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18. Abstracts of short lectures

Author

Rauwald, H. W., Conner, J., Gray, A., Reynolds, T., Waterman, P., Hartmann, T., Adolph, R. -D., Ehmke, A., Sander, H., Toppel, G., Witte, L., Nyiredy, Sz., Sticher, O., Erdelmeier, C. A. J., van Leeuwen, P. A. S., Kinghorn, A. D., Dallenbach-Tölke, K., Wink, M., Hennessy, Deirdre, Hook, Ingrid, Sheridan, Helen, Mersinger, R., Dornauer, H., Reinhard, E., Heide, L., Tabata, M., Knobloch, K., Jansen, H., Müller, B., Adzet, T., Vila, R., Cañigueral, S., Budzianowski, J., Bachmann, P., Czygan, F. -C., de Witte, P., Lemli, J., 't Hart, L. A., van Enckevort, P. H., Labadie, R. P., van der Heijden, R., de Keyzer, H. H. M., Verhey, E. R., Schripsema, J., Harkes, P. A. A., Verpoorte, R., Svendsen, A. Baerheim, Croom, Jr., E. M., Letchamo, W., Vömel, A., Bauer, R., Wray, V., Wagner, H., Marston, A., Hostettmann, K., Andersson, L., Bohlin, L., Iorizzi, M., Riccio, R., Minale, L., Moreno-Lopez, J., van Beek, T. A., van Bokhoven, H., Kraus, J., Blaschek, W., Franz, G., van den Berg, A. J. J., Radema, M. H., Corthout, J., Pieters, L., Claeys, M., Vanden Berghe, D., Vlietinck, A. J., Dungen, F. M. v. d., Vermeulen, N. P. E., Fischer, F. C., Gijbels, M. J. H., Caspers, P. W. J., Gijbels, M. J. M., Fung, S. Y., Herrebout, W. M., van Gelder, W. M. J., van der Graaf, G. M., Pennings, E. J. M., Huizer, H., van Zuilen, K., Kosasi, S., van der Leer, T., ten Hoope, S. M., van der Nat, J. M., van der Sluis, W. G., Bosch, R. v. d., Duine, J. A., Heijden, R. v. d., Leer, T. v. d., Pieters, L. A., Totté, J., Saleh, M. M., Abbas, R. Z., Zwaving, J. H., Sarer, E., Looman, A., Scheffer, J. J. C., Meijer, A. H., Langezaal, C. R., Simons, J. M., Hoof, L. Van, Vanden Berghe, D. A., Woerdenbag, H. J., Hendriks, H., van der Berg, K., van Stralen, R., Malingré, Th. M., Konings, A. W. T., Lemstra, W., Abdo, S., De Bernardi, M., Marinoni, G., Samaniego, S., Mellerio, G., Vidari, G., Adjibadé, Y., Kuballa, B., Cabalion, P., Anton, R., Ibáñez, C., Monasterio, I., Ayoub, S. M. Hussein, Yankov, L. K., Ovtcharov, R. O., Bartsch, C., BaŞaran, A. A., Calis, I., Nishibe, S., Berger, S., Junior, P., Kopanski, L., Beuscher, N., Billeter, M., Meier, B., Döll, M., Braunewell, H., Skrzypczak, L., Wesolowska, M., Gross, G. A., Winkler, T., Colombo, M. L., Tome, F., Crespi-Perellino, N., Guicciardi, A., Minghetti, A., Speroni, E., Vincieri, F., Vita-Finzi, P., Gabetta, B., Scilingo, A., Dorsaz, A. C., Hostettmann, M., Ebert, M., Economou, D., Nahrstedt, A., Schiebel, H. -M., McDowell, M., Eich, E., Kohaupt, G., Stopp, K., Maidhof, A., Müller, W. E. G., Schade, P., Müllen, K., Eilert, U., Wolters, B., El Tanbouly, N., Beck, J. P., Hanna, S., El Alfy, T., Ersöz, T., Chulia, A. J., Garcia, J., Frahm, A. W., Beutner, D., Gautier, P., Shongo, D., Vekemans, X., Van Koninckxloo, M., Van Haelen, M., Lefébvre, C., Gehrmann, B., Kraus, Lj., Giger, E., Baumann, T. W., Heinzer, F., Meusy, J. -P., Chavanne, M., Glombitza, K. -W., Knöss, W., Deutscher, B., Piepenbrink, G., Peter, J., Greinwald, R., Schultze, W., Gundidza, Mazuru, Hölzl, J., Hess, S., Holm, Y., Aho, E., Holopainen, M., Järvelä, K., Seppänen, T., von Schantz, M., Huhtikangas, A., Lapinjoki, S., Veräjänkorva, H., Heiskanen, J., Kauppinen, V., Lounasmaa, M., Huovinen, K., Härmälä, P., Ottoila, P., Jerga, Chr, Merfort, I., Willuhn, G., Jiménez, A., Manez, S., Villar, A., Kahlos, K., Kiviranta, J., Karppanen, H., Huovinen, H., Koch, A., Kreis, H., May, U., Kuštrak, P., Pepeljnjak, S., Antolić, A., Blažević, N., Laakso, I., Ekundayo, O., Oguntimein, B., Lorentzen, Bente, Rørdam, Anne Marie, Madaus, A., Marcinek, Chr, Martinelli, E. M., Seraglia, R., Briquez, M., Reginault, P., Máthé, Jr., I., Máthé, I., Máthé, A., Meiss, P., Meng, Qingchang, Zhu, Naijue, Chen, Weixin, Miething, H., Seger, V., Hänsel, R., Neuhöfer, H., Lurz, G., Noller, P., Oksman-Caldentey, K. -M., Vuorela, H., Isenegger, M., Strauss, A., Pachaly, P., Adnan, A. Z., Lansing, A., Sin, K. S., Pauli, A., Payá, M., Ivorra, M. D., Poginsky, B., Westendorf, J., Marquardt, H., Potterat, O., Stoeckli-Evans, H., Msonthi, J. D., Randriaminahy, M., Proksch, P., Reher, G., Samochowiec, L., Wójcicki, J., Kadlubowska, D., Kownacka, A., Şarer, E., Sayron-Atasü, E., Cihangir, V., Schmaus, G., Kubeczka, K. -H., Schütz, M., Schulz, G., Stahl-Biskup, E., Seidel, S., Sepasgosarian, J., Laitalainen, T., Światek, L., Grabias, B., Tanker, M., Kurucu, S., Tanker, N., Thron, U., Reichling, J., Martin, R., Vargas, D., Dominguez, X. A., Vollmann, C., Pernilä, H., Nystrand, N., Hinkkanen, R., Walker, J. R. L., Cole, A. L. J., Warncke, D., Kadlubowska, P., Ziegler, S. J., and Zogg, G.

