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9. Canvass: A Crowd-Sourced, Natural-Product Screening Library for Exploring Biological Space

Author

Kearney, SE, Zahoránszky-Köhalmi, G, Brimacombe, KR, Henderson, MJ, Lynch, C, Zhao, T, Wan, KK, Itkin, Z, Dillon, C, Shen, M, Cheff, DM, Lee, TD, Bougie, D, Cheng, K, Coussens, NP, Dorjsuren, D, Eastman, RT, Huang, R, Iannotti, MJ, Karavadhi, S, Klumpp-Thomas, C, Roth, JS, Sakamuru, S, Sun, W, Titus, SA, Yasgar, A, Zhang, YQ, Zhao, J, Andrade, RB, Brown, MK, Burns, NZ, Cha, JK, Mevers, EE, Clardy, J, Clement, JA, Crooks, PA, Cuny, GD, Ganor, J, Moreno, J, Morrill, LA, Picazo, E, Susick, RB, Garg, NK, Goess, BC, Grossman, RB, Hughes, CC, Johnston, JN, Joullie, MM, Kinghorn, AD, Kingston, DGI, Krische, MJ, Kwon, O, Maimone, TJ, Majumdar, S, Maloney, KN, Mohamed, E, Murphy, BT, Nagorny, P, Olson, DE, Overman, LE, Brown, LE, Snyder, JK, Porco, JA, Rivas, F, Ross, SA, Sarpong, R, Sharma, I, Shaw, JT, Xu, Z, Shen, B, Shi, W, Stephenson, CRJ, Verano, AL, Tan, DS, Tang, Y, Taylor, RE, Thomson, RJ, Vosburg, DA, Wu, J, Wuest, WM, Zakarian, A, Zhang, Y, Ren, T, Zuo, Z, Inglese, J, Michael, S, Simeonov, A, Zheng, W, Shinn, P, Jadhav, A, Boxer, MB, Hall, MD, Xia, M, and Guha, R

Abstract

Copyright © 2018 American Chemical Society. Natural products and their derivatives continue to be wellsprings of nascent therapeutic potential. However, many laboratories have limited resources for biological evaluation, leaving their previously isolated or synthesized compounds largely or completely untested. To address this issue, the Canvass library of natural products was assembled, in collaboration with academic and industry researchers, for quantitative high-throughput screening (qHTS) across a diverse set of cell-based and biochemical assays. Characterization of the library in terms of physicochemical properties, structural diversity, and similarity to compounds in publicly available libraries indicates that the Canvass library contains many structural elements in common with approved drugs. The assay data generated were analyzed using a variety of quality control metrics, and the resultant assay profiles were explored using statistical methods, such as clustering and compound promiscuity analyses. Individual compounds were then sorted by structural class and activity profiles. Differential behavior based on these classifications, as well as noteworthy activities, are outlined herein. One such highlight is the activity of (-)-2(S)-cathafoline, which was found to stabilize calcium levels in the endoplasmic reticulum. The workflow described here illustrates a pilot effort to broadly survey the biological potential of natural products by utilizing the power of automation and high-throughput screening. ©

Published
2018

12. Salvadiones-A and -B: two terpenoids having novel carbon skeleta from Salvia bucharica

Author

Ahmad, Vigar Uddin, Zahid, M., Ali, M. Shaiq, Jassbi, A.R., Abbas, M., Clardy, J., Lobkovsky, E., Tareen, R.B., Iqbal, M. Zafar, and Ali, Z.

Subjects
Chemistry, Organic -- Research, Carbon -- Research, Biological sciences, Chemistry
Abstract

Research concerning isolation of two carbon skeleta terpenoids from hexane soluble fraction of Salvia bucharica is presented. Single-crystal X-ray diffraction analysis has been used to determine their structure.

