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Benjamin, B., Goldgur, Y., Jork, N., Jessen, H. J., Schwer, B., and Shuman, S. (2022) Structures of Fission Yeast Inositol Pyrophosphate Kinase Asp1 in Ligand-Free, Substrate-Bound, and Product-Bound States. mBio. 10.1128/mbio.03087-22
Benavides, B. S., Valandro, S., Cioloboc, D., Taylor, A. B., Schanze, K. S., and Kurtz, D. M. (2020) Structure of a Zinc Porphyrin-Substituted Bacterioferritin and Photophysical Properties of Iron Reduction. Biochemistry. 59, 1618-1629
Ben-Nun, Y., Seo, H. - S., Harvey, E. P., Hauseman, Z. J., Wales, T. E., Newman, C. E., Cathcart, A. M., Engen, J. R., Dhe-Paganon, S., and Walensky, L. D. (2020) Identification of a Structural Determinant for Selective Targeting of HDMX. Structure. 28, 847-857.e5
Bellizzi, J. J., Sorger, P. K., and Harrison, S. C. (2007) Crystal structure of the yeast inner kinetochore subunit Cep3p. Structure. 15, 1422-30
Békés, M., van Noort, G. J. van der, Ekkebus, R., Ovaa, H., Huang, T. T., and Lima, C. D. (2016) Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease. Mol Cell. 62, 572-85
Begley, M. J., Yun, C. -hong, Gewinner, C. A., Asara, J. M., Johnson, J. L., Coyle, A. J., Eck, M. J., Apostolou, I., and Cantley, L. C. (2015) EGF-receptor specificity for phosphotyrosine-primed substrates provides signal integration with Src. Nat Struct Mol Biol. 22, 983-90
Becker, A., Kannan, T. R., Taylor, A. B., Pakhomova, O. N., Zhang, Y., Somarajan, S. R., Galaleldeen, A., Holloway, S. P., Baseman, J. B., and P Hart, J. (2015) Structure of CARDS toxin, a unique ADP-ribosylating and vacuolating cytotoxin from Mycoplasma pneumoniae. Proc Natl Acad Sci U S A. 112, 5165-70
Bazzoli, A., Vance, D. J., Rudolph, M. J., Rong, Y., Angalakurthi, S. Krishna, Toth, R. T., C Middaugh, R., Volkin, D. B., Weis, D. D., Karanicolas, J., and Mantis, N. J. (2017) Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies. Proteins. 85, 1994-2008
Baytshtok, V., Chen, J., Glynn, S. E., Nager, A. R., Grant, R. A., Baker, T. A., and Sauer, R. T. (2017) Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation. J Biol Chem. 292, 5695-5704
Baytshtok, V., Fei, X., Shih, T. - T., Grant, R. A., Santos, J. C., Baker, T. A., and Sauer, R. T. (2021) Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Cell Rep. 34, 108639
Baytshtok, V., Fei, X., Grant, R. A., Baker, T. A., and Sauer, R. T. (2016) A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure. 24, 1766-1777
Bauer, J. A., Bennett, E. M., Begley, T. P., and Ealick, S. E. (2004) Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5'-phosphate biosynthesis. J Biol Chem. 279, 2704-11
Battaglia, R. A., Price, I. R., and Ke, A. (2017) Structural basis for guanidine sensing by the ykkC family of riboswitches. RNA. 23, 578-585
Battaglia, R. A., Grigg, J. C., and Ke, A. (2019) Structural basis for tRNA decoding and aminoacylation sensing by T-box riboregulators. Nat Struct Mol Biol. 26, 1106-1113
Batool, Z., Lomakin, I. B., Polikanov, Y. S., and Bunick, C. G. (2020) Sarecycline interferes with tRNA accommodation and tethers mRNA to the 70S ribosome. Proc Natl Acad Sci U S A. 10.1073/pnas.2008671117
Batool, Z., Pavlova, J. A., Paranjpe, M. N., Tereshchenkov, A. G., Lukianov, D. A., Osterman, I. A., Bogdanov, A. A., Sumbatyan, N. V., and Polikanov, Y. S. (2024) Berberine analog of chloramphenicol exhibits a distinct mode of action and unveils ribosome plasticity. Structure. 10.1016/j.str.2024.06.013
Batki, J., Schnabl, J., Wang, J., Handler, D., Andreev, V. I., Stieger, C. E., Novatchkova, M., Lampersberger, L., Kauneckaite, K., Xie, W., Mechtler, K., Patel, D. J., and Brennecke, J. (2019) The nascent RNA binding complex SFiNX licenses piRNA-guided heterochromatin formation. Nat Struct Mol Biol. 26, 720-731
Basu, R., Eichhorn, C. D., Cheng, R., Peterson, R. D., and Feigon, J. (2020) Structure of telomerase protein Pof8 C-terminal domain is an xRRM conserved among LARP7 proteins. RNA Biol. 10.1080/15476286.2020.1836891
Bassetto, M., Zaluski, J., Li, B., Zhang, J., Badiee, M., Kiser, P. D., and Tochtrop, G. P. (2023) Tuning the Metabolic Stability of Visual Cycle Modulators through Modification of an RPE65 Recognition Motif. J Med Chem. 66, 8140-8158
Baskin, J. M., Wu, X., Christiano, R., Oh, M. S., Schauder, C. M., Gazzerro, E., Messa, M., Baldassari, S., Assereto, S., Biancheri, R., Zara, F., Minetti, C., Raimondi, A., Simons, M., Walther, T. C., Reinisch, K. M., and De Camilli, P. (2016) The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane.. Nat Cell Biol. 18, 132-8
Basavalingappa, V., Bera, S., Xue, B., Azuri, I., Tang, Y., Tao, K., Shimon, L. J. W., Sawaya, M. R., Kolusheva, S., Eisenberg, D. S., Kronik, L., Cao, Y., Wei, G., and Gazit, E. (2019) Mechanically rigid supramolecular assemblies formed from an Fmoc-guanine conjugated peptide nucleic acid. Nat Commun. 10, 5256
Basak, S., Schmandt, N., Gicheru, Y., and Chakrapani, S. (2017) Crystal structure and dynamics of a lipid-induced potential desensitized-state of a pentameric ligand-gated channel. Elife. 10.7554/eLife.23886
Barton, W. A., Liu, B. P., Tzvetkova, D., Jeffrey, P. D., Fournier, A. E., Sah, D., Cate, R., Strittmatter, S. M., and Nikolov, D. B. (2003) Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins. EMBO J. 22, 3291-302
Barton, W. A., Tzvetkova-Robev, D., Miranda, E. P., Kolev, M. V., Rajashankar, K. R., Himanen, J. P., and Nikolov, D. B. (2006) Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex. Nat Struct Mol Biol. 13, 524-32
Barnes, C. L., Salom, D., Namitz, K. E. W., W Smith, C., Knutson, B. A., Cosgrove, M. S., Kiser, P. D., and Calvert, P. D. (2024) Mechanisms of amphibian arrestin 1 self-association and dynamic distribution in retinal photoreceptors. J Biol Chem. 300, 107966

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