Publications

Found 2717 results
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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., 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
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
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., and Schwartz, T. U. (2007) Purification, crystallization and preliminary X-ray analysis of a Nup107-Nup133 heterodimeric nucleoporin complex. Acta Crystallogr Sect F Struct Biol Cryst Commun. 63, 816-8
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
Bodnar, N. O., Kim, K. H., Ji, Z., Wales, T. E., Svetlov, V., Nudler, E., Engen, J. R., Walz, T., and Rapoport, T. A. (2018) Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4. Nat Struct Mol Biol. 25, 616-622
Bodnar, N. (2018) Mechanism and Structure of the Cdc48 ATPase Complex. Ph.D. thesis, Harvard University, Cambridge, Massachusetts
Bodea, S., Funk, M. A., Balskus, E. P., and Drennan, C. L. (2016) Molecular Basis of C-N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase. Cell Chem Biol. 23, 1206-1216
Bobik, T. A., Morales, E. J., Shin, A., Cascio, D., Sawaya, M. R., Arbing, M., Yeates, T. O., and Rasche, M. E. (2014) Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii. Acta Crystallogr F Struct Biol Commun. 70, 1472-9
Blus, B. J., Hashimoto, H., Seo, H. - S., Krolak, A., and Debler, E. W. (2019) Substrate Affinity and Specificity of the ScSth1p Bromodomain Are Fine-Tuned for Versatile Histone Recognition. Structure. 27, 1460-1468.e3
Blumberg, L. J., Humphries, J. E., Jones, S. D., Pearce, L. B., Holgate, R., Hearn, A., Cheung, J., Mahmood, A., Del Tito, B., Graydon, J. S., Stolz, L. E., Bitonti, A., Purohit, S., de Graaf, D., Kacena, K., Andersen, J. T., Christianson, G. J., Roopenian, D. C., Hubbard, J. J., Gandhi, A. K., Lasseter, K., Pyzik, M., and Blumberg, R. S. (2019) Blocking FcRn in humans reduces circulating IgG levels and inhibits IgG immune complex-mediated immune responses. Sci Adv. 5, eaax9586
Blum, E., Zhang, J., Zaluski, J., Einstein, D. E., Korshin, E. E., Kubas, A., Gruzman, A., Tochtrop, G. P., Kiser, P. D., and Palczewski, K. (2021) Rational Alteration of Pharmacokinetics of Chiral Fluorinated and Deuterated Derivatives of Emixustat for Retinal Therapy. J Med Chem. 10.1021/acs.jmedchem.1c00279
Blower, T. R., Williamson, B. H., Kerns, R. J., and Berger, J. M. (2016) Crystal structure and stability of gyrase-fluoroquinolone cleaved complexes from Mycobacterium tuberculosis. Proc Natl Acad Sci U S A. 113, 1706-13
Bloch, J. S., Mukherjee, S., Kowal, J., Filippova, E. V., Niederer, M., Pardon, E., Steyaert, J., Kossiakoff, A. A., and Locher, K. P. (2021) Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins. Proc Natl Acad Sci U S A. 10.1073/pnas.2115435118
Blobaum, A. L., Xu, S., Rowlinson, S. W., Duggan, K. C., Banerjee, S., Kudalkar, S. N., Birmingham, W. R., Ghebreselasie, K., and Marnett, L. J. (2015) Action at a distance: mutations of peripheral residues transform rapid reversible inhibitors to slow, tight binders of cyclooxygenase-2. J Biol Chem. 290, 12793-803

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