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  • 1
    Electronic Resource
    Electronic Resource
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 69 (1996), S. 3423-3425 
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: HgBa2Ca2Cu3Oy (Hg-1223) films with a thickness of 1–2 μm and Tc (zero)∼130 K have been fabricated by utilizing a spray pyrolysis technique. X-ray diffraction indicates that the films consist of predominantly Hg-1223 phase grains with c-axis orientation. Moreover, the oscillation photograph taken by a Weissenberg camera confirms that the film grains are in-plane aligned and epitaxially grown on SrTiO3. In electrical transport measurements, the as-fabricated film exhibits a Tc (zero) of 123 K, and a zero-field Jc of 3.7×105 A/cm2 at 77 K. Additional post-annealing at 320 °C for 50 h in flowing oxygen has improved the transport properties as Tc (zero)∼130 K and Jc∼4.4×105 A/cm2 (77 K, 0 T). © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 72 (1998), S. 972-974 
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: (Hg1−xRex)Ba2CaCu2Oy (x(approximate)0.1) thin films have been prepared ex situ on LaAlO3 substrates by a two-step process in which an HgO/Re0.1Ba2CaCu2Oy multilayer precursor film is annealed in a quartz tube using an unreacted monoxide pellet containing HgO as an Hg vapor source. By varying the composition of the monoxide pellet, the film orientation can be changed from c-axis to the predominantly a-axis one. The a-axis growth of the grains directly on the substrate is confirmed by x-ray diffraction and transmission electron microscopic observation, although the grains are twinned with 90° orientation. The a-axis films exhibit a Tc onset and Tc zero of approximately 110–127 and 55 K, respectively, suggesting substantial influence of weak links at the grain boundaries on their transport properties. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology and Plant Molecular Biology 49 (1998), S. 1-24 
    ISSN: 1040-2519
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract Ovules are the direct precursors of seeds and thus play central roles in sexual plant reproduction and human nutrition. Extensive classical studies have elucidated the evolutionary trends and developmental processes responsible for the current wide variety of ovule morphologies. Recently, ovules have been perceived as an attractive system for the study of genetic regulation of plant development. More than a dozen regulatory genes have now been identified through isolation of ovule mutants. Characterization of these mutants shows that some aspects of ovule development follow independent pathways, while other processes are interdependent. Some of these mutants have ovules resembling those of putative ancestors of angiosperms and may help in understanding plant evolution. Clones of several of the regulatory genes have been used to determine expression patterns and putative biochemical functions of the gene products. Newly constructed models of genetic regulation of ovule development provide a framework for interpretation of future discoveries.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 252 (1996), S. 510-517 
    ISSN: 1617-4623
    Keywords: FK506 binding protein (FKBP) ; Immunophilins ; Tetratricopeptide repeat (TPR) ; Plant stress ; Arabidopsis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated clones of an Arabidopsis gene (ROF1, forrotamaseFKBP) encoding a high molecular weight member of the FK506 binding protein (FKBP) family. The deduced amino acid sequence of ROF1 predicts a 551-amino acid, 62 kDa polypeptide which is 44% identical to human FKBP59 — a 59 kDa FKBP which binds to the 90 kDa heat shock protein and is associated with inactive steroid hormone receptors. ROF1 contains three FKBP12-like domains in the N-terminal portion of the protein (in contrast to two domains in mammalian FKBP59), an internal repeat structure associated with protein-protein interactions (tetratricopeptide repeats), and a putative calmodulin binding domain near the C-terminal region of the protein. No sequences associated with protein translocation out of the cytosol were found in ROF1.ROF1 mRNA was found at equivalent low levels in light-grown roots, stems, and flowers and at slightly higher levels in leaves. The abundance ofROF1 mRNA increased several-fold under stress conditions such as wounding or exposure to elevated NaCl levels.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 252 (1996), S. 510-517 
    ISSN: 1617-4623
    Keywords: Key words FK506 binding protein (FKBP) ; Immunophilins ; Tetratricopeptide repeat (TPR) ; Plant stress ; Arabidopsis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  We have isolated clones of an Arabidopsis gene (ROF1, for rotamase FKBP) encoding a high molecular weight member of the FK506 binding protein (FKBP) family. The deduced amino acid sequence of ROF1 predicts a 551-amino acid, 62 kDa polypeptide which is 44% identical to human FKBP59 – a 59 kDa FKBP which binds to the 90 kDa heat shock protein and is associated with inactive steroid hormone receptors. ROF1 contains three FKBP12-like domains in the N-terminal portion of the protein (in contrast to two domains in mammalian FKBP59), an internal repeat structure associated with protein-protein interactions (tetratricopeptide repeats), and a putative calmodulin binding domain near the C-terminal region of the protein. No sequences associated with protein translocation out of the cytosol were found in ROF1. ROF1 mRNA was found at equivalent low levels in light-grown roots, stems, and flowers and at slightly higher levels in leaves. The abundance of ROF1 mRNA increased several-fold under stress conditions such as wounding or exposure to elevated NaCl levels.
    Type of Medium: Electronic Resource
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