Published
1999

15. Synthetic libraries of tyrosine-derived bacterial metabolites

Author

Georgiades, Savvas N., Clardy, J., and Georgiades, Savvas N. [0000-0002-6106-9904]

Subjects
Enamides, synthesis, Metabolite, Clinical Biochemistry, Libraries, Pharmaceutical Science, medicine.disease_cause, Biochemistry, chemistry.chemical_compound, Solid-phase synthesis, Antibiotics, Drug Discovery, Tyrosine, Bacteria (microorganisms), Microwave-assisted reactions, Molecular Structure, Chemistry, article, Esters, Enol, Small molecule, structure analysis, reaction analysis, solid, Acyl Meldrum's acids, Molecular Medicine, chemical reaction, Stereochemistry, metabolite, Environmental DNA, Alkenes, Enol esters, Article, Small Molecule Libraries, Escherichia coli, medicine, Molecular Biology, Bacterial metabolites, N-Acyl amino acids, nonhuman, Long chain acids, Organic Chemistry, bacterial metabolism, Amides, bacterial DNA, Alcohols, chemical structure, ester, Heterologous expression
Abstract

The preparation of a collection of 131 small molecules, reminiscent of families of long chain N-acyl tyrosines, enamides and enol esters that have been isolated from heterologous expression of environmental DNA (eDNA) in Escherichia coli, is reported. The synthetic libraries of N-acyl tyrosines and their 3-keto counterparts were prepared via solid-phase routes, whereas the enamides and enol esters were synthesized in solution-phase. © 2007 Elsevier Ltd. All rights reserved. 18 10 3117 3121

Published
2008

16. Minimum Information about a Biosynthetic Gene cluster

Author

Medema, M., Kottmann, R., Yilmaz, P., Cummings, M., Biggins, J., Blin, K., de Bruijn, I., Chooi, Y., Claesen, J., Coates, R., Cruz-Morales, P., Duddela, S., Düsterhus, S., Edwards, D., Fewer, D., Garg, N., Geiger, C., Gomez-Escribano, J., Greule, A., Hadjithomas, M., Haines, A., Helfrich, E., Hillwig, M., Ishida, K., Jones, A., Jones, C., Jungmann, K., Kegler, C., Uk Kim, H., Kötter, P., Krug, D., Masschelein, J., Melnik, A., Mantovani, S., Monroe, E., Moore, M., Moss, N., Nützmann, H., Pan, G., Pati, A., Petras, D., Reen, F., Rui, Z., Tian, Z., Tsunematsu, Y., Tobias, N., Wiemann, P., Wyckoff, E., Yan, X., Yim, G., Yu, F., Xie, Y., Aigle, B., Apel, A., Balibar, C., Balskus, E., Barona-Gómez, F., Bechthold, A., Bode, H., Borriss, R., Brady, S., Brakhage, A., Caffrey, P., Cheng, Y., Clardy, J., Cox, R., De Mot, R., Donadio, S., van der Donk, W., Dorrestein, P., Doyle, S., Driessen, A., Ehling-Schulz, M., Entian, K., Fischbach, M., Gerwick, L., Gerwick, W., Gross, H., Gust, B., Hertweck, C., Höfte, M., Jensen, S., Ju, J., Katz, L., Kaysser, L., Klassen, J., Keller, N., Kormanec, J., Kuipers, O., Kuzuyama, T., Kyrpides, N., Kwon, H., Lautru, S., Lavigne, R., Lee, C., Linquan, B., Liu, X., Liu, W., Luzhetskyy, A., Mahmud, T., Mast, Y., Méndez, C., Metsä-Ketelä, M., Micklefield, J., Mitchell, D., Moore, B., Moreira, L., Müller, R., Neilan, B., Nett, M., Nielsen, J., O’Gara, F., Oikawa, H., Osbourn, A., Osburne, M., Ostash, B., Payne, S., Pernode, J., Petricek, M., Piel, J., Ploux, O., Raaijmakers, J., Salas, J., Schmitt, E., Scott, B., Seipke, R., Shen, B., Sherman, D., Sivonen, K., Smanski, M., Sosio, M., Stegmann, E., Süssmuth, R., Tahlan, K., Thomas, C., Tang, Y., Truman, A., Viaud, M., Walton, J., Walsh, C., Weber, T., van Wezel, G., Wilkinson, B., Willey, J., Wohlleben, W., Wright, G., Ziemert, N., Zhang, C., Zotchev, S., Breitling, R., Takano, E., and Glöckner, F.

Abstract

A wide variety of enzymatic pathways that produce specialized metabolites in bacteria, fungi and plants are known to be encoded in biosynthetic gene clusters. Information about these clusters, pathways and metabolites is currently dispersed throughout the literature, making it difficult to exploit. To facilitate consistent and systematic deposition and retrieval of data on biosynthetic gene clusters, we propose the Minimum Information about a Biosynthetic Gene cluster (MIBiG) data standard.

