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  • 1
    Electronic Resource
    Electronic Resource
    Effect of Cu Dopant on the Electrical Property of ZnO Thin Films Deposited by Pulsed Laser Deposition (2007)
    s.l. ; Stafa-Zurich, Switzerland
    Solid state phenomena Vol. 124-126 (June 2007), p. 339-342 
    Details
    ISSN: 1662-9779
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Physics
    Notes: Cu-doped ZnO (denoted by ZnO:Cu) films have been prepared by pulsed laser depositionusing 3 wt. CuO doped ZnO ceramic target. The carrier concentrations (1011~1018 cm-3) and, electricalresistivity (10-1~105 [removed info] cm) of deposited Cu-doped ZnO thin films were varied depending ondeposition conditions. Variations of electrical properties of Cu-doped ZnO indicate that copperdopants may play an important role in determining their electrical properties, compared with undopedfilms. To investigate effects of copper dopants on the properties of ZnO thin films, X-Ray diffraction(XRD), photoluminescence (PL), and Hall measurements have been performed and corresponded
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/02/23/transtech_doi~10.4028%252Fwww.scientific.net%252FSSP.124-126.339.pdf
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  • 2
    Electronic Resource
    Electronic Resource
    Cloning of the 52-kDa chitinase gene from Serratia marcescens KCTC2172 and its proteolytic cleavage into an active 35-kDa enzyme (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 160 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A chitinase gene (pCHI52) encoding the 52-kDa chitinase was isolated from a Serratia marcescens KCTC2172 cosmid library. This chitinase gene consists of 2526 bp with an open reading frame that encodes 485 amino acids. Escherichia coli harboring the pCHI52 gene secreted not only a 52-kDa but also a 35-kDa chitinase into the culture supernatant. We purified both 52-kDa and 35-kDa chitinases using a chitin affinity column and Sephacryl-S-300 gel filtration chromatography. We determined that the 17 N-terminal amino acid sequences of the 52-kDa and the 35-kDa chitinase are identical. Furthermore, a protease obtained from S. marcescens KCTC2172 cleaved the 52-kDa chitinase into the 35-kDa protein with chitinase activity. These results suggest that the 35-kDa chitinase derives from the 52-kDa chitinase by post-translational proteolytic modification. The optimal reaction temperature of 45°C and the optimal pH of 5.5 were identical for both enzymes. The specific activities of the 52-kDa and 35-kDa chitinases on natural swollen chitin were 67 μmol min−1 mg−1 and 60 μmol min−1 mg−1, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb12905.x
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of the 54-kDa and 22-kDa chitinase genes of Serratia marcescens KCTC2172 (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 151 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A DNA fragment (pCHI5422) containing two genes encoding a 54-kDa and a 22-kDa chitinase was isolated from a cosmid DNA library of Serratia marcescens KCTC2172. The complete nucleotide sequence of pCHI5422 consisting of 4581 bp was determined. The nucleotide sequence of the 22-kDa chitinase consists of 681 bp of open reading frame encoding 227 amino acids and is located 1422 bp downstream of the translation termination codon of the 54-kDa chitinase sequence. The 54-kDa chitinase gene consisted of 1497 bp in a single open reading frame encoding 499 amino acids. The genes encoding the 54-kDa and 22-kDa chitinase were separately subcloned in Escherichia coli and the individual chitinases were expressed and purified from the culture broth using chitin affinity chromatography. When chitohexaose was used as substrate, the major product of the enzymatic reaction of both the 54-kDa and 22-kDa chitinases was a (GlcNAc)2 dimer with a minor amount of monomer. The specific activity of the 54-kDa and 22-kDa chitinases were 300 μM (min)−1 mg−1 and 17 μM (min)−1 mg−1 on the natural swollen chitin, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb12570.x
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  • 4
    Electronic Resource
    Electronic Resource
    Over-expressed rice ADP-ribosylation factor 1 (RARF1) induces pathogenesis-related genes and pathogen resistance in tobacco plants (2003)
    Oxford, UK : Munksgaard International Publishers
    Physiologia plantarum 119 (2003), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A cDNA encoding RARF1 (rice ADP-ribosylation factor 1) was isolated from fungal elicitor-treated rice suspension culture cells by mRNA differential display. RARF1 transcripts accumulated in response to hydrogen peroxide (H2O2) and salicylic acid (SA) and rapidly in cells inoculated with an avirulent pathogen. Constitutively over-expressed RARF1 under the control of the cauliflower mosaic virus 35S promoter (CaMV 35S) triggered spontaneous induction of lesion mimics, induced an array of pathogenosis-related (PR) genes, reduced susceptibility to a fungal pathogen, and caused accumulation of SA. From these data, we deduced that RARF1 might be a component of various plant defence signalling pathways involved in inducing the expression of a subset of PR genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1399-3054.2003.00215.x
