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Bajic, G., and Harrison, S. C. (2020) Antibodies That Engage the Hemagglutinin Receptor-Binding Site of Influenza B Viruses. ACS Infect Dis. 10.1021/acsinfecdis.0c00726
Bajic, G., Maron, M. J., Adachi, Y., Onodera, T., McCarthy, K. R., McGee, C. E., Sempowski, G. D., Takahashi, Y., Kelsoe, G., Kuraoka, M., and Schmidt, A. G. (2019) Influenza Antigen Engineering Focuses Immune Responses to a Subdominant but Broadly Protective Viral Epitope. Cell Host Microbe. 25, 827-835.e6
R Bajaj, A., Arbing, M. A., Shin, A., Cascio, D., and Miallau, L. (2016) Crystal structure of the toxin Msmeg_6760, the structural homolog of Mycobacterium tuberculosis Rv2035, a novel type II toxin involved in the hypoxic response. Acta Crystallogr F Struct Biol Commun. 72, 863-869
Bailey, L. J., Sheehy, K. M., Dominik, P. K., Liang, W. G., Rui, H., Clark, M., Jaskolowski, M., Kim, Y., Deneka, D., Tang, W. - J., and Kossiakoff, A. A. (2018) Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination. J Mol Biol. 430, 337-347
Bailey, S., Wing, R. A., and Steitz, T. A. (2006) The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases. Cell. 126, 893-904
Bailey, S., Eliason, W. K., and Steitz, T. A. (2007) Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science. 318, 459-63
Baidin, V., Owens, T. W., Lazarus, M. B., and Kahne, D. (2021) Simple Secondary Amines Inhibit Growth of Gram-Negative Bacteria through Highly Selective Binding to Phenylalanyl-tRNA Synthetase. J Am Chem Soc. 143, 623-627
Bai, Y., McCoy, J. G., Levin, E. J., Sobrado, P., Rajashankar, K. R., Fox, B. G., and Zhou, M. (2015) X-ray structure of a mammalian stearoyl-CoA desaturase. Nature. 524, 252-6
Bae, B., Davis, E., Brown, D., Campbell, E. A., Wigneshweraraj, S., and Darst, S. A. (2013) Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of σ70 domain 1.1.. Proc Natl Acad Sci U S A. 110, 19772-7
Bae, B., Feklistov, A., Lass-Napiorkowska, A., Landick, R., and Darst, S. A. (2015) Structure of a bacterial RNA polymerase holoenzyme open promoter complex. Elife. 10.7554/eLife.08504
Bae, H., Viennet, T., Park, E., Chu, N., Salguero, A., Eck, M. J., Arthanari, H., and Cole, P. A. (2022) PH domain-mediated autoinhibition and oncogenic activation of Akt. Elife. 10.7554/eLife.80148
Baconguis, I., and Gouaux, E. (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature. 489, 400-5
Backman, L. Rf, Huang, Y. Y., Andorfer, M. C., Gold, B., Raines, R. T., Balskus, E. P., and Drennan, C. L. (2020) Molecular basis for catabolism of the abundant metabolite -4-hydroxy-L-proline by a microbial glycyl radical enzyme. Elife. 10.7554/eLife.51420
Bacik, J. - P., Walker, J. R., Ali, M., Schimmer, A. D., and Dhe-Paganon, S. (2010) Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5) bound to ATP: mechanistic insights into a minimalistic E1 enzyme. J Biol Chem. 285, 20273-80
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
Babayeva, N. D., Wilder, P. J., Shiina, M., Mino, K., Desler, M., Ogata, K., Rizzino, A., and Tahirov, T. H. (2010) Structural basis of Ets1 cooperative binding to palindromic sequences on stromelysin-1 promoter DNA. Cell Cycle. 9, 3054-62
Babayeva, N. D., Baranovskaya, O. I., and Tahirov, T. H. (2012) Structural basis of Ets1 cooperative binding to widely separated sites on promoter DNA. PLoS One. 7, e33698
Babault, N., Allali-Hassani, A., Li, F., Fan, J., Yue, A., Ju, K., Liu, F., Vedadi, M., Liu, J., and Jin, J. (2018) Discovery of Bisubstrate Inhibitors of Nicotinamide N-Methyltransferase (NNMT). J Med Chem. 61, 1541-1551
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Aziz, F., Reddy, K., Vega, V. Fernandez, Dey, R., Hicks, K. A., Rao, S., Jordan, L. Ortiz, Smith, E., Shumate, J., Scampavia, L., Carpino, N., Spicer, T. P., and French, J. B. (2024) Rebamipide and Derivatives are Potent, Selective Inhibitors of Histidine Phosphatase Activity of the Suppressor of T Cell Receptor Signaling Proteins. J Med Chem. 67, 1949-1960
Ayres, C. A., Schormann, N., Senkovich, O., Fry, A., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2014) Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface. Acta Crystallogr F Struct Biol Commun. 70, 1333-9
Avital-Shmilovici, M., Mandal, K., Gates, Z. P., Phillips, N. B., Weiss, M. A., and Kent, S. B. H. (2013) Fully convergent chemical synthesis of ester insulin: determination of the high resolution X-ray structure by racemic protein crystallography. J Am Chem Soc. 135, 3173-85
Ausin, I., Greenberg, M. V. C., Simanshu, D. K., Hale, C. J., Vashisht, A. A., Simon, S. A., Lee, T. -fen, Feng, S., Española, S. D., Meyers, B. C., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2012) INVOLVED IN DE NOVO 2-containing complex involved in RNA-directed DNA methylation in Arabidopsis. Proc Natl Acad Sci U S A. 109, 8374-81
Atkison, J. H., Parnham, S., Marcotte, W. R., and Olsen, S. K. (2016) Crystal Structure of the Nephila clavipes Major Ampullate Spidroin 1A N-terminal Domain Reveals Plasticity at the Dimer Interface. J Biol Chem. 291, 19006-17
Atapattu, L., Saha, N., Chheang, C., Eissman, M. F., Xu, K., Vail, M. E., Hii, L., Llerena, C., Liu, Z., Horvay, K., Abud, H. E., Kusebauch, U., Moritz, R. L., Ding, B. - S., Cao, Z., Rafii, S., Ernst, M., Scott, A. M., Nikolov, D. B., Lackmann, M., and Janes, P. W. (2016) An activated form of ADAM10 is tumor selective and regulates cancer stem-like cells and tumor growth. J Exp Med. 213, 1741-57
Assadieskandar, A., Yu, C., Maisonneuve, P., Kurinov, I., Sicheri, F., and Zhang, C. (2019) Rigidification Dramatically Improves Inhibitor Selectivity for RAF Kinases. ACS Med Chem Lett. 10, 1074-1080

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