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  • 1995-1999  (6)
  • Bayesian inference  (2)
  • Ethylene  (2)
  • endothelial cells  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    International journal of legal medicine 110 (1997), S. 244-250 
    ISSN: 1437-1596
    Keywords: Key words DNA profiling ; Forensic identification ; Bayesian inference ; Likelihood ratio ; Coancestry ; coefficient ; Probability ; Statistics ; PCR ; STR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Law
    Notes: Abstract A previous paper in this journal has described the conventional statistical analysis of three databases (Caucasian, Afro-Caribbean and Asians from the Indian subcontinent) where individuals are typed at six short tandem repeat (STR) loci. This paper presents a Bayesian analysis of the same data and the approach is centred on the concept of estimating coancestry coefficients from mixed databases. Posterior distributions for the three databases are presented and discussed and the consequences of implementing bootstrap estimation procedures are also shown.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Key words:Arabidopsis (GTP binding) ; Cytokinin ; Ethylene ; Protein Phosphorylation ; GTP-binding proteins (small)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Binding of [α-32P]guanosine 5′-triphosphate ([α-32P]GTP) has been demonstrated in a Triton X-100-solubilised membrane fraction from leaves of Arabidopsis thaliana (L.) Heynh. Binding was stimulated by 1 h pre-treatment of leaves with ethylene and this effect was antagonised by the inclusion of N6-benzyladenine in the medium used for homogenisation. The ethylene-insensitive mutants eti5 and etr showed contrasting responses. In eti5 the constitutive level of GTP binding was higher than in the wild type whereas in etr the level was much lower. Neither ethylene nor cytokinin affected GTP binding in the mutants. The GTP-binding activity was localised in two bands at 22 and 25 kDa, both of which were immunoprecipitated by anti-pan-Ras antibodies, indicating that the activity is due to small GTP-binding proteins. In a similar membrane fraction, ethylene was shown to increase protein phosphorylation and benzyladenine antagonised this effect. In eti5 the constitutive level of protein phosphorylation was higher than in the wild type, but benzyladenine increased activity substantially while ethylene was without effect. In etr, protein phosphorylation was lower than in the wild type, ethylene was without effect, but cytokinin increased activity. A protein of Mr 17 kDa was detected on gels using antibodies to nucleoside diphosphate kinase. Phosphorylation of this protein was upregulated by ethylene but nucleoside diphosphate kinase activity was unaffected. The results are compared with the effect of the two hormones on the senescence of detached leaves and discussed in relation to pathways proposed for ethylene signal transduction.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2048
    Keywords: Ethylene ; Guanosine ; 5′-triphosphate binding ; Guanosine 5′-triphosphate-binding proteins (small) ; Membrane (GTP binding) ; Pisum ; Signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Binding of [35S]guanosine 5′-o-(3-thiotriphosphate) (GTPγS) and of [α-32P]guanosine triphosphate ([α-32P]GTP) has been demonstrated in membrane preparations from epicotyl tips of etiolated plants ofPisum sativum L.; binding has also been shown in KCl-and Triton X-100-solubilised fractions from these membranes. Binding of GTPγS was of high affinity (K D = 3.17 × 10−8M), showed high specificity for guanine nucleotides and was stimulated by Mg2+ in the micromolar range. Binding was associated with only low levels of guanosine 5′-triphosphatase activity and was unaffected by treatment with mastoparan. In-vivo application of ethylene at 1 μl·l−1 stimulated GTP binding in fractions released from membranes by treatment with 750 mM KCl and Triton X-100. Affinity probing with ([α-32P]GTP) showed pronounced specific GTP binding to polypeptide(s) with relative molecular mass (Mr) of 28 kDa. The binding was stimulated markedly by ethylene and to some extent by AIF4 −. Mouse monoclonal anti-pan-ras antibodies cross-reacted with several polypeptides in the 20 to 30-kDa region, and an [α-32P]GTP-labelled protein of Mr 28 kDa was precipitated by the same antibodies. The data indicate that the transduction of the ethylene signal may involve the intervention of GTP-binding proteins similar to the small monomeric GTP-binding proteins.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Statistics and computing 6 (1996), S. 277-287 
