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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 143 (1967), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 331 (1988), S. 721-723 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 Visualization of fibre gap junctions by anti-MP70 immuno- fluorescence microscopy. Each fluorescent plaque represents a gap junction structure based on previous correlations with immunoelectron microscopy7. Methods. A lens of a ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 83 (1988), S. 129-145 
    ISSN: 1573-4919
    Keywords: tight junction ; zonula occludens ; epithelium ; junctional complex ; cell polarity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The tight junction, or zonula occludens (ZO), forms a semi-permeable barrier in the paracellular pathway in most vertebrate epithelia. The ZO is the apical-most member of a series of intercellular junctions, collectively known as the junctional complex, found at the interface of the apical and lateral cell surface. This structure not only restricts movement of substances around the cells, but may also serve as a ‘fence’ acting to maintain the cell surface compositional polarity characteristic of epithelial cells. The morphology and physiology of the ZO have been well documented and are briefly reviewed here. The biochemistry of this important intercellular junction remains largely unknown, although a tight junction-specific polypeptide called ‘ZO-1’ has recently been identified. Preliminary observations regarding the role of this peripheral phosphoprotein in the biology of the ZO are presented.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1059-910X
    Keywords: Cell-to-cell channels ; Connexins ; Membranes ; Intercellular communication ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Recent advances in understanding lens fiber gap junction formation are reviewed. These include studies of junctional protein expression in the embryonic lens, and of age related changes affecting gap junction structure and composition in the adult lens. An in vitro assembly system based on detergent solubilized pore complexes and endogenous lipids has been developed to provide information on the molecular interactions involved in gap junction formation and to provide material for structure analysis. Important information on the electrical properties of lens gap junction channels is obtained using electrophysiological techniques including planar lipid bilayer analysis and patch clamping. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    BioEssays 9 (1988), S. 167-168 
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The intercellular junctions connecting the cytoplasms of fibre cells in the mammalian lens have until recently been regarded as a class of junction which is fundamentally different from that of the gap junctions in other organs. Recent observations, however, suggest that the lens junctions fit protein topology predictions common for all gap junctions. While the homologous peptide portions are predicted to form the channels, the divergent peptide portions of the gap junction polypeptides may adapt channel activity to the special tissue requirements.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    BioEssays 5 (1986), S. 79-83 
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Two kinds of membrane contacts in the vertebrate lens are described. Fiber gap junctions are domains where small molecules can pass between lens cells. Membrane structures of ball-and-socket type interlock adjacent lens fibers and thus contribute to the structural integrity of the lens. Both of these membrane contacts appear crucial for the maintenance of lens transparency.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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