Search Results - (Author, Cooperation:K. E. Zinsmaier)

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  1. 1
    Y. Zhou ; C. O. Wong ; K. J. Cho ; D. van der Hoeven ; H. Liang ; D. P. Thakur ; J. Luo ; M. Babic ; K. E. Zinsmaier ; M. X. Zhu ; H. Hu ; K. Venkatachalam ; J. F. Hancock
    American Association for the Advancement of Science (AAAS)
    Published 2015
    Staff View
    Publication Date:
    2015-08-22
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Animals ; Cell Line, Tumor ; Cell Membrane/metabolism/*physiology ; Cricetinae ; Drosophila melanogaster ; Fibroblasts ; *Membrane Potentials ; Mice ; Neurons ; Phosphatidylinositol 4,5-Diphosphate/*metabolism ; Phosphatidylserines/*metabolism ; Signal Transduction ; ras Proteins/*metabolism
    Published by:
    http://www.aaas.org/

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  2. 2
    Staff View
    ISSN:
    1432-0878
    Keywords:
    Key words Exocytosis ; “J” domain ; Gene knock-out ; Temperature-sensitive paralysis ; Chaperone ; Calcium channel ; Drosophila melanogaster (Insecta)
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Medicine
    Notes:
    Abstract  The “cysteine string protein” (CSP) genes of higher eukaryotes code for a novel family of proteins characterized by a “J” domain and an unusual cysteine-rich region. Previous studies had localized the proteins in neuropil and synaptic terminals of larval and adult Drosophila and linked the temperature-sensitive paralysis of the mutants described here to conditional failure of synaptic transmission. We now use the null mutants as negative controls in order to reliably detect even low concentrations of CSPs by immunohistochemistry, employing three monoclonal antibodies. In wild-type flies high levels of cysteine string proteins are found not only in apparently all synaptic terminals of the embryonic, larval, and adult nervous systems, but also in the “tall cells” of the cardia, in the follicle cells of the ovary, in specific structures of the female spermatheca, and in the male testis and ejaculatory bulb. In addition, low levels of CSPs appear to be present in all tissues examined, including neuronal perikarya, axons, muscles, Malpighian tubules, and salivary glands. Western blots of isolated tissues demonstrate that of the four isoforms expressed in heads only the largest is found in non-neural organs. The wide expression of CSPs suggests that at least some of the various phenotypes of the null mutants observed at permissive temperatures, such as delayed development, short adult lifespan, modified electroretinogram, and optomotor behavior, may be caused by the lack of CSPs outside synaptic terminals.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/s004410051170

    Articles: DFG German National Licenses