Published
1987
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20. Gender stereotypes Policy Brief #2

Author

White, A., Richardson, N., Wray, V., Klinge, I., Furnee, C.A., Quevedo-Gomez, M.C., Verdonk, P., Maguire, P., and Semancik, K.

Published
2011

22. New purine derivatives from the marine sponge Petrosia nigricans

Author

Ashour, M., RuAngelie Edrada-Ebel, Ebel, R., Wray, V., Soest, R. W. M., Proksch, P., and Research of the Zoological Museum of Amsterdam (ZMA)

Subjects
parasitic diseases
Abstract

Four new purine analogues (nigricines 1 - 4) have been isolated from the Indonesian marine sponge Petrosia nigricans. The structures were elucidated by extensive 2D-NMR spectroscopic experiments and mass spectrometry.

Published
2008

24. A new bromotyrosine alkaloid from the Caribbean sponge Aiolochroia crassa

Author

Assman, M., Wray, V., van Soest, R.W.M., Proksch, P., and Evolutionary and Population Biology (IBED, FNWI)

Abstract

A detailed analysis of the chemical constituents of a Caribbean specimen of Aiolochroia crassa was performed. Five brominated products (1-5) were isolated and one of these was a new bromotyrosine metabolite. The structure of the new compound 1 has been established from spectral studies. Compounds 1 and 2, which are the major brominated metabolites and have not been previously identified in any Aiolochroia species, could be usefully employed as chemotaxonomic makers.

