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Bethel, N. P., Borst, A. J., Parmeggiani, F., Bick, M. J., Brunette, T. J., Nguyen, H., Kang, A., Bera, A. K., Carter, L., Miranda, M. C., Kibler, R. D., Lamb, M., Li, X., Sankaran, B., and Baker, D. (2023) Precisely patterned nanofibres made from extendable protein multiplexes. Nat Chem. 10.1038/s41557-023-01314-x
Beyett, T. S., To, C., Heppner, D. E., Rana, J. K., Schmoker, A. M., Jang, J., De Clercq, D. J. H., Gomez, G., Scott, D. A., Gray, N. S., Jänne, P. A., and Eck, M. J. (2022) Molecular basis for cooperative binding and synergy of ATP-site and allosteric EGFR inhibitors. Nat Commun. 13, 2530
Beyett, T. S., Rana, J. K., Schaeffner, I. K., Heppner, D. E., and Eck, M. J. (2024) Structural Analysis of the Macrocyclic Inhibitor BI-4020 Binding to EGFR Kinase. ChemMedChem. 19, e202300343
Bhandari, S., Biswas, S., Chaudhary, A., Dutta, S., and Suguna, K. (2019) Dodecameric structure of a small heat shock protein from Mycobacterium marinum M. Proteins. 10.1002/prot.25657
Bhardwaj, G., O'Connor, J., Rettie, S., Huang, Y. - H., Ramelot, T. A., Mulligan, V. Khipple, Alpkilic, G. Gokce, Palmer, J., Bera, A. K., Bick, M. J., Di Piazza, M., Li, X., Hosseinzadeh, P., Craven, T. W., Tejero, R., Lauko, A., Choi, R., Glynn, C., Dong, L., Griffin, R., van Voorhis, W. C., Rodriguez, J., Stewart, L., Montelione, G. T., Craik, D., and Baker, D. (2022) Accurate de novo design of membrane-traversing macrocycles. Cell. 10.1016/j.cell.2022.07.019
Bhardwaj, R., Lindinger, S., Neuberger, A., Nadezhdin, K. D., Singh, A. K., Cunha, M. R., Derler, I., Gyimesi, G., Reymond, J. - L., Hediger, M. A., Romanin, C., and Sobolevsky, A. I. (2020) Inactivation-mimicking block of the epithelial calcium channel TRPV6. Sci Adv. 10.1126/sciadv.abe1508
Bhattacharjee, D., Bakar, J., Chitnis, S. P., Sausville, E. L., Ashtekar, K. Dilip, Mendelson, B. E., Long, K., Smith, J. C., Heppner, D. E., and Sheltzer, J. M. (2023) Inhibition of a lower potency target drives the anticancer activity of a clinical p38 inhibitor. Cell Chem Biol. 30, 1211-1222.e5
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
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
Bi, Y., Mann, E., Whitfield, C., and Zimmer, J. (2018) Architecture of a channel-forming O-antigen polysaccharide ABC transporter. Nature. 553, 361-365
Bick, M. J., Banik, J. J., Darst, S. A., and Brady, S. F. (2010) Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone. Biochemistry. 49, 4159-68
Bick, M. J., Lamour, V., Rajashankar, K. R., Gordiyenko, Y., Robinson, C. V., and Darst, S. A. (2009) How to switch off a histidine kinase: crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda. J Mol Biol. 386, 163-77
Biester, A., Dementin, S., and Drennan, C. L. (2022) Visualizing the gas channel of a monofunctional carbon monoxide dehydrogenase. J Inorg Biochem. 230, 111774
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
Bilokapic, S., and Schwartz, T. U. (2012) Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex. Proc Natl Acad Sci U S A. 109, 15241-6
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
Blaha, G., Stanley, R. E., and Steitz, T. A. (2009) Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome. Science. 325, 966-70
Blaha, G., Gürel, G., Schroeder, S. J., Moore, P. B., and Steitz, T. A. (2008) Mutations outside the anisomycin-binding site can make ribosomes drug-resistant. J Mol Biol. 379, 505-19
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., Pemberton, T. A., Chow, J. - Y., C Poulter, D., and Christianson, D. W. (2018) Crystal Structure of Cucumene Synthase, a Terpenoid Cyclase That Generates a Linear Triquinane Sesquiterpene. Biochemistry. 57, 6326-6335
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., Barrow, G. H., and Christianson, D. W. (2019) Crystal structure of F95Q epi-isozizaene synthase, an engineered sesquiterpene cyclase that generates biofuel precursors β- and γ-curcumene.. J Struct Biol. 207, 218-224
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
Blankenchip, C. L., Nguyen, J. V., Lau, R. K., Ye, Q., Gu, Y., and Corbett, K. D. (2022) Control of bacterial immune signaling by a WYL domain transcription factor. Nucleic Acids Res. 50, 5239-5250

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