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  • 1
    ISSN: 1573-5028
    Keywords: 14-3-3 protein ; Arabidopsis/ ; ascorbate peroxidase ; oxidative stress ; peroxisome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An Arabidopsis 14-3-3 protein, AFT1, was used as a ‘bait’ in the two-hybrid system to identify its interacting proteins. One of the candidate proteins, APX3, was identified as a putative peroxisomal membrane-bound ascorbate peroxidase. Ascorbate peroxidases are important defense enzymes that protect plant cells from oxidative stress damage. DNA blot analysis indicates that APX3 is encoded by a single-copy gene in the Arabidopsis genome. RNA blot analyses show that APX3 transcript levels increase slightly in response to cold, UV light, and treatments with hydrogen peroxide and paraquat. The activity of APX3 in Arabidopsis may be controlled in two ways: its enzymatic activity through protein-protein interactions and its transcription by transcriptional or posttranscriptional regulation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 31 (1993), S. 847-851 
    ISSN: 0887-624X
    Keywords: anionic ; free-radical ; transformation polymerization ; block copolymers ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: To get hydrogenated polybutadiene-polymethyl methacrylate (HPB-b-PMMA) block copolymer to be used as a compatibilizer for blends of polyolefin/polar polymer, PB-b-PMMA was synthesized by anionic-free radical mechanism transformation polymerization. Selective extraction, gradient elution thin layer chromatography, and oil-oil emulsion separation techniques were tried to attempt to separate the copolymerization products. Hydrogenation of the PB sequence in PB-b-PMMA yielded HPB-b-PMMA. The compatibilizing function of PB-b-PMMA was shown in blending experiments. © 1993 John Wiley & Sons, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The left-handed Z-DNA structure of an araC-containing (where araC stands for arabinosylcytosine) hexamer, (araC-dG)3, has been solved by x-ray diffraction analysis at 1.3 A resolution. This hexamer was crystallized in the hexagonal P6522 (a = b = 17.96 Å, c = 43.22 Å) space group in which the hexamers have statistically disordered packing arrangement along the 65 screw axis, yet the crystals diffract x-rays to high resolution. Its structure has been refined by the constrained least square refinement to a final R factor of 0.287 using 737 [〉 3.0 σ(F)] observed reflections. The asymmetric unit of the unit cell contains only a dinucleotide, 5′-p(araC)p(dG). The overall conformation resembles that of the canonical Z-DNA, but with some differences in details. The O2′ hydroxyl groups of the araC residues form intramolecular hydrogen bonds with N2 of the 5′-guanine residues. In the deep groove of Z-DNA, these hydroxy groups replace the bridging water molecules that stabilize the guanine in the syn conformation. The results reinforce the earlier observation made by the structural analysis of another hexamer, d(CG[araC]GCG), with a mono-substitution of araC [M.-K. Teng, Y.-C. Liaw, G. A. van der Marel, J. H. van Boom, and A. H.-J. Wang (1989) Biochemistry, vol. 28, pp. 4923-4928]. These two structures show that araC residue can be incorporated readily into the Z structure and probably facilitates the B to Z transition, as supported by uv absorption spectroscopic studies in a number of araC-containing oligonucleotides. The potential biological roles of the araC-modified Z-DNA are discussed. © 1992 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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