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  • 5
    Electronic Resource
    Electronic Resource
    Purification of an antifungal PR-5 protein from flower buds of Brassica campestris and cloning of its gene (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 101 (1997), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: An antifungal pathogenesis-related (PR) group 5 protein with a molecular mass of 27 kDa (BFTP) was purified from flower buds of Brassica campestris. BFTP exhibits antifungal activity against Neurospora crassa, causing rapid release of cytoplasmic material at the hyphal tips of the fungus. BFTP immuno-cross-reacts with antiserum raised against the tobacco osmotin-like PR-5 protein. Using a PCR product generated with the help of two degenerate PCR primers for (1) the N-terminal amino acid sequence of the protein and (2) the conserved peptide domain that appears in all PR-5 proteins, we were able to isolate from a flower-bud cDNA library a cDNA (933 bp) that encodes this protein (pBFTP). The deduced amino acid sequence shows high similarity to PWIR2 from wheat (43%) and thaumatin II from Thaumatococcus daniellii Benth (40%). It contains the 16 cysteine residues that are conserved in all PR-5 proteins at their invariant positions. The cDNA predicts the synthesis of a preprotein which is subsequently processed into the mature protein by removal of an N-terminal signal peptide. The mRNA is predominantly expressed in flower buds, with a moderate level of transcripts detected in stems. Very low levels of the mRNA are present in root and leaf tissue. The gene is a member of a small multigene family in the genome of B. campestris.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1997.tb01041.x
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  • 6
    Electronic Resource
    Electronic Resource
    Mutations in the amino-terminal domain of λ-integrase have differential effects on integrative and excisive recombination (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 55 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Lambda integrase (Int) forms higher-order protein–DNA complexes necessary for site-specific recombination. The carboxy-terminal domain of Int (75–356) is responsible for catalysis at specific core-type binding sites whereas the amino-terminal domain (1–70) is responsible for cooperative arm-type DNA binding. Alanine scanning mutagenesis of residues 64–70, within full-length integrase, has revealed differential effects on cooperative arm binding interactions that are required for integrative and excisive recombination. Interestingly, while these residues are required for cooperative arm-type binding on both P′1,2 and P′2,3 substrates, cooperative binding at the arm-type sites P′2,3 was more severely compromised than binding at arm-type sites P′1,2 for L64A. Concomitantly, L64A had a much stronger effect on integrative than on excisive recombination. The arm-binding properties of Int appear to be intrinsic to the amino-terminal domain because the phenotype of L64A was the same in an amino-terminal fragment (Int 1–75) as it was in the full-length protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04447.x
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of two fungal-elicitor-induced rice cDNAs encoding functional homologues of the rab-specific GDP-dissociation inhibitor (1999)
    Springer
    Planta 210 (1999), S. 143-149 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Differential display ; Functional analysis ; Fungal elicitor treatment ; Oryza (rab-GDIs) ; Pathogen signaling ; Rab-specific GDP dissociation inhibitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. By using the mRNA differential display approach to isolate defense signaling genes active at the early stage of fungal infection two cDNA fragments with high sequence homology to rab-specific GDP-dissociation inhibitors (GDIs) were identified in rice (Oryza sativa L.) suspension cells. Using polymerase-chain-reaction products as probes, two full-length cDNA clones were isolated from a cDNA library of fungal-elicitor-treated rice, and designated as OsGDI1 and OsGDI2. The deduced amino acid sequences of the isolated cDNAs exhibited substantial homology to Arabidopsis rab-GDIs. Northern analysis revealed that transcripts detected with the 3′-gene-specific DNA probes accumulated to high levels within 30 min after treatment with a fungal elicitor derived from Magnaporthe grisea. The functionality of the OsGDIs was demonstrated by their ability to rescue the Sec19 mutant of Saccharomyces cerevisiae which is defective in vesicle transport. The proteins, expressed in Escherchia coli, cross-reacted with a polyclonal antibody prepared against bovine rab-GDI. Like bovine rab-GDI, the OsGDI proteins efficiently dissociated rab3A from bovine synaptic membranes. Using the two-hybrid system, it was shown that the OsGDIs specifically interact with the small GTP-binding proteins belonging to the rab subfamily. The specific interaction was also demonstrated in vitro by glutathione S-transferase resin pull-down assay.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050663