Published
2015

19. The cytoplasmic prolyl-tRNA synthetase of the malaria parasite is a dual-stage target of febrifugine and its analogs

Author

Harvard University--MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology. Department of Biology, Herman, Jonathan D, Lindquist, Susan, Pepper, L. R., Cortese, J. F., Estiu, G., Galinsky, K., Zuzarte-Luis, V., Derbyshire, E. R., Ribacke, U., Lukens, A. K., Santos, S. A., Patel, V., Clish, C. B., Sullivan, W. J., Zhou, H., Bopp, S. E., Schimmel, P., Clardy, J., Mota, M. M., Keller, T. L., Whitman, M., Wiest, O., Wirth, D. F., Mazitschek, R., Herman, Jonathan D., Harvard University--MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology. Department of Biology, Herman, Jonathan D, Lindquist, Susan, Pepper, L. R., Cortese, J. F., Estiu, G., Galinsky, K., Zuzarte-Luis, V., Derbyshire, E. R., Ribacke, U., Lukens, A. K., Santos, S. A., Patel, V., Clish, C. B., Sullivan, W. J., Zhou, H., Bopp, S. E., Schimmel, P., Clardy, J., Mota, M. M., Keller, T. L., Whitman, M., Wiest, O., Wirth, D. F., Mazitschek, R., and Herman, Jonathan D.

Abstract

The emergence of drug resistance is a major limitation of current antimalarials. The discovery of new druggable targets and pathways including those that are critical for multiple life cycle stages of the malaria parasite is a major goal for developing next-generation antimalarial drugs. Using an integrated chemogenomics approach that combined drug resistance selection, whole-genome sequencing, and an orthogonal yeast model, we demonstrate that the cytoplasmic prolyl–tRNA (transfer RNA) synthetase (PfcPRS) of the malaria parasite Plasmodium falciparum is a biochemical and functional target of febrifugine and its synthetic derivative halofuginone. Febrifugine is the active principle of a traditional Chinese herbal remedy for malaria. We show that treatment with febrifugine derivatives activated the amino acid starvation response in both P. falciparum and a transgenic yeast strain expressing PfcPRS. We further demonstrate in the Plasmodium berghei mouse model of malaria that halofuginol, a new halofuginone analog that we developed, is active against both liver and asexual blood stages of the malaria parasite. Halofuginol, unlike halofuginone and febrifugine, is well tolerated at efficacious doses and represents a promising lead for the development of dual-stage next-generation antimalarials., Howard Hughes Medical Institute

