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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, 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, 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, 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
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
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
Brohawn, S. G., Leksa, N. C., Spear, E. D., Rajashankar, K. R., and Schwartz, T. U. (2008) Structural evidence for common ancestry of the nuclear pore complex and vesicle coats. Science. 322, 1369-73
Brohawn, S. G., Wang, W., Handler, A., Campbell, E. B., Schwarz, J. R., and MacKinnon, R. (2019) The mechanosensitive ion channel TRAAK is localized to the mammalian node of Ranvier. Elife. 10.7554/eLife.50403
Brohawn, S. G., and Schwartz, T. U. (2009) Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice. Nat Struct Mol Biol. 16, 1173-7
Brohawn, S. G., Campbell, E. B., and MacKinnon, R. (2014) Physical mechanism for gating and mechanosensitivity of the human TRAAK K+ channel. Nature. 516, 126-30
Bridwell-Rabb, J., Zhong, A., Sun, H. G., Drennan, C. L., and Liu, H. -wen (2017) A B12-dependent radical SAM enzyme involved in oxetanocin A biosynthesis. Nature. 544, 322-326
Bridwell-Rabb, J., Kang, G., Zhong, A., Liu, H. -wen, and Drennan, C. L. (2016) An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis. Proc Natl Acad Sci U S A. 113, 13750-13755
Brewer, M. Red, Yun, C. -hong, Lai, D., Lemmon, M. A., Eck, M. J., and Pao, W. (2013) Mechanism for activation of mutated epidermal growth factor receptors in lung cancer. Proc Natl Acad Sci U S A. 110, E3595-604
Brasch, J., Goodman, K. M., Noble, A. J., Rapp, M., Mannepalli, S., Bahna, F., Dandey, V. P., Bepler, T., Berger, B., Maniatis, T., Potter, C. S., Carragher, B., Honig, B., and Shapiro, L. (2019) Visualization of clustered protocadherin neuronal self-recognition complexes. Nature. 569, 280-283
Braffman, N. R., Piscotta, F. J., Hauver, J., Campbell, E. A., A Link, J., and Darst, S. A. (2019) Structural mechanism of transcription inhibition by lasso peptides microcin J25 and capistruin. Proc Natl Acad Sci U S A. 116, 1273-1278
Bradshaw, N., Levdikov, V. M., Zimanyi, C. M., Gaudet, R., Wilkinson, A. J., and Losick, R. (2017) A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases. Elife. 10.7554/eLife.26111
Bradley, T., Fera, D., Bhiman, J., Eslamizar, L., Lu, X., Anasti, K., Zhang, R., Sutherland, L. L., Scearce, R. M., Bowman, C. M., Stolarchuk, C., Lloyd, K. E., Parks, R., Eaton, A., Foulger, A., Nie, X., Karim, S. S. Abdool, Barnett, S., Kelsoe, G., Kepler, T. B., S Alam, M., Montefiori, D. C., M Moody, A., Liao, H. - X., Morris, L., Santra, S., Harrison, S. C., and Haynes, B. F. (2016) Structural Constraints of Vaccine-Induced Tier-2 Autologous HIV Neutralizing Antibodies Targeting the Receptor-Binding Site. Cell Rep. 14, 43-54
Bozzi, A. T., Bane, L. B., Weihofen, W. A., Singharoy, A., Guillen, E. R., Ploegh, H. L., Schulten, K., and Gaudet, R. (2016) Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter. Structure. 24, 2102-2114
Bozzi, A. T., Zimanyi, C. M., Nicoludis, J. M., Lee, B. K., Zhang, C. H., and Gaudet, R. (2019) Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter. Elife. 10.7554/eLife.41124
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
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
Borowska, M. T., Dominik, P. K., S Anghel, A., Kossiakoff, A. A., and Keenan, R. J. (2015) A YidC-like Protein in the Archaeal Plasma Membrane. Structure. 23, 1715-1724
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
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

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