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All Library Books, journals and Electronic Records Telegrafenberg

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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 97 (1975), S. 6181-6186 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 101 (1979), S. 272-273 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 105 (1983), S. 4226-4232 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 386 (1997), S. 757-758 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] And as our vineyards, fallows, meads and hedges, Defective in their natures, grow to wildness, Even so our houses and ourselves and children Have lost, or do not want to learn for want of time, The sciences that should become our country. Henry V.V.ii 54-58 Throughout the world, but ...
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Entomology 48 (2003), S. 1-27 
    ISSN: 0066-4170
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: In the absence of fossils, the cells of vertebrates are often described in lieu of a general animal eukaryote model, neglecting work on insects. However, a common ancestor is nearly a billion years in the past, making some vertebrate generalizations inappropriate for insects. For example, insect cells are adept at the cell remodeling needed for molting and metamorphosis, they have plasma membrane reticular systems and vacuolar ferritin, and their Golgi complexes continue to work during mitosis. This review stresses the ways that insect cells differ from those of vertebrates, summarizing the structure of surfacce membranes and vacuolar systems, especially of the epidermis and fat body, as a prerequisite for the molecular studies needed to understand cell function. The objective is to provide a structural base from which molecular biology can emerge from biochemical description into a useful analysis of function.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Naturwissenschaften 53 (1966), S. 510-510 
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Naturwissenschaften 53 (1966), S. 510-510 
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 21 (1992), S. 101-110 
    ISSN: 0886-1544
    Keywords: F-actin ; silk gland ; phalloin ; periluminal circumferential actin bundles ; actin-coated vacuoles ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Labeling of silk glands with rhodaminyl-phalloin shows that most F-actin is restricted to parallel bundles that form rings around the gland lumen at the apical cell surface. The bundles are lost when larval feeding stops at moulting, and the F-actin is redistributed through the cytoplasm as coats to vacuoles and, occasionally, in variably oriented strands. After moulting there is a return to the distribution of filamentous actin in the apical periluminal rings of bundles. These events occur at the same time as F-actin in the nuclear shell [Henderson and Locke, submitted] undergoes its own set of changes. In silk gland cells two kinds of f-actin deployment take place concurrently.
    Additional Material: 9 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 23 (1992), S. 169-187 
    ISSN: 0886-1544
    Keywords: nuclear actin ; nuclear myosin ; nuclear shell ; nuclear shape ; nuclear matrix ; silk gland ; nuclear structure ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The branched nuclei from silk gland cells of larvae of Calpodes ethlius label with antibodies to actin and myosin and with rhodaminyl-phalloin, which is specific for f-actin. Optical sectioning localizes this actin and myosin to the nuclear periphery. Residual nuclear-associated fractions prepared from these cells contain sheets of nuclear lamina-like structures that bind heavy meromyosin and gold-tagged antibodies to actin and myosin. The results suggest that both actin and myosin, or a myosin-like protein, are components of a layer at the nucleocytoplasmic boundary that we call the nuclear shell. The nuclear shell appears to be associated with the nuclear envelope and may correspond to a zone on the cytoplasmic face of the envelope seen in electron micrographs of unextracted cells. The residual nuclear-associated fraction has a unique isoform of actin (43 kD, pl 6.45) that might allow the nuclei to associate with an actin network structurally and developmentally distinct from that of the cytoplasm. © 1992 Wiley-Liss, Inc.
    Additional Material: 14 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 29 (1994), S. 1-10 
    ISSN: 1059-910X
    Keywords: Aldehyde/UA fixation ; Preservation of cytoskeleton ; Nuclear skeleton ; Perinuclear shell ; Immunogold and lectin-gold labelling ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Conventional treatment of tissues for sectioning and transmission electron microscopy uses aldehyde fixation and osmium tetroxide postfixation. Although the result is aesthetically pleasing, osmication destroys some cell components and reduces the chemical activity of others, such as reactions with antibodies and lectins. We have found that aldehyde fixation followed by uranyl acetate preserves and contrasts most structures and visualizes some that are not easily seen after osmication. Aldehyde/UA treated tissues have enough contrast to be observed without section staining while retaining some of the chemical activity that is lost through osmication. Sections of tissues with good preservation and contrast can be used for immunogold and lectin-gold labelling of at least some molecules. © 1994 Wiley-Liss, Inc.
    Additional Material: 12 Ill.
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