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Xiong, Y., Li, F., Babault, N., Wu, H., Dong, A., Zeng, H., Chen, X., Arrowsmith, C. H., Brown, P. J., Liu, J., Vedadi, M., and Jin, J. (2017) Structure-activity relationship studies of G9a-like protein (GLP) inhibitors. Bioorg Med Chem. 25, 4414-4423
Xiong, Y., Li, F., Babault, N., Wu, H., Dong, A., Zeng, H., Chen, X., Arrowsmith, C. H., Brown, P. J., Liu, J., Vedadi, M., and Jin, J. (2017) Structure-activity relationship studies of G9a-like protein (GLP) inhibitors. Bioorg Med Chem. 25, 4414-4423
Mann, M. K., Zepeda-Velázquez, C. A., González-Álvarez, H., Dong, A., Kiyota, T., Aman, A. M., Loppnau, P., Li, Y., Wilson, B., Arrowsmith, C. H., Al-awar, R., Harding, R. J., and Schapira, M. (2021) Structure-Activity Relationship of USP5 Inhibitors. J Med Chem. 64, 15017-15036
Mann, M. K., Zepeda-Velázquez, C. A., González-Álvarez, H., Dong, A., Kiyota, T., Aman, A. M., Loppnau, P., Li, Y., Wilson, B., Arrowsmith, C. H., Al-awar, R., Harding, R. J., and Schapira, M. (2021) Structure-Activity Relationship of USP5 Inhibitors. J Med Chem. 64, 15017-15036
Sudhamsu, J., Lee, G. In, Klessig, D. F., and Crane, B. R. (2008) The structure of YqeH. An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition. J Biol Chem. 283, 32968-76
Grasty, K. C., Guzik, C., D'Lauro, E. J., Padrick, S. B., Beld, J., and Loll, P. J. (2023) Structure of VanS from vancomycin-resistant enterococci: A sensor kinase with weak ATP binding.. J Biol Chem. 299, 103001
Callahan, S. J., Luyten, Y. A., Gupta, Y. K., Wilson, G. G., Roberts, R. J., Morgan, R. D., and Aggarwal, A. K. (2016) Structure of Type IIL Restriction-Modification Enzyme MmeI in Complex with DNA Has Implications for Engineering New Specificities. PLoS Biol. 14, e1002442
Yuan, P., Paterson, R. G., Leser, G. P., Lamb, R. A., and Jardetzky, T. S. (2012) Structure of the ulster strain newcastle disease virus hemagglutinin-neuraminidase reveals auto-inhibitory interactions associated with low virulence. PLoS Pathog. 8, e1002855
Yuan, P., Paterson, R. G., Leser, G. P., Lamb, R. A., and Jardetzky, T. S. (2012) Structure of the ulster strain newcastle disease virus hemagglutinin-neuraminidase reveals auto-inhibitory interactions associated with low virulence. PLoS Pathog. 8, e1002855
Lim, D., Gold, D. A., Julien, L., Rosowski, E. E., Niedelman, W., Yaffe, M. B., and Saeij, J. P. J. (2013) Structure of the Toxoplasma gondii ROP18 kinase domain reveals a second ligand binding pocket required for acute virulence. J Biol Chem. 288, 34968-80
Yunus, A. A., and Lima, C. D. (2009) Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA. Mol Cell. 35, 669-82
Antipenko, A., Himanen, J. - P., van Leyen, K., Nardi-Dei, V., Lesniak, J., Barton, W. A., Rajashankar, K. R., Lu, M., Hoemme, C., Püschel, A. W., and Nikolov, D. B. (2003) Structure of the semaphorin-3A receptor binding module. Neuron. 39, 589-98
Antipenko, A., Himanen, J. - P., van Leyen, K., Nardi-Dei, V., Lesniak, J., Barton, W. A., Rajashankar, K. R., Lu, M., Hoemme, C., Püschel, A. W., and Nikolov, D. B. (2003) Structure of the semaphorin-3A receptor binding module. Neuron. 39, 589-98
Leksa, N. C., Brohawn, S. G., and Schwartz, T. U. (2009) The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture. Structure. 17, 1082-91
Lou, X., Toresson, G., Benod, C., Suh, J. Ho, Philips, K. J., Webb, P., and Gustafsson, J. - Å. (2014) Structure of the retinoid X receptor α-liver X receptor β (RXRα-LXRβ) heterodimer on DNA.. Nat Struct Mol Biol. 21, 277-81
Strugatsky, D., McNulty, R., Munson, K., Chen, C. - K., S Soltis, M., Sachs, G., and Luecke, H. (2013) Structure of the proton-gated urea channel from the gastric pathogen Helicobacter pylori. Nature. 493, 255-8
Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., M Manzini, C., Shapiro, L., and Mancia, F. (2016) Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun. 7, 10175
Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., M Manzini, C., Shapiro, L., and Mancia, F. (2016) Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun. 7, 10175
Smith, N. A., Clarke, O. B., Lee, M., Hodder, A. N., and Smith, B. J. (2020) Structure of the Plasmodium falciparum PfSERA5 pseudo-zymogen. Protein Sci. 29, 2245-2258
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
Mompeán, M., Li, W., Li, J., Laage, S., Siemer, A. B., Bozkurt, G., Wu, H., and McDermott, A. E. (2018) The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex. Cell. 173, 1244-1253.e10
Mompeán, M., Li, W., Li, J., Laage, S., Siemer, A. B., Bozkurt, G., Wu, H., and McDermott, A. E. (2018) The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex. Cell. 173, 1244-1253.e10
Mompeán, M., Li, W., Li, J., Laage, S., Siemer, A. B., Bozkurt, G., Wu, H., and McDermott, A. E. (2018) The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex. Cell. 173, 1244-1253.e10
Sukumar, N., Liu, S., Li, W., Mathews, F. S., Mitra, B., and Kandavelu, P. (2018) Structure of the monotopic membrane protein (S)-mandelate dehydrogenase at 2.2Å resolution.. Biochimie. 10.1016/j.biochi.2018.07.017
Sukumar, N., Liu, S., Li, W., Mathews, F. S., Mitra, B., and Kandavelu, P. (2018) Structure of the monotopic membrane protein (S)-mandelate dehydrogenase at 2.2Å resolution.. Biochimie. 10.1016/j.biochi.2018.07.017

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