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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 377 (1995), S. 454-457 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Using a GAL4 DNA-binding domain (DBD)-RXR fusion in a yeast two-hybrid screening4, we isolated several complementary DNA clones. One of these clones, SMRT, interacts strongly with unliganded full-length retinoic-acid receptor (RAR) but weakly or ...
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We and others have previously shown that Drosophila USP dimerized with EcR and can substitute for its vertebrate counterpart, the retinoid X receptor (RXR)6, to form high-affinity DNA-binding complexes with several vertebrate nuclear receptors5'7'8. Although EcR/USP binds specifically to an ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 134 (1988), S. 189-199 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The growth of tissue culture TO-2 cells derived from the warm water fish Tilapia, the induction of thermotolerance, and protein synthesis profiles of these cells in response to temperature changes were examined. TO-2 cells can grow between 15 to 34°, with an optimal growth temperature of 31°. There is no apparent killing of the cells when the temperature is lowered to 4° for up to 3 days. Survival of TO-2 cells at 43° was studied after various preheat treatments: (1) acute heating at 40° for 15 min followed by 31° incubation, (2) chronic exposure at 37° for several hr, or (3) long-term thermal adaptation at 34°. The cells acquire thermotolerance from pre-exposure to 37° for as short as 6 hr. Preheating at 40° followed by incubation at 31° also induces thermotolerance against a subsequent 43° heat challenge. In addition, 34° thermal adapted cells are resistant to 43° heating. One- and two-dimensional gel electrophoresis of proteins after heat treatments show that three major heat shock proteins with molecular weights around 87, 70, and 27 kD are preferentially synthesized. The synthesis of two additional proteins with an isoelectric point of 6.9 and molecular weights of 60 and 44 kD are significantly enhanced in 34° thermal-adapted and 37° chronic heated cells, but not in cells subjected to an acute heat shock at either 40° or 43°. On the other hand, the 27 kD heat shock proteins are mainly present in the 43°, 40°, and 37° heat-shocked cells, but not in the 34° thermal-adapted cells.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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