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Manz, T. D., Sivakumaren, S. C., Yasgar, A., Hall, M. D., Davis, M. I., Seo, H. - S., Card, J. D., Ficarro, S. B., Shim, H., Marto, J. A., Dhe-Paganon, S., Sasaki, A. T., Boxer, M. B., Simeonov, A., Cantley, L. C., Shen, M., Zhang, T., Ferguson, F. M., and Gray, N. S. (2020) Structure-Activity Relationship Study of Covalent Pan-phosphatidylinositol 5-Phosphate 4-Kinase Inhibitors. ACS Med Chem Lett. 11, 346-352
Marcia, M., Humphris-Narayanan, E., Keating, K. S., Somarowthu, S., Rajashankar, K., and Pyle, A. Marie (2013) Solving nucleic acid structures by molecular replacement: examples from group II intron studies. Acta Crystallogr D Biol Crystallogr. 69, 2174-85
Martin, S. E. S., Tan, Z. - W., Itkonen, H. M., Duveau, D. Y., Paulo, J. A., Janetzko, J., Boutz, P. L., Törk, L., Moss, F. A., Thomas, C. J., Gygi, S. P., Lazarus, M. B., and Walker, S. (2018) Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. J Am Chem Soc. 10.1021/jacs.8b07328
Martin, R., Gupta, K., Ninan, N. S., Perry, K., and Van Duyne, G. D. (2012) The survival motor neuron protein forms soluble glycine zipper oligomers. Structure. 20, 1929-39
Mason, E. O., Goldgur, Y., Robev, D., Freywald, A., Nikolov, D. B., and Himanen, J. P. (2021) Structure of the EphB6 receptor ectodomain. PLoS One. 16, e0247335
Matthews, M. M., Thomas, J. M., Zheng, Y., Tran, K., Phelps, K. J., Scott, A. I., Havel, J., Fisher, A. J., and Beal, P. A. (2016) Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity. Nat Struct Mol Biol. 23, 426-33
McCarthy, K. R., Timpona, J. L., Jenni, S., Bloyet, L. - M., Brusic, V., Johnson, W. E., Whelan, S. P. J., and Robinson-McCarthy, L. R. (2020) Structure of the Receptor Binding Domain of EnvP(b)1, an Endogenous Retroviral Envelope Protein Expressed in Human Tissues. mBio. 10.1128/mBio.02772-20
McCoy, J. G., Ren, Z., Stanevich, V., Lee, J., Mitra, S., Levin, E. J., Poget, S., Quick, M., Im, W., and Zhou, M. (2016) The Structure of a Sugar Transporter of the Glucose EIIC Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport. Structure. 24, 956-64
McCulloch, K. M., Kinsland, C., Begley, T. P., and Ealick, S. E. (2008) Structural studies of thiamin monophosphate kinase in complex with substrates and products. Biochemistry. 47, 3810-21
McCulloch, K. M., Mukherjee, T., Begley, T. P., and Ealick, S. E. (2010) Structure determination and characterization of the vitamin B6 degradative enzyme (E)-2-(acetamidomethylene)succinate hydrolase. Biochemistry. 49, 1226-35
McCulloch, K. M., Mukherjee, T., Begley, T. P., and Ealick, S. E. (2009) Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications. Biochemistry. 48, 4139-49
McFarland, A. P., Luo, S., Ahmed-Qadri, F., Zuck, M., Thayer, E. F., Goo, Y. Ah, Hybiske, K., Tong, L., and Woodward, J. J. (2017) Sensing of Bacterial Cyclic Dinucleotides by the Oxidoreductase RECON Promotes NF-κB Activation and Shapes a Proinflammatory Antibacterial State.. Immunity. 46, 433-445
McMillan, B. J., Tibbe, C., Drabek, A. A., Seegar, T. C. M., Blacklow, S. C., and Klein, T. (2017) Structural Basis for Regulation of ESCRT-III Complexes by Lgd. Cell Rep. 19, 1750-1757
McMillan, B. J., Zimmerman, B., Egan, E. D., Lofgren, M., Xu, X., Hesser, A., and Blacklow, S. C. (2017) Structure of human POFUT1, its requirement in ligand-independent oncogenic Notch signaling, and functional effects of Dowling-Degos mutations. Glycobiology. 10.1093/glycob/cwx020
McNamara, D. E., Cascio, D., Jorda, J., Bustos, C., Wang, T. - C., Rasche, M. E., Yeates, T. O., and Bobik, T. A. (2014) Structure of dihydromethanopterin reductase, a cubic protein cage for redox transfer. J Biol Chem. 289, 8852-64
McNamara, D. E., Senese, S., Yeates, T. O., and Torres, J. Z. (2015) Structures of potent anticancer compounds bound to tubulin. Protein Sci. 24, 1164-72
Meador, K., Castells-Graells, R., Aguirre, R., Sawaya, M. R., Arbing, M. A., Sherman, T., Senarathne, C., and Yeates, T. O. (2024) A suite of designed protein cages using machine learning and protein fragment-based protocols. Structure. 10.1016/j.str.2024.02.017
Meeks, K. R., Bogner, A. N., and Tanner, J. J. (2024) Screening a knowledge-based library of low molecular weight compounds against the proline biosynthetic enzyme 1-pyrroline-5-carboxylate 1 (PYCR1). Protein Sci. 33, e5072
Mehboob, S., Mulhearn, D. C., Truong, K., Johnson, M. E., and Santarsiero, B. D. (2010) Structure of dihydroorotase from Bacillus anthracis at 2.6 Å resolution.. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 1432-5
Meisner, J., Maehigashi, T., André, I., Dunham, C. M., and Moran, C. P. (2012) Structure of the basal components of a bacterial transporter. Proc Natl Acad Sci U S A. 109, 5446-51
Melillo, B., Liang, S., Park, J., Schön, A., Courter, J. R., Lalonde, J. M., Wendler, D. J., Princiotto, A. M., Seaman, M. S., Freire, E., Sodroski, J., Madani, N., Hendrickson, W. A., and Smith, A. B. (2016) Small-Molecule CD4-Mimics: Structure-Based Optimization of HIV-1 Entry Inhibition. ACS Med Chem Lett. 7, 330-4
Melly, G. C., Stokas, H., Dunaj, J. L., Hsu, F. - F., Rajavel, M., Su, C. - C., Yu, E. W., and Purdy, G. E. (2019) Structural and functional evidence that lipoprotein LpqN supports cell envelope biogenesis in . J Biol Chem. 10.1074/jbc.RA119.008781
Merz, G. E., Borbat, P. P., Muok, A. R., Srivastava, M., Bunck, D. N., Freed, J. H., and Crane, B. R. (2018) Site-Specific Incorporation of a Cu Spin-Label Into Proteins for Measuring Distances by Pulsed Dipolar ESR Spectroscopy. J Phys Chem B. 10.1021/acs.jpcb.8b05619
Mi, L. - Z., Brown, C. T., Gao, Y., Tian, Y., Le, V. Q., Walz, T., and Springer, T. A. (2015) Structure of bone morphogenetic protein 9 procomplex. Proc Natl Acad Sci U S A. 112, 3710-5
Miallau, L., Faller, M., Chiang, J., Arbing, M., Guo, F., Cascio, D., and Eisenberg, D. (2009) Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J Biol Chem. 284, 276-83

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