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  • 1
    Electronic Resource
    Electronic Resource
    Lectin binding sites during Drosophila embryogenesis (1995)
    Springer
    Development genes and evolution 204 (1995), S. 229-243 
    Details
    ISSN: 1432-041X
    Keywords: Glycan structures ; Lectins ; Drosophila Embryogenesis ; Development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The spectrum of lectin binding sites as it emerges during embryonic development of Drosophila was analysed by means of fluorescein-labelled lectins. As development and morphogenesis proceed, the reaction pattern becomes more and more complex. Mannose/glucose-, mannose-, N-acetylglucosamine- and poly-N-ace-tylglucosamine-specific lectins bind ubiquitously. Nuclear envelopes only have binding sites for wheat germ agglutinin. N-acetylgalactosamine-binding lectins are specific for ectodermal derivatives. Gaβ-3-N-acetylgalac-tosamine-binding lectins are highly selective markers for neural structures, haemocytes and Garland cells. It is also shown that Drosophila laminin is differentially glycosylated. The possible implications of differential and germ layer-specific glycosylation are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00208490
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  • 2
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of a transactivating Bombyx mori nuclear polyhedrosis virus immediate early gene
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression 1129 (1992), S. 328-330 
    Details
    ISSN: 0167-4781
    Keywords: Baculovirus ; BmNPVIEG ; Nuclear polyhediosis virus ; Transactivation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0167-4781(92)90511-W
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of a Cloned Locust Tyramine Receptor cDNA by Functional Expression in Permanently Transformed Drosophila S2 Cells (1995)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 64 (1995), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The cDNA for Tyr-Loc, a G protein-coupled receptor that clearly shows homology to a number of mammalian and fruit fly receptors for biogenic amines, was cloned from the nervous system of Locusta migratoria. Functional expression of the cloned cDNA was obtained in cultured insect cells, i.e., in Spodoptera SF9 cells using a baculoviral expression system and in stably transformed Drosophila Schneider 2 (S2) cells. Multiple copies of the receptor expression construct are inserted into the genome of these permanently transformed cells. The expression of the receptor cDNA was driven by the upstream sequences of a Bombyx mori baculoviral immediate early gene. Tyramine shows a much higher binding affinity to this receptor than other possible endogenous ligands. It also reduces forskolin-induced cyclic AMP production in the permanently transformed S2 cells. The pharmacological profile of the Tyr-Loc receptor is distinct from that of any locust receptor-type described so far, but it is similar to that of the Drosophila tyramine/octopamine receptor. In the locust CNS, the Tyr-Loc mRNA is not present in the distal part of the optic lobes but has a widespread distribution in the brain and the ventral nerve cord.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1995.64062387.x
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    Paper (German National Licenses)
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