J., Valenstein, M. L., Yario, T. A., Steitz, T. A., and Steitz, J. A. (2014) Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix. Nat Struct Mol Biol. 21, 633-40
Brown, S., Gauvin, C. C., Charbonneau, A. A., Burman, N., and C Lawrence, M. (2020) Csx3 is a cyclic oligonucleotide phosphodiesterase associated with type III CRISPR-Cas that degrades the second messenger cA. J Biol Chem. 295, 14963-14972
Bruce, H. A., Singer, A. U., Filippova, E. V., Blazer, L. L., Adams, J. J., Enderle, L., Ben-David, M., Radley, E. H., Mao, D. Y. L., Pau, V., Orlicky, S., Sicheri, F., Kourinov, I., Atwell, S., Kossiakoff, A. A., and Sidhu, S. S. (2023) Engineered Antigen-Binding Fragments for Enhanced Crystallization of Antibody:Antigen Complexes. Protein Sci. 10.1002/pro.4824
Bruce, H. A., Singer, A. U., Blazer, L. L., Luu, K., Ploder, L., Pavlenco, A., Kurinov, I., Adams, J. J., and Sidhu, S. S. (2024) Antigen-binding fragments with improved crystal lattice packing and enhanced conformational flexibility at the elbow region as crystallization chaperones. Protein Sci. 33, e5081
Bruender, N. A., Grell, T. A. J., Dowling, D. P., McCarty, R. M., Drennan, C. L., and Bandarian, V. (2017) 7-Carboxy-7-deazaguanine Synthase: A Radical S-Adenosyl-l-methionine Enzyme with Polar Tendencies. J Am Chem Soc. 139, 1912-1920
Brugarolas, P., Movahedzadeh, F., Wang, Y., Zhang, N., Bartek, I. L., Gao, Y. N., Voskuil, M. I., Franzblau, S. G., and He, C. (2012) The oxidation-sensing regulator (MosR) is a new redox-dependent transcription factor in Mycobacterium tuberculosis. J Biol Chem. 287, 37703-12
Brugger, C., Schwartz, J., Novick, S., Tong, S., Hoskins, J., Majdalani, N., Kim, R., Filipovski, M., Wickner, S., Gottesman, S., Griffin, P., and Deaconescu, A. M. (2023) Structure of Phosphorylated-like RssB, the Adaptor Delivering σ to the ClpXP Proteolytic Machinery, Reveals an Interface Switch for Activation.. J Biol Chem. 10.1016/j.jbc.2023.105440
Brumshtein, B., Esswein, S. R., Landau, M., Ryan, C. M., Whitelegge, J. P., Phillips, M. L., Cascio, D., Sawaya, M. R., and Eisenberg, D. S. (2014) Formation of amyloid fibers by monomeric light chain variable domains. J Biol Chem. 289, 27513-25
Brumshtein, B., Esswein, S. R., Sawaya, M. R., Rosenberg, G., Ly, A. T., Landau, M., and Eisenberg, D. S. (2018) Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light chain amyloidosis. J Biol Chem. 10.1074/jbc.RA118.004142
Brumshtein, B., Esswein, S. R., Salwinski, L., Phillips, M. L., Ly, A. T., Cascio, D., Sawaya, M. R., and Eisenberg, D. S. (2015) Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain. Elife. 4, e10935
Brunette, T. J., Bick, M. J., Hansen, J. M., Chow, C. M., Kollman, J. M., and Baker, D. (2020) Modular repeat protein sculpting using rigid helical junctions. Proc Natl Acad Sci U S A. 10.1073/pnas.1908768117
Bryan, C. M., Rocklin, G. J., Bick, M. J., Ford, A., Majri-Morrison, S., Kroll, A. V., Miller, C. J., Carter, L., Goreshnik, I., Kang, A., DiMaio, F., Tarbell, K. V., and Baker, D. (2021) Computational design of a synthetic PD-1 agonist. Proc Natl Acad Sci U S A. 10.1073/pnas.2102164118
Bryk, R., Arango, N., Maksymiuk, C., Balakrishnan, A., Wu, Y. - T., Wong, C. - H., Masquelin, T., Hipskind, P., Lima, C. D., and Nathan, C. (2013) Lipoamide channel-binding sulfonamides selectively inhibit mycobacterial lipoamide dehydrogenase. Biochemistry. 52, 9375-84
Bryk, R., Arango, N., Venugopal, A., J Warren, D., Park, Y. - H., Patel, M. S., Lima, C. D., and Nathan, C. (2010) Triazaspirodimethoxybenzoyls as selective inhibitors of mycobacterial lipoamide dehydrogenase . Biochemistry. 49, 1616-27
Bryson, D. I., Fan, C., Guo, L. - T., Miller, C., Söll, D., and Liu, D. R. (2017) Continuous directed evolution of aminoacyl-tRNA synthetases. Nat Chem Biol. 13, 1253-1260
Brzezinski, K., Dauter, Z., Baj, A., Wałejko, P., and Witkowski, S. (2011) rac-6-Hy-droxy-2,5,7,8-tetra-methyl-chroman-2-carboxamide from synchrotron data. Acta Crystallogr Sect E Struct Rep Online. 67, o503-4

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