Publications

Found 1413 results
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2019
Korasick, D. A., Končitíková, R., Kopečná, M., Hájková, E., Vigouroux, A., Moréra, S., Becker, D. F., Šebela, M., Tanner, J. J., and Kopečný, D. (2019) Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants. J Mol Biol. 431, 576-592
Korasick, D. A., Končitíková, R., Kopečná, M., Hájková, E., Vigouroux, A., Moréra, S., Becker, D. F., Šebela, M., Tanner, J. J., and Kopečný, D. (2019) Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants. J Mol Biol. 431, 576-592
Korasick, D. A., Končitíková, R., Kopečná, M., Hájková, E., Vigouroux, A., Moréra, S., Becker, D. F., Šebela, M., Tanner, J. J., and Kopečný, D. (2019) Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants. J Mol Biol. 431, 576-592
Korasick, D. A., Končitíková, R., Kopečná, M., Hájková, E., Vigouroux, A., Moréra, S., Becker, D. F., Šebela, M., Tanner, J. J., and Kopečný, D. (2019) Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants. J Mol Biol. 431, 576-592
Garg, P., Ceccarelli, D. F., Keszei, A. Fa, Kourinov, I., Sicheri, F., and Sidhu, S. S. (2019) Structural and Functional Analysis of Ubiquitin-based inhibitors that Target the Backsides of E2 Enzymes. J Mol Biol. 10.1016/j.jmb.2019.09.024
Garg, P., Ceccarelli, D. F., Keszei, A. Fa, Kourinov, I., Sicheri, F., and Sidhu, S. S. (2019) Structural and Functional Analysis of Ubiquitin-based inhibitors that Target the Backsides of E2 Enzymes. J Mol Biol. 10.1016/j.jmb.2019.09.024
Teyra, J., Singer, A. U., Schmitges, F. W., Jaynes, P., Lui, S. Kit Leng, Polyak, M. J., Fodil, N., Krieger, J. R., Tong, J., Schwerdtfeger, C., Brasher, B. B., Ceccarelli, D. F. J., Moffat, J., Sicheri, F., Moran, M. F., Gros, P., Eichhorn, P. J. A., Lenter, M., Boehmelt, G., and Sidhu, S. S. (2019) Structural and Functional Characterization of Ubiquitin Variant Inhibitors of USP15. Structure. 27, 590-605.e5
de Araujo, E. D., Erdogan, F., Neubauer, H. A., Meneksedag-Erol, D., Manaswiyoungkul, P., Eram, M. S., Seo, H. - S., Qadree, A. K., Israelian, J., Orlova, A., Suske, T., Pham, H. T. T., Boersma, A., Tangermann, S., Kenner, L., Rülicke, T., Dong, A., Ravichandran, M., Brown, P. J., Audette, G. F., Rauscher, S., Dhe-Paganon, S., Moriggl, R., and Gunning, P. T. (2019) Structural and functional consequences of the STAT5B driver mutation. Nat Commun. 10, 2517
Grudzien-Nogalska, E., Wu, Y., Jiao, X., Cui, H., Mateyak, M. K., Hart, R. P., Tong, L., and Kiledjian, M. (2019) Structural and mechanistic basis of mammalian Nudt12 RNA deNADding. Nat Chem Biol. 15, 575-582
Kudalkar, S. N., Ullah, I., Bertoletti, N., Mandl, H. K., Cisneros, J. A., Beloor, J., Chan, A. H., Quijano, E., W Saltzman, M., Jorgensen, W. L., Kumar, P., and Anderson, K. S. (2019) Structural and pharmacological evaluation of a novel non-nucleoside reverse transcriptase inhibitor as a promising long acting nanoformulation for treating HIV. Antiviral Res. 167, 110-116
Kudalkar, S. N., Ullah, I., Bertoletti, N., Mandl, H. K., Cisneros, J. A., Beloor, J., Chan, A. H., Quijano, E., W Saltzman, M., Jorgensen, W. L., Kumar, P., and Anderson, K. S. (2019) Structural and pharmacological evaluation of a novel non-nucleoside reverse transcriptase inhibitor as a promising long acting nanoformulation for treating HIV. Antiviral Res. 167, 110-116
Zuo, H., Glaaser, I., Zhao, Y., Kurinov, I., Mosyak, L., Wang, H., Liu, J., Park, J., Frangaj, A., Sturchler, E., Zhou, M., McDonald, P., Geng, Y., Slesinger, P. A., and Fan, Q. R. (2019) Structural basis for auxiliary subunit KCTD16 regulation of the GABA receptor. Proc Natl Acad Sci U S A. 116, 8370-8379
Battaglia, R. A., Grigg, J. C., and Ke, A. (2019) Structural basis for tRNA decoding and aminoacylation sensing by T-box riboregulators. Nat Struct Mol Biol. 26, 1106-1113
Roose, B. W., Zemerov, S. D., Wang, Y., Kasimova, M. A., Carnevale, V., and Dmochowski, I. J. (2019) A Structural Basis for Xe Hyper-CEST Signal in TEM-1 β-Lactamase.. Chemphyschem. 20, 260-267
Hashimoto, H., Kafková, L., Raczkowski, A., Jordan, K. D., Read, L. K., and Debler, E. W. (2019) Structural Basis of Protein Arginine Methyltransferase Activation by a Catalytically Dead Homolog (Prozyme). J Mol Biol. 10.1016/j.jmb.2019.11.002
Owens, T. W., Taylor, R. J., Pahil, K. S., Bertani, B. R., Ruiz, N., Kruse, A. C., and Kahne, D. (2019) Structural basis of unidirectional export of lipopolysaccharide to the cell surface. Nature. 567, 550-553
Owens, T. W., Taylor, R. J., Pahil, K. S., Bertani, B. R., Ruiz, N., Kruse, A. C., and Kahne, D. (2019) Structural basis of unidirectional export of lipopolysaccharide to the cell surface. Nature. 567, 550-553
Clayton, G. M., White, J., Lee, S., Kappler, J. W., and Chan, S. K. (2019) Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6. PLoS One. 14, e0213052
De Ioannes, P., Leon, V. A., Kuang, Z., Wang, M., Boeke, J. D., Hochwagen, A., and Armache, K. - J. (2019) Structure and function of the Orc1 BAH-nucleosome complex. Nat Commun. 10, 2894
Trachman, R. J., Autour, A., C Y Jeng, S., Abdolahzadeh, A., Andreoni, A., Cojocaru, R., Garipov, R., Dolgosheina, E. V., Knutson, J. R., Ryckelynck, M., Unrau, P. J., and Ferré-D'Amaré, A. R. (2019) Structure and functional reselection of the Mango-III fluorogenic RNA aptamer. Nat Chem Biol. 15, 472-479
Kattke, M. D., Gosschalk, J. E., Martinez, O. E., Kumar, G., Gale, R. T., Cascio, D., Sawaya, M. R., Philips, M., Brown, E. D., and Clubb, R. T. (2019) Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria. PLoS Pathog. 15, e1007723
Kattke, M. D., Gosschalk, J. E., Martinez, O. E., Kumar, G., Gale, R. T., Cascio, D., Sawaya, M. R., Philips, M., Brown, E. D., and Clubb, R. T. (2019) Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria. PLoS Pathog. 15, e1007723
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18

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