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Bosnakovski, D., Toso, E. A., Ener, E. T., Gearhart, M. D., Yin, L., Lüttmann, F. F., Magli, A., Shi, K., Kim, J., Aihara, H., and Kyba, M. (2023) Antagonism among DUX family members evolved from an ancestral toxic single homeodomain protein. iScience. 26, 107823
Boughton, A. J., Krueger, S., and Fushman, D. (2020) Branching via K11 and K48 Bestows Ubiquitin Chains with a Unique Interdomain Interface and Enhanced Affinity for Proteasomal Subunit Rpn1. Structure. 28, 29-43.e6
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. (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
Boys, I. N., Johnson, A. G., Quinlan, M., Kranzusch, P. J., and Elde, N. C. (2023) Structural homology screens reveal poxvirus-encoded proteins impacting inflammasome-mediated defenses. bioRxiv. 10.1101/2023.02.26.529821
Boys, I. N., Johnson, A. G., Quinlan, M. R., Kranzusch, P. J., and Elde, N. C. (2023) Structural homology screens reveal host-derived poxvirus protein families impacting inflammasome activity. Cell Rep. 42, 112878
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
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
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
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
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
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
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
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
Brogan, A. P., Habib, C., Hobbs, S. J., Kranzusch, P. J., and Rudner, D. Z. (2023) Bacterial SEAL domains undergo autoproteolysis and function in regulated intramembrane proteolysis. Proc Natl Acad Sci U S A. 120, e2310862120
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., Campbell, E. B., and MacKinnon, R. (2014) Physical mechanism for gating and mechanosensitivity of the human TRAAK K+ channel. Nature. 516, 126-30
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., 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., 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., 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
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

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