    ISSN: 1573-1375
    Keywords: Bayesian inference ; contingency tables ; Gibbs sampling ; graphical methods ; hypothesis testing ; independence ; intraclass tables ; model comparison ; predictive densities ; quasisymmetry ; simulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Computer Science , Mathematics
    Notes: Abstract In this paper we present a simulation and graphics-based model checking and model comparison methodology for the Bayesian analysis of contingency tables. We illustrate the approach by testing the hypotheses of independence and symmetry on complete and incomplete simulated tables.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 349-352 
    ISSN: 1573-3904
    Keywords: calcium ; endothelial cells ; metalloendopeptidase EC 3.4.24.16 ; secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The two closely related soluble zinc metalloendopeptidases EC 3.4.24.15 (EP24.15) and EC 3.4.24.16 (EP24.16) readily hydrolyze the vasocative peptide bradykinin in vitro, and therefore may play a role in cardiovascular regulation. Although primarily soluble cytosolic enzymes, both secreted and membrane-associated forms of both peptidases have been reported. However, these enzymes have neither a transmembrane domain nor a signal sequence; thus, the mechanisms of membrane anchoring and secretion are unknown. In the present study, secreted/released EP24.15 and EP24.16 activity from aortic endothelial cells in culture was assessed by the cleavage of a specific quenched fluorescent substrate. An increase in enzyme activity released from endothelial cells, which express both peptidases, was seen following incubation with calcium-free media. In the AtT-20 endocrine cell (mouse pituitary corticotrope), which predominantly expresses EP24.15, the release of activity into media was unaffected by calcium removal. The release of enzyme activity from endothelial cells was inversely proportional to calcium concentrations ranging between 0.01 mM (activity equivalent to calcium-free media) and 0.5 mM (activity equivalent to normal media). Cleavage of the EP24.16-specific substrate AcNT8–13 indicated that the increase in enzyme activity released upon incubation with calcium-free medium was due at least in part to the release of EP24.16. These results suggest that EP24.15 and EP24.16 are secreted from endothelial cells, and that removal of calcium selectively enhances the release of EP24.16 by an as yet unknown mechanism.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 349-352 
    ISSN: 1573-3904
    Keywords: calcium ; endothelial cells ; metalloendopeptidase EC 3.4.24.16 ; secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The two closely related soluble zinc metalloendopeptidases EC 3.4.24.15 (EP24.15) and EC 3.4.24.16 (EP24.16) readily hydrolyze the vasoactive peptide bradykinin in vitro, and therefore may play a role in cardiovascular regulation. Although primarily soluble cytosolic enzymes, both secreted and membrane-associated forms of both peptidases have been reported. However, these enzymes have neither a transmembrane domain nor a signal sequence; thus, the mechanisms of membrane anchoring and secretion are unknown. In the present study, secreted/released EP24.15 and EP24.16 activity from aortic endothelial cells in culture was assessed by the cleavage of a specific quenched fluorescent substrate. An increase in enzyme activity released from endothelial cells, which express both peptidases, was seen following incubation with calcium-free media. In the AtT-20 endocrine cell (mouse pituitary corticotrope), which predominantly expresses EP24.15, the release of activity into media was unaffected by calcium removal. The release of enzyme activity from endothelial cells was inversely proportional to calcium concentrations ranging between 0.01 mM (activity equivalent to calcium-free media) and 0.5 mM (activity equivalent to normal media). Cleavage of the EP24.16-specific substrate AcNT8-13 indicated that the increase in enzyme activity released upon incubation with calcium-free medium was due at least in part to the release of EP24.16. These results suggest that EP24.15 and EP24.16 are secreted from endothelial cells, and that removal of calcium selectively enhances the release of EP24.16 by an as yet unknown mechanism.
    Type of Medium: Electronic Resource
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