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Chen, Y., Bauer, B. W., Rapoport, T. A., and Gumbart, J. C. (2015) Conformational Changes of the Clamp of the Protein Translocation ATPase SecA. J Mol Biol. 427, 2348-59
Wang, L., Ferrao, R., Li, Q., Hatcher, J. M., Choi, H. Geun, Buhrlage, S. J., Gray, N. S., and Wu, H. (2019) Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4). J Biol Chem. 10.1074/jbc.RA118.005428
Blankenship, E., Vukoti, K., Miyagi, M., and Lodowski, D. T. (2014) Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state. Acta Crystallogr D Biol Crystallogr. 70, 833-40
Raymond, D. D., Bajic, G., Ferdman, J., Suphaphiphat, P., Settembre, E. C., M Moody, A., Schmidt, A. G., and Harrison, S. C. (2018) Conserved epitope on influenza-virus hemagglutinin head defined by a vaccine-induced antibody. Proc Natl Acad Sci U S A. 115, 168-173
Buffalo, C. Z., Bahn-Suh, A. J., Hirakis, S. P., Biswas, T., Amaro, R. E., Nizet, V., and Ghosh, P. (2016) Conserved patterns hidden within group A Streptococcus M protein hypervariability recognize human C4b-binding protein. Nat Microbiol. 1, 16155
Buffalo, C. Z., Bahn-Suh, A. J., Hirakis, S. P., Biswas, T., Amaro, R. E., Nizet, V., and Ghosh, P. (2016) Conserved patterns hidden within group A Streptococcus M protein hypervariability recognize human C4b-binding protein. Nat Microbiol. 1, 16155
Buffalo, C. Z., Bahn-Suh, A. J., Hirakis, S. P., Biswas, T., Amaro, R. E., Nizet, V., and Ghosh, P. (2016) Conserved patterns hidden within group A Streptococcus M protein hypervariability recognize human C4b-binding protein. Nat Microbiol. 1, 16155
Bryson, D. I., Fan, C., Guo, L. - T., Miller, C., Söll, D., and Liu, D. R. (2017) Continuous directed evolution of aminoacyl-tRNA synthetases. Nat Chem Biol. 13, 1253-1260
Xia, S., Vashishtha, A., Bulkley, D., Eom, S. Hyun, Wang, J., and Konigsberg, W. H. (2012) Contribution of partial charge interactions and base stacking to the efficiency of primer extension at and beyond abasic sites in DNA. Biochemistry. 51, 4922-31
Li, X., Lee, H., Wu, J., and Breslow, E. (2007) Contributions of the interdomain loop, amino terminus, and subunit interface to the ligand-facilitated dimerization of neurophysin: crystal structures and mutation studies of bovine neurophysin-I. Protein Sci. 16, 52-68
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
Gilbert, N. C., Rui, Z., Neau, D. B., Waight, M. T., Bartlett, S. G., Boeglin, W. E., Brash, A. R., and Newcomer, M. E. (2012) Conversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at Serine-663. FASEB J. 26, 3222-9
Gilbert, N. C., Rui, Z., Neau, D. B., Waight, M. T., Bartlett, S. G., Boeglin, W. E., Brash, A. R., and Newcomer, M. E. (2012) Conversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at Serine-663. FASEB J. 26, 3222-9
Gilbert, N. C., Rui, Z., Neau, D. B., Waight, M. T., Bartlett, S. G., Boeglin, W. E., Brash, A. R., and Newcomer, M. E. (2012) Conversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at Serine-663. FASEB J. 26, 3222-9
Fetherolf, M. M., Boyd, S. D., Taylor, A. B., Kim, H. Jong, Wohlschlegel, J. A., Blackburn, N. J., P Hart, J., Winge, D. R., and Winkler, D. D. (2017) Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site. J Biol Chem. 292, 12025-12040
Fetherolf, M. M., Boyd, S. D., Taylor, A. B., Kim, H. Jong, Wohlschlegel, J. A., Blackburn, N. J., P Hart, J., Winge, D. R., and Winkler, D. D. (2017) Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site. J Biol Chem. 292, 12025-12040
Geng, Y., Deng, Z., Zhang, G., Budelli, G., Butler, A., Yuan, P., Cui, J., Salkoff, L., and Magleby, K. L. (2020) Coupling of Ca and voltage activation in BK channels through the αB helix/voltage sensor interface.. Proc Natl Acad Sci U S A. 117, 14512-14521
Geng, Y., Deng, Z., Zhang, G., Budelli, G., Butler, A., Yuan, P., Cui, J., Salkoff, L., and Magleby, K. L. (2020) Coupling of Ca and voltage activation in BK channels through the αB helix/voltage sensor interface.. Proc Natl Acad Sci U S A. 117, 14512-14521
Ippolito, J. A., Niu, H., Bertoletti, N., Carter, Z. J., Jin, S., Spasov, K. A., Cisneros, J. A., Valhondo, M., Cutrona, K. J., Anderson, K. S., and Jorgensen, W. L. (2021) Covalent Inhibition of Wild-Type HIV-1 Reverse Transcriptase Using a Fluorosulfate Warhead. ACS Med Chem Lett. 12, 249-255
Chan, A. H., Lee, W. - G., Spasov, K. A., Cisneros, J. A., Kudalkar, S. N., Petrova, Z. O., Buckingham, A. B., Anderson, K. S., and Jorgensen, W. L. (2017) Covalent inhibitors for eradication of drug-resistant HIV-1 reverse transcriptase: From design to protein crystallography. Proc Natl Acad Sci U S A. 10.1073/pnas.1711463114
Campbell, A. C., Becker, D. F., Gates, K. S., and Tanner, J. J. (2020) Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate. ACS Chem Biol. 10.1021/acschembio.9b00935
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., 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
Baca, C. F., Yu, Y., Rostøl, J. T., Majumder, P., Patel, D. J., and Marraffini, L. A. (2024) The CRISPR effector Cam1 mediates membrane depolarization for phage defence. Nature. 10.1038/s41586-023-06902-y
Banerjee, S. (2019) The Critical Tools Needed To Deal with Challenging Crystallography. Department of Biophysics & Biophysical Chemistry, Johns Hopkins School of Medicine

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