Published
1998

27. Is stimulation of carotenoid biosynthesis in arbuscular mycorrhizal roots a general phenomenon?

Author

Fester, Thomas, Wray, V., Nimtz, M., Strack, D., Fester, Thomas, Wray, V., Nimtz, M., and Strack, D.

Abstract

The identification and quantification of cyclohexenone glycoside derivatives from the model legume Lotus japonicus revealed far higher levels than expected according to the stoichiometric relation to another, already determined carotenoid cleavage product, i.e., mycorradicin. Mycorradicin is responsible for the yellow coloration of many arbuscular mycorrhizal (AM) roots and is usually esterified in a complex way to other compounds. After liberation from such complexes it has been detected in AM roots of many, but not of all plants examined. The non-stoichiometric occurrence of this compound compared with other carotenoid cleavage products suggested that carotenoid biosynthesis might be activated upon mycorrhization even in plant species without detectable levels of mycorradicin. This assumption has been supported by inhibition of a key enzyme of carotenoid biosynthesis (phytoene desaturase) and quantification of the accumulating enzymic substrate (phytoene). Our observations suggest that the activation of carotenoid biosynthesis in AM roots is a general phenomenon and that quantification of mycorradicin is not always a good indicator for this activation. (c) 2005 Elsevier Ltd. All rights reserved

Published
2005

28. Solution structure of the hydrophilic region of HIV-1 encoded virus protein U (Vpu) by CD and 1H NMR spectroscopy

Author

Wray V, Federau T, Henklein P, Klabunde S, Olaf Kunert, Schomburg D, and Schubert U

Subjects
Magnetic Resonance Spectroscopy, Molecular Structure, Circular Dichroism, Helix-Loop-Helix Motifs, Human Immunodeficiency Virus Proteins, Molecular Sequence Data, Water, Peptide Fragments, Protein Structure, Secondary, Solutions, Models, Chemical, Solubility, Genetic Code, Viral Regulatory and Accessory Proteins, Amino Acid Sequence
Abstract

The HIV-1 specific Vpu is a class I oligomeric membrane phosphoprotein of unknown structure and mechanism. The first experimental evidence for the position of secondary structural elements present in the hydrophilic C-terminal region of Vpu under various solution regimes is reported. CD data for nine overlapping 15 amino-acid fragments and 3 longer fragments indicate the presence of only transitory amounts of stable structure in aqueous solution alone, while with increasing trifluoroethanol content limiting structures were found indicating two helical segments in the hydrophilic region of Vpu. These limiting structures were more precisely defined from a detailed study of Vpu41-58, Vpu52-74 and Vpu63-81, by a combination of 2D 1H NMR spectroscopy, distance geometry, and restrained molecular dynamics and energy minimization calculations. Sets of low-energy conformations compatible with the quantitative NOE data indicate that Vpu41-58 has an alpha-helix from residues 42 to 50 while a second helix is found for Vpu52-74 from residues 57 to 69. Vpu63-81 shows only the presence of a single reverse turn at residues 74 to 77, without any evidence of helix, under the same conditions. From CD measurements the first helix extends back to residue 30 and is connected to the N-terminal anchor of Vpu. Thus the hydrophilic region of Vpu consists of two alpha-helices joined by a flexible region of 6 or 7 residues, which contains the phosphoacceptor sites of Vpu at positions 52 and 56. The second helix is followed by a single reverse turn and a flexible C-terminus.

Published
1995

45. Online Analysis of Xestodecalactones A - C, Novel Bioactive Metabolites from Fungus Penicillium cf. montanense and their subsequent Isolation from the sponge Xestospongia exigua

Author

Edrada, R. A., Heubes, M., Brauers, G., Wray, V., Berg, Anders, Gräfe, U., Wohlfahrt, M., Mühlbacher, J., Schaumann, K., Sudarsono, K., Bringmann, G., Proksch, P., Edrada, R. A., Heubes, M., Brauers, G., Wray, V., Berg, Anders, Gräfe, U., Wohlfahrt, M., Mühlbacher, J., Schaumann, K., Sudarsono, K., Bringmann, G., and Proksch, P.

Published
2002

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