Publications

Found 1581 results
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2018
Kono, M., Ochida, A., Oda, T., Imada, T., Banno, Y., Taya, N., Masada, S., Kawamoto, T., Yonemori, K., Nara, Y., Fukase, Y., Yukawa, T., Tokuhara, H., Skene, R., Sang, B. - C., Hoffman, I. D., Snell, G. P., Uga, K., Shibata, A., Igaki, K., Nakamura, Y., Nakagawa, H., Tsuchimori, N., Yamasaki, M., Shirai, J., and Yamamoto, S. (2018) Discovery of [cis-3-({(5 R)-5-[(7-Fluoro-1,1-dimethyl-2,3-dihydro-1H-inden-5-yl)carbamoyl]-2-methoxy-7,8-dihydro-1,6-naphthyridin-6(5H)-yl}carbonyl)cyclobutyl]acetic Acid (TAK-828F) as a Potent Selective and Orally Available Novel Retinoic Acid Receptor-R. J Med Chem. 10.1021/acs.jmedchem.8b00061
Goodman, M. C., Xu, S., Rouzer, C. A., Banerjee, S., Ghebreselasie, K., Migliore, M., Piomelli, D., and Marnett, L. J. (2018) Dual cyclooxygenase-fatty acid amide hydrolase inhibitor exploits novel binding interactions in the cyclooxygenase active site. J Biol Chem. 10.1074/jbc.M117.802058
Goodman, M. C., Xu, S., Rouzer, C. A., Banerjee, S., Ghebreselasie, K., Migliore, M., Piomelli, D., and Marnett, L. J. (2018) Dual cyclooxygenase-fatty acid amide hydrolase inhibitor exploits novel binding interactions in the cyclooxygenase active site. J Biol Chem. 10.1074/jbc.M117.802058
Assadieskandar, A., Yu, C., Maisonneuve, P., Liu, X., Chen, Y. - C., Prakash, G. K. Surya, Kurinov, I., Sicheri, F., and Zhang, C. (2018) Effects of rigidity on the selectivity of protein kinase inhibitors. Eur J Med Chem. 146, 519-528
Mukherjee, S., Griffin, D. H., Horn, J. R., Rizk, S. S., Nocula-Lugowska, M., Malmqvist, M., Kim, S. S., and Kossiakoff, A. A. (2018) Engineered synthetic antibodies as probes to quantify the energetic contributions of ligand binding to conformational changes in proteins.. J Biol Chem. 10.1074/jbc.RA117.000656
Mukherjee, S., Griffin, D. H., Horn, J. R., Rizk, S. S., Nocula-Lugowska, M., Malmqvist, M., Kim, S. S., and Kossiakoff, A. A. (2018) Engineered synthetic antibodies as probes to quantify the energetic contributions of ligand binding to conformational changes in proteins.. J Biol Chem. 10.1074/jbc.RA117.000656
Benveniste, P. M., Roy, S., Nakatsugawa, M., L Y Chen, E., Nguyen, L., Millar, D. G., Ohashi, P. S., Hirano, N., Adams, E. J., and Zúñiga-Pflücker, J. Carlos (2018) Generation and molecular recognition of melanoma-associated antigen-specific human γδ T cells.. Sci Immunol. 10.1126/sciimmunol.aav4036
Yoo, J., Mashalidis, E. H., C Y Kuk, A., Yamamoto, K., Kaeser, B., Ichikawa, S., and Lee, S. - Y. (2018) GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for inhibition of N-glycosylation. Nat Struct Mol Biol. 10.1038/s41594-018-0031-y
Mieher, J. L., Larson, M. R., Schormann, N., Purushotham, S., Wu, R., Rajashankar, K. R., Wu, H., and Deivanayagam, C. (2018) Glucan Binding Protein C of Mediates both Sucrose-Independent and Sucrose-Dependent Adherence. Infect Immun. 10.1128/IAI.00146-18
Klum, S. M., Chandradoss, S. D., Schirle, N. T., Joo, C., and MacRae, I. J. (2018) Helix-7 in Argonaute2 shapes the microRNA seed region for rapid target recognition. EMBO J. 37, 75-88
Fera, D., Lee, M. S., Wiehe, K., R Meyerhoff, R., Piai, A., Bonsignori, M., Aussedat, B., Walkowicz, W. E., Ton, T., Zhou, J. O., Danishefsky, S., Haynes, B. F., and Harrison, S. C. (2018) HIV envelope V3 region mimic embodies key features of a broadly neutralizing antibody lineage epitope. Nat Commun. 9, 1111
