Publications

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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, 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
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
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
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
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., 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
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
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
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
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
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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