Published
2016

21. Minimum Information about a Biosynthetic Gene cluster

Author

Medema, M.H., Kottmann, R., Yilmaz, P., Cummings, M., Biggins, J.B., Blin, K., de Bruijn, I., Chooi, Y.H., Claesen, J., Coates, R.C., Cruz-Morales, P., Duddela, S., Düsterhus, S., Edwards, D.J., Fewer, D.P., Garg, N., Geiger, C., Gomez-Escribano, J.P., Greule, A., Hadjithomas, M., Haines, A.S., Helfrich, E.J., Hillwig, M.L., Ishida, K., Jones, A.C., Jones, C.S., Jungmann, K., Kegler, C., Kim, H.U., Kötter, P., Krug, D., Masschelein, J., Melnik, A.V., Mantovani, S.M., Monroe, E.A., Moore, M., Moss, N., Nützmann, H.W., Pan, G., Pati, A., Petras, D., Reen, F.J., Rosconi, F., Rui, Z., Tian, Z., Tobias, N.J., Tsunematsu, Y., Wiemann, P., Wyckoff, E., Yan, X., Yim, G., Yu, F., Xie, Y., Aigle, B., Apel, A.K., Balibar, C.J., Balskus, E.P., Barona-Gómez, F., Bechthold, A., Bode, H.B., Borriss, R., Brady, S.F., Brakhage, Axel A., Caffrey, P., Cheng, Yo, Clardy, J., Cox, R.J., De Mot, R., Donadio, S., Donia, M.S., van der Donk, W.A., Dorrestein, P.C., Doyle, Sean, Driessen, A.J., Ehling-Schulz, M., Entian, K.D., Fischbach, M.A., Gerwick, L., Gerwick, W.H., Gross, H., Gust, B., Hertweck, C., Höfte, M., Jensen, S.E., Ju, J., Katz, L., Kaysser, L., Klassen, J.L., Keller, N.P., Kormanec, J., Kuipers, O.P., Kuzuyama, T., Kyrpides, N.C., Kwon, H.J., Lautru, S., Lavigne, R., Lee, C.Y., Linquan, B., Liu, X., Liu, W., Luzhetskyy, A., Mahmud, T., Mast, Y., Méndez, C., Metsä-Ketelä, M., Micklefield, J., Mitchell, D.A., Moore, B.S., Moreira, L.M., Muller, R., Neilan, B.A., Nett, M., Nielsen, J., O'Gara, F., Oikawa, H., Osbourn, A., Osburne, M.S., Ostash, B., Payne, S.M., Pernodet, J.L., Petricek, M., Piel, J., Ploux, O., Raaijmakers, J.M., Salas, J.A., Schmitt, E.K., Scott, B., Seipke, R.F., Shen, B., Sherman, D.H., Sivonen, K., Smanski, M.J., Sosio, M., Stegmann, E., Süssmuth, R.D., Tahlan, K., Thomas, C.M., Tang, Y., Truman, A.W., Viaud, M., Walton, J.D., Walsh, C.T., Weber, T., van Wezel, G.P., Wilkinson, B., Willey, J.M., Wohlleben, W., Wright, G.D., Ziemert, N., Zhang, C., Zotchev, S.B., Breitling, R., Takano, E., Glöckner, F.O., Medema, M.H., Kottmann, R., Yilmaz, P., Cummings, M., Biggins, J.B., Blin, K., de Bruijn, I., Chooi, Y.H., Claesen, J., Coates, R.C., Cruz-Morales, P., Duddela, S., Düsterhus, S., Edwards, D.J., Fewer, D.P., Garg, N., Geiger, C., Gomez-Escribano, J.P., Greule, A., Hadjithomas, M., Haines, A.S., Helfrich, E.J., Hillwig, M.L., Ishida, K., Jones, A.C., Jones, C.S., Jungmann, K., Kegler, C., Kim, H.U., Kötter, P., Krug, D., Masschelein, J., Melnik, A.V., Mantovani, S.M., Monroe, E.A., Moore, M., Moss, N., Nützmann, H.W., Pan, G., Pati, A., Petras, D., Reen, F.J., Rosconi, F., Rui, Z., Tian, Z., Tobias, N.J., Tsunematsu, Y., Wiemann, P., Wyckoff, E., Yan, X., Yim, G., Yu, F., Xie, Y., Aigle, B., Apel, A.K., Balibar, C.J., Balskus, E.P., Barona-Gómez, F., Bechthold, A., Bode, H.B., Borriss, R., Brady, S.F., Brakhage, Axel A., Caffrey, P., Cheng, Yo, Clardy, J., Cox, R.J., De Mot, R., Donadio, S., Donia, M.S., van der Donk, W.A., Dorrestein, P.C., Doyle, Sean, Driessen, A.J., Ehling-Schulz, M., Entian, K.D., Fischbach, M.A., Gerwick, L., Gerwick, W.H., Gross, H., Gust, B., Hertweck, C., Höfte, M., Jensen, S.E., Ju, J., Katz, L., Kaysser, L., Klassen, J.L., Keller, N.P., Kormanec, J., Kuipers, O.P., Kuzuyama, T., Kyrpides, N.C., Kwon, H.J., Lautru, S., Lavigne, R., Lee, C.Y., Linquan, B., Liu, X., Liu, W., Luzhetskyy, A., Mahmud, T., Mast, Y., Méndez, C., Metsä-Ketelä, M., Micklefield, J., Mitchell, D.A., Moore, B.S., Moreira, L.M., Muller, R., Neilan, B.A., Nett, M., Nielsen, J., O'Gara, F., Oikawa, H., Osbourn, A., Osburne, M.S., Ostash, B., Payne, S.M., Pernodet, J.L., Petricek, M., Piel, J., Ploux, O., Raaijmakers, J.M., Salas, J.A., Schmitt, E.K., Scott, B., Seipke, R.F., Shen, B., Sherman, D.H., Sivonen, K., Smanski, M.J., Sosio, M., Stegmann, E., Süssmuth, R.D., Tahlan, K., Thomas, C.M., Tang, Y., Truman, A.W., Viaud, M., Walton, J.D., Walsh, C.T., Weber, T., van Wezel, G.P., Wilkinson, B., Willey, J.M., Wohlleben, W., Wright, G.D., Ziemert, N., Zhang, C., Zotchev, S.B., Breitling, R., Takano, E., and Glöckner, F.O.

