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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 260 (1976), S. 151-153 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The experimental design was as follows: a solution of 11 % fluorescein isothiocyanate-labelled gelatin was micro-injected into the vegetal hemispheres of grown Rana pipiens oocytes at 34 C The oocytes were immediately cooled in ice-cold Ringer's to gel the gelatin, and then brought to 15 C. The ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 254 (1975), S. 109-114 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The permeability of the amphibian oocyte nuclear envelope in situ has been determined for three tritiated dextrans. The envelope is a sieve, restricting molecular movement between the cytoplasm and nucleus. The patent radius of its pores is about 45 ...
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 291 (1981), S. 258-261 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Oocytes were microinjected at 34 C with 50-100 nl of 14% gelatin sol, sometimes containing 3H-sucrose. The gelatin, which displaces a volume of cytoplasm, was gelled by immersing the oocyte in iced Ringer's solution for 5 min. Subsequent incubation was at 5 C. The gelled gelatin or reference phase ...
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  • 4
    ISSN: 0730-2312
    Keywords: nucclear pore complex ; nuclear transport ; Nuclear Proteins ; Nuclear nvelope ; facilitated transport ; nuclear localization signal ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Many proteins - including not only structural proteins, but also enzymes, hormone receptors, and other transcription factors - accumulate to much higher nuclear than cytoplasmic concentrations. Nuclear Localization sequences or signals (NLSs) within their primary structures entrain specific transport of these proteins through the nuclear pore complexes. Thios transport process is energy-dependent, but evidence for a true active transport mechanism is not conclusive. An alternative mechanism - facilitated transport of NLS proteins followed by their intranuclear binding - has been implicated by experiments with oil-isolated nuclei. However, there has been no agreement as to a role for binding in the in vivo nuclear accumulation of NLS-containing proteins. We Demonstrate herein that a prototypical NLs protein, Nucleoplasmin (NP), binds within the nucleus of the living Xenopus oocyte and that this binding accounts for its nuclear accumulation. © Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-7217
    Keywords: breast cancer ; cell lines ; image analysis ; infiltrating ductal carcinoma ; polypeptides ; two-dimensional polyacrylamide gel electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The protein populations of epithelial cells cultured from two neoplastic and five non-neoplastic human breast tissues were resolved and displayed by two-dimensional polyacrylamide gel electrophoresis and silverstaining. With a computer-based image analysis system, we identified eight polypeptides which are present in both of the neoplastic cell lines, but absent from all five of the cultures of non-neoplastic breast cells. The eight polypeptides are not unique to cells cultured from neoplastic breast, because they are also found in cells cultured from non-breast tissues, both neoplastic and non-neoplastic. Two of the eight polypeptides (∼ Mr 25,000/pI 4.4 and ∼ Mr 31,000/pI 5.5) are present in the patterns of whole tissue samples from infiltrating ductal carcinomas and absent in most normal breast tissue.
    Type of Medium: Electronic Resource
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