Cao, Q., Shin, W. Shik, Chan, H., Vuong, C. K., Dubois, B., Li, B., Murray, K. A., Sawaya, M. R., Feigon, J., Black, D. L., Eisenberg, D. S., and Jiang, L. (2018) Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design.. Nat Chem. 10.1038/s41557-018-0147-z
Zeiske, T., Baburajendran, N., Kaczynska, A., Brasch, J., Palmer, A. G., Shapiro, L., Honig, B., and Mann, R. S. (2018) Intrinsic DNA Shape Accounts for Affinity Differences between Hox-Cofactor Binding Sites. Cell Rep. 24, 2221-2230
Harris, N. C., Born, D. A., Cai, W., Huang, Y., Martin, J., Khalaf, R., Drennan, C. L., and Zhang, W. (2018) Isonitrile Formation by a Non-Heme Iron(II)-Dependent Oxidase/Decarboxylase. Angew Chem Int Ed Engl. 57, 9707-9710
Song, X., Jensen, M. Ø., Jogini, V., Stein, R. A., Lee, C. - H., Mchaourab, H. S., Shaw, D. E., and Gouaux, E. (2018) Mechanism of NMDA receptor channel block by MK-801 and memantine. Nature. 10.1038/s41586-018-0039-9
Hong, S., Sunita, S., Maehigashi, T., Hoffer, E. D., Dunkle, J. A., and Dunham, C. M. (2018) Mechanism of tRNA-mediated +1 ribosomal frameshifting. Proc Natl Acad Sci U S A. 10.1073/pnas.1809319115
Melnikov, S. V., Khabibullina, N. F., Mairhofer, E., Vargas-Rodriguez, O., Reynolds, N. M., Micura, R., Söll, D., and Polikanov, Y. S. (2018) Mechanistic insights into the slow peptide bond formation with D-amino acids in the ribosomal active site. Nucleic Acids Res. 10.1093/nar/gky1211
Melnikov, S. V., Khabibullina, N. F., Mairhofer, E., Vargas-Rodriguez, O., Reynolds, N. M., Micura, R., Söll, D., and Polikanov, Y. S. (2018) Mechanistic insights into the slow peptide bond formation with D-amino acids in the ribosomal active site. Nucleic Acids Res. 10.1093/nar/gky1211
Melnikov, S. V., Khabibullina, N. F., Mairhofer, E., Vargas-Rodriguez, O., Reynolds, N. M., Micura, R., Söll, D., and Polikanov, Y. S. (2018) Mechanistic insights into the slow peptide bond formation with D-amino acids in the ribosomal active site. Nucleic Acids Res. 10.1093/nar/gky1211
Dionne, G., Qiu, X., Rapp, M., Liang, X., Zhao, B., Peng, G., Katsamba, P. S., Ahlsen, G., Rubinstein, R., Potter, C. S., Carragher, B., Honig, B., Müller, U., and Shapiro, L. (2018) Mechanotransduction by PCDH15 Relies on a Novel cis-Dimeric Architecture. Neuron. 99, 480-492.e5
Lavoie, H., Sahmi, M., Maisonneuve, P., Marullo, S. A., Thevakumaran, N., Jin, T., Kurinov, I., Sicheri, F., and Therrien, M. (2018) MEK drives BRAF activation through allosteric control of KSR proteins. Nature. 10.1038/nature25478
Lavoie, H., Sahmi, M., Maisonneuve, P., Marullo, S. A., Thevakumaran, N., Jin, T., Kurinov, I., Sicheri, F., and Therrien, M. (2018) MEK drives BRAF activation through allosteric control of KSR proteins. Nature. 10.1038/nature25478
McCarthy, K. R., Watanabe, A., Kuraoka, M., Do, K. T., McGee, C. E., Sempowski, G. D., Kepler, T. B., Schmidt, A. G., Kelsoe, G., and Harrison, S. C. (2018) Memory B Cells that Cross-React with Group 1 and Group 2 Influenza A Viruses Are Abundant in Adult Human Repertoires. Immunity. 48, 174-184.e9
McCarthy, K. R., Watanabe, A., Kuraoka, M., Do, K. T., McGee, C. E., Sempowski, G. D., Kepler, T. B., Schmidt, A. G., Kelsoe, G., and Harrison, S. C. (2018) Memory B Cells that Cross-React with Group 1 and Group 2 Influenza A Viruses Are Abundant in Adult Human Repertoires. Immunity. 48, 174-184.e9
Dong, C., Zhang, H., Li, L., Tempel, W., Loppnau, P., and Min, J. (2018) Molecular basis of GID4-mediated recognition of degrons for the Pro/N-end rule pathway. Nat Chem Biol. 14, 466-473

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