Abstract

A wide variety of enzymatic pathways that produce specialized metabolites in bacteria, fungi and plants are known to be encoded in biosynthetic gene clusters. Information about these clusters, pathways and metabolites is currently dispersed throughout the literature, making it difficult to exploit. To facilitate consistent and systematic deposition and retrieval of data on biosynthetic gene clusters, we propose the Minimum Information about a Biosynthetic Gene cluster (MIBiG) data standard.

Published
2015

23. New insight into the catalytic mechanism of chorismate mutases from structural studies

Author

Jon D. Stewart, Angela Y. Lee, Clardy J, and Bruce Ganem

Subjects
Stereochemistry, Clinical Biochemistry, Biochemistry, Catalysis, chemistry.chemical_compound, Biosynthesis, Drug Discovery, Chorismic acid, Aromatic amino acids, Animals, Humans, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, Pharmacology, chemistry.chemical_classification, biology, Chemistry, General Medicine, Enzyme, Committed step, biology.protein, Chorismate mutase, Molecular Medicine, Chorismate Mutase, Prephenic acid
Abstract

Chorismate mutase catalyzes the rearrangement of chorismic acid to prephenic acid, which is the first committed step in the biosynthesis of aromatic amino acids. Its catalytic mechanism has been much studied, but is poorly understood. Recent structural information on enzymes from two species, and on an antibody that catalyzes the same reaction, has shed new light on this topic.

Published
1995

28. FOXO3a is broadly neuroprotective in vitro and in vivo against insults implicated in motor neuron diseases

Author

Mojsilovic-Petrovic, J., Nedelsky, N., Boccitto, M., Mano, I., Georgiades, Savvas N., Zhou, W., Liu, Y., Neve, R. L., Taylor, J. P., Driscoll, M., Clardy, J., Merry, D., Kalb, R. G., and Georgiades, Savvas N. [0000-0002-6106-9904]

Subjects
Cell Culture Techniques, nerve degeneration, Cell Count, Rats, Sprague-Dawley, Mice, androgen receptor, Excitatory Amino Acid Agonists, rat, Motor Neurons, Kainic Acid, Cell Death, General Neuroscience, Neurodegeneration, Forkhead Box Protein O3, article, transcription factor DAF 16, Forkhead Transcription Factors, Immunohistochemistry, medicine.anatomical_structure, Neuroprotective Agents, priority journal, Spinal Cord, motor neuron disease, transcription factor FKHRL1, Female, Drosophila, neuroprotection, Signal transduction, Neuron death, excitotoxicity, signal transduction, Signal Transduction, Programmed cell death, in vitro study, animal experiment, Blotting, Western, embryo, Biology, Neuroprotection, Article, Fluorescence, animal tissue, in vivo study, male, In vivo, medicine, Animals, controlled study, Motor Neuron Disease, protein expression, mouse, nonhuman, nerve cell necrosis, animal model, Computational Biology, Motor neuron, medicine.disease, Embryo, Mammalian, nuclear localization signal, Rats, Androgen receptor, Mice, Inbred C57BL, Disease Models, Animal, Tyrosine, Neuroscience
Abstract

