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Brzezinski, K., Brzuszkiewicz, A., Dauter, M., Kubicki, M., Jaskolski, M., and Dauter, Z. (2011) High regularity of Z-DNA revealed by ultra high-resolution crystal structure at 0.55 A. Nucleic Acids Res. 39, 6238-48
Bu, W., Settembre, E. C., Kouni, M. H. el, and Ealick, S. E. (2005) Structural basis for inhibition of Escherichia coli uridine phosphorylase by 5-substituted acyclouridines. Acta Crystallogr D Biol Crystallogr. 61, 863-72
Bubenik, M., Mader, P., Mochirian, P., Vallée, F., Clark, J., Truchon, J. - F., Perryman, A. L., Pau, V., Kurinov, I., Zahn, K. E., Leclaire, M. - E., Papp, R., Mathieu, M. - C., Hamel, M., Duffy, N. M., Godbout, C., Casas-Selves, M., Falgueyret, J. - P., Baruah, P. S., Nicolas, O., Stocco, R., Poirier, H., Martino, G., Fortin, A. Bonneau, Roulston, A., Chefson, A., Dorich, S., St-Onge, M., Patel, P., Pellerin, C., Ciblat, S., Pinter, T., Barabé, F., Bakkouri, M. El, Parikh, P., Gervais, C., Sfeir, A., Mamane, Y., Morris, S. J., W Black, C., Sicheri, F., and Gallant, M. (2022) Identification of , an Orally Bioavailable Compound that Inhibits the DNA Polymerase Activity of Polθ.. J Med Chem. 10.1021/acs.jmedchem.2c00998
Buckley, D. P., Becker, D. F., and Tanner, J. J. (2025) Visualization of Covalent Intermediates and Conformational States of Proline Utilization A by X-ray Crystallography and Molecular Dynamics Simulations. J Biol Chem. 10.1016/j.jbc.2025.110532
Buechner, G. S., Millington, M. E., Perry, K., and D'Antonio, E. L. (2019) The crystal structure of glucokinase from Leishmania braziliensis. Mol Biochem Parasitol. 227, 47-52
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
Bulkley, D., C Innis, A., Blaha, G., and Steitz, T. A. (2010) Revisiting the structures of several antibiotics bound to the bacterial ribosome. Proc Natl Acad Sci U S A. 107, 17158-63
Bulkley, D., Brandi, L., Polikanov, Y. S., Fabbretti, A., O'Connor, M., Gualerzi, C. O., and Steitz, T. A. (2014) The antibiotics dityromycin and GE82832 bind protein S12 and block EF-G-catalyzed translocation. Cell Rep. 6, 357-65
Bunker, R. D., Mandal, K., Bashiri, G., Chaston, J. J., Pentelute, B. L., J Lott, S., Kent, S. B. H., and Baker, E. N. (2015) A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography. Proc Natl Acad Sci U S A. 112, 4310-5
Burdi, D. F., Campbell, J. E., Wang, J., Zhao, S., Zhong, H., Wei, J., Campbell, U., Shao, L., Herman, L., Koch, P., Jones, P. G., and Hewitt, M. C. (2015) Evolution and synthesis of novel orally bioavailable inhibitors of PDE10A. Bioorg Med Chem Lett. 25, 1864-8
Burke, H. G., and Heldwein, E. E. (2015) Crystal Structure of the Human Cytomegalovirus Glycoprotein B. PLoS Pathog. 11, e1005227
Buss, J. M., McTamney, P. M., and Rokita, S. E. (2012) Expression of a soluble form of iodotyrosine deiodinase for active site characterization by engineering the native membrane protein from Mus musculus. Protein Sci. 21, 351-61
Busscher, B. M., Befekadu, H. B., Liu, Z., and Xiao, T. Sam (2023) SARS-CoV-2 ORF3a-Mediated NF-κB Activation Is Not Dependent on TRAF-Binding Sequence.. Viruses. 10.3390/v15112229
Butler, E. B., Xiong, Y., Wang, J., and Strobel, S. A. (2011) Structural basis of cooperative ligand binding by the glycine riboswitch. Chem Biol. 18, 293-8
Buzovetsky, O., Kwon, Y., Pham, N. Tuyet, Kim, C., Ira, G., Sung, P., and Xiong, Y. (2017) Role of the Pif1-PCNA Complex in Pol δ-Dependent Strand Displacement DNA Synthesis and Break-Induced Replication.. Cell Rep. 21, 1707-1714
Buzovetsky, O., Tang, C., Knecht, K. M., Antonucci, J. M., Wu, L., Ji, X., and Xiong, Y. (2018) The SAM domain of mouse SAMHD1 is critical for its activation and regulation. Nat Commun. 9, 411
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C Y Jeng, S., Trachman, R. J., Weissenboeck, F., Truong, L., Link, K. A., Jepsen, M. D. E., Knutson, J. R., Andersen, E. S., Ferré-D'Amaré, A. R., and Unrau, P. J. (2021) Fluorogenic aptamers resolve the flexibility of RNA junctions using orientation-dependent FRET. RNA. 27, 433-444
C Y Kuk, A., Mashalidis, E. H., and Lee, S. - Y. (2017) Crystal structure of the MOP flippase MurJ in an inward-facing conformation. Nat Struct Mol Biol. 24, 171-176
C Y Kuk, A., Hao, A., Guan, Z., and Lee, S. - Y. (2019) Visualizing conformation transitions of the Lipid II flippase MurJ. Nat Commun. 10, 1736
Cabarca, S., de Souza, M. Frazão, de Oliveira, A. Albert, Muniz, G. S. Vignoli, M Lamy, T., Reis, C. Vinicius D., Takarada, J., Effer, B., Souza, L. Santos, de la Torre, L. Iriarte, Couñago, R., Oliveira, C. Luis Pinto, and Balan, A. (2021) Structure of the PknF and conformational changes induced in forkhead-associated regulatory domains. Curr Res Struct Biol. 3, 165-178
Cai, Z., Chehab, N. H., and Pavletich, N. P. (2009) Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase. Mol Cell. 35, 818-29
Cai, R., Price, I. R., Ding, F., Wu, F., Chen, T., Zhang, Y., Liu, G., Jardine, P. J., Lu, C., and Ke, A. (2019) ATP/ADP modulates gp16-pRNA conformational change in the Phi29 DNA packaging motor. Nucleic Acids Res. 10.1093/nar/gkz692
Cai, Y., Deng, Y., Horenkamp, F., Reinisch, K. M., and Burd, C. G. (2014) Sac1-Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus. J Cell Biol. 206, 485-91
Cai, X. - C., Zhang, T., Kim, E. - J., Jiang, M., Wang, K., Wang, J., Chen, S., Zhang, N., Wu, H., Li, F., Seña, C. C. Dela, Zeng, H., Vivcharuk, V., Niu, X., Zheng, W., Lee, J. P., Chen, Y., Barsyte, D., Szewczyk, M., Hajian, T., Ibáñez, G., Dong, A., Dombrovski, L., Zhang, Z., Deng, H., Min, J., Arrowsmith, C. H., Mazutis, L., Shi, L., Vedadi, M., Brown, P. J., Xiang, J., Qin, L. - X., Xu, W., and Luo, M. (2019) A chemical probe of CARM1 alters epigenetic plasticity against breast cancer cell invasion. Elife. 10.7554/eLife.47110
Cai, Y., Chin, H. F., Lazarova, D., Menon, S., Fu, C., Cai, H., Sclafani, A., Rodgers, D. W., De La Cruz, E. M., Ferro-Novick, S., and Reinisch, K. M. (2008) The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes. Cell. 133, 1202-13

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