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  • Articles  (4)
  • Articles: DFG German National Licenses  (4)
  • Blackwell Publishing Ltd  (4)
  • American Chemical Society (ACS)
  • Elsevier
  • 1995-1999  (4)
  • 1960-1964
  • 1998  (4)
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  • Articles  (4)
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  • 1995-1999  (4)
  • 1960-1964
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  • 1
    Electronic Resource
    Electronic Resource
    Inheritance of Russian wheat aphid resistance in PI 140207 spring wheat (1998)
    Oxford, UK : Blackwell Publishing Ltd
    Plant breeding 117 (1998), S. 0 
    Details
    ISSN: 1439-0523
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: The Russian wheat aphid (RWA), Diuraphis noxia (Mordvilko), has become a serious, perennial pest of wheat (Triticum aestivum L.) in many areas of the world. This study was initiated to determine the inheritance of RWA resistance in PI 140207 (a RWA-resistant spring wheat) and to determine its allelic relationship with a previously reported RWA resistance gene. Crosses were made between PI 140207 and ‘Pavon’ (a RWA-susceptible spring wheat). Genetic analysis was performed on the parents, F1, F2, backcross (BC) population and F2-derived F3 families. Analyses of segregation patterns of plants in the F1, F2, and BC populations, and F2-derived F3 families indicated single dominant gene control of RWA resistance in PI 140207. Results of the allelism test indicated that the resistance gene in PI 140207, while conferring distinctly different seedling reactions to RWA feeding, is the same as Dn 1, the resistance gene in PI 137739.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1439-0523.1998.tb01944.x
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  • 2
    Electronic Resource
    Electronic Resource
    A RAPID NON-INVASIVE TECHNIQUE FOR DISTINGUISHING HARBOR SEALS (PHOCA VITULINA) IN THEIR FIRST YEAR FROM OLDER AGE CLASSES (1998)
    Oxford, UK : Blackwell Publishing Ltd
    Marine mammal science 14 (1998), S. 0 
    Details
    ISSN: 1748-7692
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1748-7692.1998.tb00729.x
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  • 3
    Electronic Resource
    Electronic Resource
    Two highly related regulatory proteins, Shigella flexneri VirF and enterotoxigenic Escherichia coli Rns, have common and distinct regulatory properties (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 162 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The Rns protein of enterotoxigenic Escherichia coli (ETEC) and the VirF protein of Shigella flexneri are members of the AraC family of transcription regulators. Rns is required for positive activation of the CS1 fimbrial genes, while VirF is a positive regulator of an invasion gene regulon. The amino acid sequences of the proteins are 36% identical, and both proteins activate transcription in response to increases in temperature. Here, we show that Rns is capable of complementing fully a null mutation in the S. flexneri virF gene. However, the VirF protein cannot replace Rns as an activator of CS1 gene expression in ETEC. This failure is not due to the absence from ETEC of a co-factor required by VirF since it also occurs when the CS1 system is moved into an S. flexneri genetic background. Nor is it a function of growth medium composition or a failure in virF gene expression. Instead, these findings point to important differences in the mechanisms by which these related transcription factors regulate gene expression in Gram-negative pathogens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13013.x
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  • 4
    Electronic Resource
    Electronic Resource
    Retention of neutralising activity by recombinant anti-pneumolysin antibody fragments (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 22 (1998), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The variable domains of a neutralising (prevents erythrocyte lysis) anti-pneumolysin monoclonal antibody have been cloned and expressed as functional protein in Escherichia coli. Purification of the anti-pneumolysin single-chain antibody fragment, via antibody-affinity or metal-chelate affinity chromatography, resulted in product that was predominantly in a dimeric or monomeric form, respectively. The dimeric single-chain antibody fragment showed a higher sensitivity and affinity for immobilised antigen in both ELISA and BIAcore studies. The dimeric single-chain antibody fragment was as effective at protecting erythrocytes from lysis as the parent monoclonal. The monomeric, low affinity single-chain antibody fragment, showed reduced neutralising potency. As antibiotic resistant Streptococcus pneumoniae strains continue to show an increasing word-wide distribution, recombinant, neutralising antibody fragments, may provide an additional class of molecules useful in the treatment of toxaemia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1998.tb01210.x
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