Aging is a risk factor for the development of adult-onset neurodegenerative diseases. Although some of the molecular pathways regulating longevity and stress resistance in lower organisms are defined (i.e., those activating the transcriptional regulators DAF-16 and HSF-1 in Caenorhabditis elegans), their relevance to mammals and disease susceptibility are unknown. We studied the signaling controlled by the mammalian homolog of DAF-16, FOXO3a, in model systems of motor neuron disease. Neuron death elicited in vitro by excitotoxic insult or the expression of mutant SOD1, mutant p150glued, or polyQ-expanded androgen receptor was abrogated by expression of nuclear-targeted FOXO3a. We identify a compound [Psammaplysene A (PA)] that increases nuclear localization of FOXO3a in vitro and in vivo and show that PA also protects against these insults in vitro. Administration of PA to invertebrate model systems of neurodegeneration similarly blocked neuron death in a DAF-16/FOXO3a-dependent manner. These results indicate that activation of the DAF-16/FOXO3a pathway, genetically or pharmacologically, confers protection against the known causes of motor neuron diseases. Copyright © 2009 Society for Neuroscience. 29 25 8236 8247 Cited By :52

Published
2009

29. LIST OF CONTRIBUTORS

Author

Alazard, J.P., primary, Amin, S.G., additional, Andrus, A., additional, ApSimon, J.W., additional, Armstrong, V.W., additional, Au-Yeung, B.-W., additional, Avram, M., additional, Ayer, W.A., additional, Babin, D., additional, Backinowsky, L.V., additional, Baldwin, J.E., additional, Bally, I., additional, Balsetan, A.T., additional, Bamezai, S., additional, Bandara, B.M.R., additional, Barth, G., additional, Barton, D.H.R., additional, Beaujean, M., additional, Beeley, N.R.A., additional, Berke, C.M., additional, Besselièvre, R., additional, Betaneli, V.I., additional, Beugelmans, R., additional, Birch, A.J., additional, Bose, A.K., additional, Brambilla, R., additional, Braun-Keller, E., additional, Brown, E., additional, Brownbridge, P., additional, Caspi, E., additional, Chamberlain, K., additional, Chan, T.H., additional, Chauncy, B., additional, Chottard, J.C., additional, Clardy, J., additional, Clark, B.C., additional, Collins, J.B., additional, Coulton, S., additional, Crouse, G.D., additional, Dadoun, H., additional, Dahler, P., additional, Day, A.I., additional, De Ville, G., additional, Dinulescu, I.G., additional, Djerassi, C., additional, von E. Doering, W., additional, Drâghici, C., additional, Elian, M., additional, Factor, R.E., additional, Faulkner, D.J., additional, Fernandez, I.F., additional, Finer-Moore, J., additional, Fleming, I., additional, Florent, J.-C., additional, Fourneron, J.-D., additional, Friary, R., additional, Fuhrer, H., additional, Fukuyama, T., additional, Funke, P.T., additional, Furmanova, N.G., additional, Fürst, A., additional, Furuhata, K., additional, Gala, K., additional, Ganguly, A., additional, Georgescu, E.G., additional, Gheorghiu, M.D., additional, Girard, P., additional, Gneuss, K.D., additional, Greaves, A.M., additional, Grier, D., additional, Gruska, R., additional, Guilhem, J., additional, Hangauer, D.G., additional, Hendrickson, J.B., additional, Hillenbrand, G.F., additional, Holohan, J.J., additional, Huber, C.P., additional, Huffman, J.W., additional, Husson, H.-P., additional, Iacobucci, G.A., additional, Ireland, C., additional, Irwin, A.J., additional, Janousek, Z., additional, Jenkins, I.D., additional, Johnson, M.A., additional, Jones, B.B., additional, Julia, M., additional, Kagan, H.B., additional, Kägi, D., additional, Kalvoda, J., additional, Kapur, J.C., additional, Katritzky, A.R., additional, Kaufmann, H., additional, Kelly, L.P., additional, Khajavi, M.S., additional, Khor, T.-C., additional, Kishi, Y., additional, Kitchin, J.P., additional, Kochetkov, N.K., additional, Kreder, J., additional, Kretschmer, G., additional, Kriemler, H.-P., additional, Ksander, G.M., additional, Kuwano, H., additional, Lansbury, P.T., additional, Lester, D.J., additional, Lewis, M., additional, Ley, S.V., additional, Liepa, A.J., additional, Lindley, M., additional, Lusinchi, X., additional, Mahanty, M.K., additional, Mallion, K.B., additional, Manhas, M.S., additional, Mansuy, D., additional, Mastrocola, A.R., additional, McMurry, J.E., additional, McPhail, A.T., additional, Meerholz, C.A., additional, Merenyi, R., additional, Metlushenko, V.P., additional, Mignani, S., additional, Minkin, V.I., additional, Mohr, P., additional, Monneret, C., additional, Motherwell, W.B., additional, Mukkavilli, L., additional, Müller, G., additional, Müller, M., additional, Mulliez, E., additional, Musser, J.H., additional, Naegeli, P., additional, Nakatsuka, S.-I., additional, Namy, J.L., additional, Narula, A.S., additional, Ogura, H., additional, Olekhnovich, L.P., additional, Onan, K.D., additional, Ovchinnikov, M.V., additional, Papoula, M.T.B., additional, Paquette, L.A., additional, Parker, W.L., additional, Pârvulescu, L., additional, Patel, R.C., additional, Peel, R., additional, Pickett, J.E., additional, Piper, J.U., additional, Puar, M.S., additional, Ragault, M., additional, Ram, B., additional, Ramachandran, P.V., additional, Ramage, R., additional, Ranganathan, D., additional, Ranganathan, S., additional, Rathnum, M.L., additional, Raverty, W.D., additional, Reed, N.V., additional, Rizzardo, E., additional, Roussi, G., additional, Saeedi-Ghomi, M.H., additional, Saito, I., additional, Scheuer, P.J., additional, Schriver, G.W., additional, Schwartz, R.E., additional, Scott, A.I., additional, Sell, C., additional, Sependa, G.J., additional, Shapiro, S., additional, Sing, L.Y., additional, Smith, K.M., additional, Sondheimer, F., additional, Soulié, J., additional, Stanescu, L., additional, Stephenson, G.R., additional, Stiller, K., additional, Streitwieser, A., additional, Sugiura, M., additional, Sum, F.W., additional, Sundararaman, P., additional, Sunday, B.R., additional, Sutherland, J.K., additional, Suzuki, M., additional, Tagle, B., additional, Tamm, Ch., additional, Tho, N.-D., additional, Thomas, E.J., additional, Thompson, D.J., additional, Toczko, G.A., additional, Van Engen, D., additional, van der Veen, J.M., additional, Viehe, H.G., additional, Vincent, J.E., additional, Wasserman, H.H., additional, Watson, W.H., additional, Weiler, L., additional, Wetli, M., additional, Wiley, D.C., additional, Williamson, D.H., additional, Wolff, M.S., additional, Wong, H.N.C., additional, Wright, J.J., additional, Zabel, V., additional, and Zimmerman, H.E., additional

