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  • 1
    Electronic Resource
    Electronic Resource
    Influence of Si addition on thermal stability and soft magnetic properties for Fe–Al–Ga–P–C–B glassy alloys : The 7th joint MMM-intermag conference on magnetism and magnetic materials (1998)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 83 (1998), S. 6329-6331 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: The thermal stability of the supercooled liquid region (ΔTx), defined by the difference between crystallization temperature (Tx) and glass transition temperature (Tg), and soft magnetic properties were investigated for Fe70Al5Ga2P12.65−xC5.75B4.6Six(x=0–4) and Fe77Al2.14Ga0.86P11−xC5B4Six(x=0–3) glassy alloys. The thermal stability, glass forming ability and effective permeability (μe) at 1 kHz are improved with the replacement of P by 1–3 at. % Si for Fe70Al5Ga2P12.65−xC5.75B4.6Six and by 1–2.6 at. % Si for Fe77Al2.14Ga0.86P11−xC5B4Six. The ΔTx and the maximum thickness for glass formation (tmax) reach maximum values of 60 K and 280 μm, respectively, for Fe70Al5Ga2P12.65−xC5.75B4.6Six and 34 K and 220 μm, respectively, for Fe77Al2.14Ga0.86P11−xC5B4Six at Si(at. %)/(Si(at. %)+P(at. %))=0.24. Core losses for Fe77Al2.14Ga0.86P8.4C5B4Si2.6 glassy alloy is much lower than that for amorphous Fe–Si–B alloy at the sheet thickness more than 70 μm. Therefore, it can be said that the Fe–Al–Ga–P–C–B–Si glassy alloys are useful for inductive applications because of their bulky shape and good soft magnetic properties. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.367812
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  • 2
    Electronic Resource
    Electronic Resource
    Pressure-induced intra-4f luminescence in GaAs:Er,O (1997)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 71 (1997), S. 93-95 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: In metalorganic chemical vapor deposition grown GaAs:Er,O samples, at ambient pressure, only the ErGa−2O center is excited by above band gap host photoexcitation (host excitation) and shows a sharp infrared luminescence spectra due to intra-4f transitions in the Er3+ ion. It is found, at high pressure, that at least two other Er centers become optically active by host excitation. One of these pressure-induced centers is assigned to a specific Er center having slightly different atomic configuration than the ErGa−2O center by comparing the pressure-induced photoluminescence (PL) spectra with the site-selective PL spectra. © 1997 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.119479
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  • 3
    Electronic Resource
    Electronic Resource
    Pressure-Induced Increase of the Intra-4f Luminescence of GaAs:Er,O at Room Temperature (1995)
    s.l. ; Stafa-Zurich, Switzerland
    Materials science forum Vol. 196-201 (Nov. 1995), p. 645-650 
    Details
    ISSN: 1662-9752
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/02/01/transtech_doi~10.4028%252Fwww.scientific.net%252FMSF.196-201.645.pdf
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  • 4
    Electronic Resource
    Electronic Resource
    Phenotypes ofdnaA mutants ofEscherichia coli sensitive to phenothiazine derivatives (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 212-215 
    Details
    ISSN: 1617-4623
    Keywords: Escherichia coli ; Phenothiazine derivatives ; DnaA protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The activation of DnaA protein by cardiolipin is inhibited by fluphenazinein vitro. We therefore examined the sensitivity of temperature-sensitivednaA mutants ofEscherichia coli to fluphenazine and other phenothiazine derivatives. Among the eightdnaA mutants tested,dnaA5, dnaA46 dnaA602, anddnaA604, mutants with mutations in the putative ATP binding site of DnaA protein, showed higher sensitivities to phenothiazine derivatives than did the wild-type strain. ThednaA508 anddnaA167 mutants, which have mutations in the N-terminal region of DnaA protein, also showed higher sensitivities to phenothiazine derivatives. On the other hand, thednaA204 anddnaA205 mutants, with lesions in the C-terminal region of the DnaA protein, showed the same sensitivity to phenothiazine derivatives as the wild-type strain. Complementation analysis with a plasmid containing the wild-typednaA gene and phage P1-mediated transduction confirmed thatdnaA mutations are responsible for these sensitivity phenotypes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02173222
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  • 5
    Electronic Resource
    Electronic Resource
    Increase in synthesis and stability of σ 32 on treatment with inhibitors of DNA gyrase in Escherichia coli (1996)
    Springer
    Molecular genetics and genomics 253 (1996), S. 297-302 
    Details
    ISSN: 1617-4623
    Keywords: Key words Inhibitors of DNA gyrase ; Heat shock response ; σ32
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  We report here that in Escherichia coli, the anti-bacterial agent nalidixic acid induces transient stabilization and increased synthesis of σ32, accompanied by the induction of heat shock proteins (Dnak and GroEL proteins). The induction of heat shock proteins, increased synthesis of σ32, and stabilization of σ32 observed on treatment of wild-type cells with nalidixic acid were not observed in a nalA26 mutant, a strain that is resistant to nalidixic acid as the result of a mutation in the gyrA gene. Not only oxolinic acid, but also novobiocin, whose targets are the A and B subunits of DNA gyrase, respectively, also induced stabilization and increased synthesis of σ32. Thus, inhibition of the activity of DNA gyrase may cause stabilization and increased synthesis of σ32, resulting in turn in induction of heat shock proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00008596
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