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  • 8
    Electronic Resource
    Electronic Resource
    High-temperature superconducting dual-mode resonator on (100) MgO substrate (1995)
    Springer
    Journal of superconductivity 8 (1995), S. 227-231 
    Details
    ISSN: 1572-9605
    Keywords: High-temperature superconductivity ; superconducting dual-mode resonator ; superconducting thin film ; superconducting microwave device ; pulsed laser deposition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: Abstract We report, for the first time to our knowledge, a clear resonant peak split in the range of 7.7–9.7 GHz in a perturbed dual-mode disk-type resonator (DMDR) made of YBa2Cu3O7−x (YBCO) superconducting thin film on MgO substrate. Epitaxial YBCO superconducting thin films were grown on (100) MgO substrates by pulsed laser deposition technique. The critical temperature of superconducting thin film on MgO substrate was 85 K. Superconducting dualmode disk resonators were designed by microwave design software, EEsof, and patterned by photolithography and a wet-etch process. The unloaded quality factor (QUL) of the superconducting DMDR was found to be 1,312 at 77 K. We believe this type of DMDR can be utilized for dual-mode resonator-based filters for satellite communications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00732375
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  • 9
    Electronic Resource
    Electronic Resource
    Effect of PrBa2Cu3O7−x buffer layer thickness on the properties of YBa2Cu3O7−x thin films grown on sapphire by laser ablation (1996)
    Springer
    Journal of superconductivity 9 (1996), S. 545-549 
    Details
    ISSN: 1572-9605
    Keywords: Laser ablation ; superconducting thin film ; buffer layer thickness ; interdiffusion ; sapphire substrate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: Abstract Superconducting YBa2Cu3O7−x (YBCO) thin films were deposited onr-plane A12O3 substrates with PrBa2Cu3O7−x (PBCO) buffer layer by XeCl excimer laser ablation. The thickness of PBCO buffer layer was systematically changed to investigate the superconducting properties of YBCO thin films on sapphire. The structure and surface morphology of the films were characterized by X-ray diffraction and scanning electron microscopy (SEM). Superconducting transition temperatures were varied depending on the buffer layer thickness. Interdiffusion between laser-ablated YBCO thin films and A12O3 substrates had been studied by Auger electron spectroscopy (AES). The results of this study show that diffusion does not occur between the YBCO thin film and the substrate even with 20 Å thick PBCO buffer layer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00723529
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  • 10
    Electronic Resource
    Electronic Resource
    Characterization and cDNA cloning of two glycine- and histidine-rich antimicrobial peptides from the roots of shepherd's purse, Capsella bursa-pastoris (2000)
    Springer
    Plant molecular biology 44 (2000), S. 187-197 
    Details
    ISSN: 1573-5028
    Keywords: antimicrobial peptide ; Capsella bursa-pastoris ; glycine-rich peptide ; histidine-rich peptide ; shepherd's purse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two novel antimicrobial peptides were isolated and characterized from the roots of shepherd's purse, Capsella bursa-pastoris. These antimicrobial peptides, named shepherin I and shepherin II, consist of 28 and 38 amino acids, respectively, and are glycine- and histidine-rich peptides. Shepherin I and shepherin II have 67.9% and 65.8% (mol/mol) glycine, respectively, and 28.6% and 21.1% (mol/mol) histidine, respectively. Both shepherins have a Gly-Gly-His motif. These antimicrobial peptides exhibit antimicrobial activity against Gram-negative bacteria and fungi. Circular dichroism spectra of shepherin I and shepherin II showed that shepherin I and shepherin II in 50% trifluoroethanol have 66.7% and 75% random coils, respectively, without any α-helices. cDNA sequence analysis revealed that shepherin I and shepherin II are produced from a single polypeptide, designated shep-GRP, consisting of 120 amino acids; shep-GRP has five distinct domains, an amino-terminal putative signal peptide, a shepherin I, a linker dipeptide, a shepherin II and a carboxy-terminal peptide. Southern blot analysis indicates that the gene encoding shepherins belongs to a low-complexity gene family. Northern blot analysis revealed that transcripts of shep-GRP are present in roots but not in leaves and stems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006431320677
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