Published
1982
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30. RESEARCH NEEDS FOR COAL GASIFICATION AND COAL LIQUEFACTION

Author

PENNER, S.S., primary, ALPERT, S.B., additional, BENDANILLO, V., additional, CLARDY, J., additional, FURLONG, L.E., additional, LEDER, F., additional, LEES, L., additional, REICHL, E., additional, ROSS, J., additional, SIEG, R.P., additional, SQUIRES, A.M., additional, and THOMAS, J., additional

Published
1982
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32. RESEARCH NEEDS FOR SHALE-OIL RECOVERY

Author

PENNER, S.S., primary, BERGEN, W.S., additional, CLARDY, J., additional, HOPKINS, J.M., additional, KELLEY, A.E., additional, LESSARD, R.R., additional, LEWIS, A.E., additional, OBLAD, A.G., additional, ROSS, J., additional, SIEG, R.P., additional, THOMAS, J.R., additional, WEISS, M.A., additional, and WEISZ, P.B., additional

Published
1982
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33. Total synthesis of psammaplysenes A and B, naturally occurring inhibitors of FOXO1a nuclear export

Author

Georgiades, Savvas N., Clardy, J., and Georgiades, Savvas N. [0000-0002-6106-9904]

Subjects
drug antagonism, synthesis, Stereochemistry, Active Transport, Cell Nucleus, chemistry, Biochemistry, psammaplysenes B, psammaplysene A, medicine, Molecule, active transport, Physical and Theoretical Chemistry, Nuclear export signal, Biological sciences, Molecular Structure, Extramural, Chemistry, Organic Chemistry, article, Total synthesis, Forkhead Transcription Factors, Combinatorial chemistry, Cell nucleus, medicine.anatomical_structure, drug derivative, chemical structure, Tyrosine, forkhead transcription factor, metabolism, tyrosine
Abstract

