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  • 1995-1999  (2)
  • 1975-1979  (3)
  • 1970-1974  (1)
  • 1
    Electronic Resource
    Electronic Resource
    COLD-LABILE AND COLD-STABLE MICROTUBULES IN THE MITOTIC SPINDLE OF MAMMALIAN CELLS (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 253 (1975), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1975.tb19218.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The cenpB gene is not essential in mice (1998)
    Springer
    Chromosoma 107 (1998), S. 570-576 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract.  Centromere protein B (CENP-B) is a centromeric DNA-binding protein that binds to α-satellite DNA at the 17 bp CENP-B box sequence. The binding of CENP-B, along with other proteins, to α-satellite DNA sequences at the centromere, is thought to package the DNA into heterochromatin subjacent to the kinetochore of mitotic chromosomes. To determine the importance of CENP-B to kinetochore assembly and function, we generated a mouse null for the cenpB gene. The deletion removed part of the promoter and the entire coding sequence except for the carboxyl-terminal 35 amino acids of the CENP-B polypeptide. Mice heterozygous or homozygous for the cenpB null mutation are viable and healthy, with no apparent defect in growth and morphology. We have established mouse embryo fibroblasts from heterozygous and homozygous cenpB null littermates. Microscopic analysis, using immunofluorescence and electron microscopy of the cultured cells, indicated that the centromere-kinetochore complex was intact and identical to control cells. Mitosis was identical in fibroblasts derived from cenpB wild-type, heterozygous and null animals. Our studies demonstrate that CENP-B is not required for the assembly of heterochromatin or the kinetochore, or for completion of mitosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004120050343
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Localization of tubulin in the mitotic apparatus of mammalian cells by immunofluorescence and immunoelectron microscopy (1977)
    Springer
    Chromosoma 60 (1977), S. 223-235 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Antitubulin antibody was used as an immunofluorescent and immunoelectron microscopic probe to localize tubulin in components of the mitotic apparatus of rat kangaroo (strain PtK1) cells in vitro. In addition to the detection of tubulin in the spindle microtubules and centrioles, other structures were found to display specific staining including kinetochores, amorphous pericentriolar material and small virus-like particles associated with the centrioles. The kinetochores consisted of a densely stained outer layer about 400 Å thick which is separated from an inner layer of the same dimension by a lightly staining middle layer. Microtubules were primarily associated with the outermost plate of the kinetochore but tubulin was uniformly distributed in both outer and inner plates. Colcemid treatment prevented the assembly of spindle microtubules and resulted in specific alterations of the kinetochore but failed to diminish the staining of the kinetochores. These observations suggest that tubulin molecules may comprise an important structural component of the kinetochore.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00329772
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation (1997)
    Springer
    Chromosoma 106 (1997), S. 348-360 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. We have generated and characterized a novel site-specific antibody highly specific for the phosphorylated form of the amino-terminus of histone H3 (Ser10). In this study, we used this antibody to examine in detail the relationship between H3 phosphorylation and mitotic chromosome condensation in mammalian cells. Our results extend previous biochemical studies by demonstrating that mitotic phosphorylation of H3 initiates nonrandomly in pericentromeric heterochromatin in late G2 interphase cells. Following initiation, H3 phosphorylation appears to spread throughout the condensing chromatin and is complete in most cell lines just prior to the formation of prophase chromosomes, in which a phosphorylated, but nonmitotic, chromosomal organization is observed. In general, there is a precise spatial and temporal correlation between H3 phosphorylation and initial stages of chromatin condensation. Dephosphorylation of H3 begins in anaphase and is complete immediately prior to detectable chromosome decondensation in telophase cells. We propose that the singular phosphorylation of the amino-terminus of histone H3 may be involved in facilitating two key functions during mitosis: (1) regulate protein-protein interactions to promote binding of trans-acting factors that “drive” chromatin condensation as cells enter M-phase and (2) coordinate chromatin decondensation associated with M-phase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004120050256
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  • 5
    Electronic Resource
    Electronic Resource
    Arrangement of centromeres in mouse cells (1971)
    Springer
    Chromosoma 34 (1971), S. 73-87 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Applying a staining procedure which reveals constitutive heterochromatin to cytological preparations of the mouse (Mus musculus), one detects heterochromatin pieces at the centromeric areas of all chromosomes except the Y. The Y chromosome is somewhat heteropyenotic in general but possesses no intensely stained centromeric heterochromatin. The arrangement of the centromeric heterochromatin in interphase cells is apparently specific for a given cell type. In meiotic prophase, centromeric heterochromatin may form clusters among bivalents. From the location of the centromeric heterochromatin of the X chromosome in the sex bivalent, it is concluded that the association between the X and Y (common end) in meiosis is limited to the distal portions of the sex elements.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00285517
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Structure and control of assembly of cytoplasmic microtubules in normal and transformed cells (1976)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 5 (1976), S. 497-514 
    Details
    ISSN: 0091-7419
    Keywords: Cytoplasmic microtubule complex ; calcium ; normal and transformed cells ; in vivo control ; effects of trypsin ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Indirect immunoflurescence analyses using antibodieis directed against 6S tubulin have shown an elaborate cytoplasmic microtubule complex (CMTC) in nontransformed cells in culture. The CMTC is strikingly altered in cells that have been transformed spontaneously by viruses or by chemicals. Assembly of microtubules in vitro and in vivo is markedly inhibited in the presence of elevated levels of calcium. Alteration of the surface of normal cells by brief treatment with low concentrations of trypsin initiate a rapid breakdown of cytoplasmic microtubules. Finally, a hypothesis is presented relating microtubule assembly and surface membrane modulation suggesting that calcium is the primary modulating signal.
    Additional Material: 19 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400050407
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