Found 2702 results
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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
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
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
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
Borowska, M. T., Drees, C., Yarawsky, A. E., Viswanathan, M., Ryan, S. M., Bunker, J. J., Herr, A. B., Bendelac, A., and Adams, E. J. (2021) The molecular characterization of antibody binding to a superantigen-like protein from a commensal microbe. Proc Natl Acad Sci U S A. 10.1073/pnas.2023898118
Borowska, M. T., Boughter, C. T., Bunker, J. J., Guthmiller, J. J., Wilson, P. C., Roux, B., Bendelac, A., and Adams, E. J. (2023) Biochemical and biophysical characterization of natural polyreactivity in antibodies. Cell Rep. 42, 113190
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
Bonsor, D. A., Alexander, P., Snead, K., Hartig, N., Drew, M., Messing, S., Finci, L. I., Nissley, D. V., McCormick, F., Esposito, D., Rodriguez-Viciana, P., Stephen, A. G., and Simanshu, D. K. (2022) Structure of the SHOC2-MRAS-PP1C complex provides insights into RAF activation and Noonan syndrome. Nat Struct Mol Biol. 29, 966-977
Bonsignori, M., Kreider, E. F., Fera, D., R Meyerhoff, R., Bradley, T., Wiehe, K., S Alam, M., Aussedat, B., Walkowicz, W. E., Hwang, K. - K., Saunders, K. O., Zhang, R., Gladden, M. A., Monroe, A., Kumar, A., Xia, S. - M., Cooper, M., Louder, M. K., McKee, K., Bailer, R. T., Pier, B. W., Jette, C. A., Kelsoe, G., Williams, W. B., Morris, L., Kappes, J., Wagh, K., Kamanga, G., Cohen, M. S., Hraber, P. T., Montefiori, D. C., Trama, A., Liao, H. - X., Kepler, T. B., M Moody, A., Gao, F., Danishefsky, S. J., Mascola, J. R., Shaw, G. M., Hahn, B. H., Harrison, S. C., Korber, B. T., and Haynes, B. F. (2017) Staged induction of HIV-1 glycan-dependent broadly neutralizing antibodies. Sci Transl Med. 10.1126/scitranslmed.aai7514
Bolon, D. N., Grant, R. A., Baker, T. A., and Sauer, R. T. (2004) Nucleotide-dependent substrate handoff from the SspB adaptor to the AAA+ ClpXP protease. Mol Cell. 16, 343-50
Bolon, D. N., Grant, R. A., Baker, T. A., and Sauer, R. T. (2005) Specificity versus stability in computational protein design. Proc Natl Acad Sci U S A. 102, 12724-9
Bollmeyer, M. M., Coleman, R. E., Majer, S. H., Ferrao, S. D., and Lancaster, K. M. (2023) Cytochrome P460 Cofactor Maturation Proceeds via Peroxide-Dependent Post-translational Modification. J Am Chem Soc. 145, 14404-14416
Bollenbach, M., Ortega, M., Orman, M., Drennan, C. L., and Balskus, E. P. (2020) Discovery of a Cyclic Choline Analog That Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. ACS Med Chem Lett. 11, 1980-1985
Bolla, J. Reddy, Su, C. - C., Delmar, J. A., Radhakrishnan, A., Kumar, N., Chou, T. - H., Long, F., Rajashankar, K. R., and Yu, E. W. (2015) Crystal structure of the Alcanivorax borkumensis YdaH transporter reveals an unusual topology. Nat Commun. 6, 6874
Bolla, J. Reddy, Su, C. - C., Do, S. V., Radhakrishnan, A., Kumar, N., Long, F., Chou, T. - H., Delmar, J. A., Lei, H. - T., Rajashankar, K. R., Shafer, W. M., and Yu, E. W. (2014) Crystal structure of the Neisseria gonorrhoeae MtrD inner membrane multidrug efflux pump. PLoS One. 9, e97903
Bolla, J. Reddy, Do, S. V., Long, F., Dai, L., Su, C. - C., Lei, H. - T., Chen, X., Gerkey, J. E., Murphy, D. C., Rajashankar, K. R., Zhang, Q., and Yu, E. W. (2012) Structural and functional analysis of the transcriptional regulator Rv3066 of Mycobacterium tuberculosis. Nucleic Acids Res. 40, 9340-55
Bohl, T. E., Ieong, P., Lee, J. K., Lee, T., Kankanala, J., Shi, K., Demir, Ö., Kurahashi, K., Amaro, R. E., Wang, Z., and Aihara, H. (2018) The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem. 10.1074/jbc.RA118.002503
Bohl, T. E., Shi, K., Lee, J. K., and Aihara, H. (2018) Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli. Nat Commun. 9, 377
Bogner, A. N., Ji, J., and Tanner, J. J. (2022) Structure-based engineering of minimal Proline dehydrogenase domains for inhibitor discovery. Protein Eng Des Sel. 10.1093/protein/gzac016
Bogner, A. N., Stiers, K. M., McKay, C. M., Becker, D. F., and Tanner, J. J. (2021) Structural Basis for the Stereospecific Inhibition of the Dual Proline/Hydroxyproline Catabolic Enzyme ALDH4A1 by Trans-4-Hydroxy-L-Proline. Protein Sci. 10.1002/pro.4131
Bogner, A. N., and Tanner, J. J. (2022) Structure-affinity relationships of reversible proline analog inhibitors targeting proline dehydrogenase. Org Biomol Chem. 10.1039/d1ob02328d
Boekhout, M., Karasu, M. E., Wang, J., Acquaviva, L., Pratto, F., Brick, K., Eng, D. Y., Xu, J., R Camerini-Otero, D., Patel, D. J., and Keeney, S. (2019) REC114 Partner ANKRD31 Controls Number, Timing, and Location of Meiotic DNA Breaks. Mol Cell. 10.1016/j.molcel.2019.03.023
Boehmer, T., Jeudy, S., Berke, I. C., and Schwartz, T. U. (2008) Structural and functional studies of Nup107/Nup133 interaction and its implications for the architecture of the nuclear pore complex. Mol Cell. 30, 721-31