(Chemical Equation Presented) Two inhibitors of FOXO1a-mediated nuclear export, psammaplysenes A and B, have been synthesized by a flexible and efficient route. A common starting material, 4-iodophenol, was used to prepare both halves of these pseudosymmetric dibromotyrosine-derived metabolites. © 2005 American Chemical Society. 7 19 4091 4094 Cited By :21

Published
2005

41. NMR structure of lassomycin

Author

Gavrish, E., primary, Sit, C.S., additional, Kandror, O., additional, Spoering, A., additional, Peoples, A., additional, Ling, L., additional, Fetterman, A., additional, Hughes, D., additional, Cao, S., additional, Bissell, A., additional, Torrey, H., additional, Akopian, T., additional, Mueller, A., additional, Epstein, S., additional, Goldberg, A., additional, Clardy, J., additional, and Lewis, K., additional

Published
2014
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42. Crystal and solution structures of an odorant-binding protein from the southern house mosquito complexed with an oviposition pheromone

Author

Mao, Y., Xu, X., Xu, W., Ishida, Y., Leal, W.S., Ames, J.B., Clardy, J., Mao, Y., Xu, X., Xu, W., Ishida, Y., Leal, W.S., Ames, J.B., and Clardy, J.

Abstract

Culex mosquitoes introduce the pathogens responsible for filariasis, West Nile virus, St. Louis encephalitis, and other diseases into humans. Currently, traps baited with oviposition semiochemicals play an important role in detection efforts and could provide an environmentally friendly approach to controlling their populations. The odorant binding proteins (OBPs) in the female's antenna play a crucial, if yet imperfectly understood, role in sensing oviposition cues. Here, we report the X-ray crystallography and NMR 3D structures of OBP1 for Culex quinquefasciatus (CquiOBP1) bound to an oviposition pheromone (5R,6S)-6-acetoxy-5-hexadecanolide (MOP). In both studies, CquiOBP1 had the same overall six-helix structure seen in other insect OBPs, but a detailed analysis revealed an important previously undescribed feature. There are two models for OBP-mediated signal transduction: (i) direct release of the pheromone from an internal binding pocket in a pH-dependent fashion and (ii) detection of a pheromone-induced conformational change in the OBP·pheromone complex. Although CquiOBP1 binds MOP in a pH-dependent fashion, it lacks the C terminus required for the pH-dependent release model. This study shows that CquiOBP binds MOP in an unprecedented fashion using both a small central cavity for the lactone head group and a long hydrophobic channel for its tail.

Published
2010

43. The Biosynthetic genes of pantocin A and pantocin B of Pantoea agglomerans Eh318

Author

Wright, Sandra A. I., Jin, M., Clardy, J., Beer, S. V., Wright, Sandra A. I., Jin, M., Clardy, J., and Beer, S. V.

Abstract

Pantocin A and pantocin B are low-molecular weight, peptide-based antibiotics that are produced in minimal media by the biocontrol agent Pantoea agglomerans, which are inhibitory to the fire blight pathogen, Erwinia amylovora. Pantocin A and pantocin B are members of a family of antibiotics whose toxicity is inhibited by certain amino acids. They inhibit enzymes in pathways for histidine and arginine biosynthesis, respectively. The biosynthetic gene cluster for pantocin A was sequenced, and it is 2.84 kb in size. It contains a small gene (paaP) that encodes a thirty-amino acid precursor peptide and three genes, paaA, paaB and paaC that encode the enzymes necessary to process the precursor into pantocin A. PaaC is proposed to be responsible for resistance to pantocin A. The determinants for pantocin B biosynthesis are encoded in a cluster of 13 open reading frames (PabA through pabM within a 17.5 kb region. Functions are proposed for the individual gene products, based on DNA sequence homology and on the chemical structure of pantocin B. PabA is similar to multidrug resistance proteins (like YqjV of Bacmus subtilis) and is likely responsible for pantocin B resistance. However, pabB, pabC and pabD may also encode resistance determinants. The products of the pabJKLM operon are believed to be involved in the addition of the methyl sulfonyl moiety of pantocin B. Cryptic transposase genes are found within and outside of the biosynthetic region, and the G+C ratio is lower inside than outside of the cluster. Thus, the pantocin B biosynthetic region may be a genomic island whose DNA originated from other organisms and was generated through two separate transposition events.

Published
2006

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