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See detailClonal diversity and metallo-beta-lactamase production in clinical isolates of Stenotrophomonas maltophilia
Mercuri, Paola ULg; Ishii, Y.; Ma, L. et al

in Microbial Drug Resistance : Mechanism, Epidemiology, & Disease (2002), 8(3), 193-200

Stenotrophomonas maltophilia is a nosocomial pathogen with an intrinsic broad-spectrum resistance to beta-lactam compounds and other antibacterial agents. It produces two chromosomal beta-lactamases: a ... [more ▼]

Stenotrophomonas maltophilia is a nosocomial pathogen with an intrinsic broad-spectrum resistance to beta-lactam compounds and other antibacterial agents. It produces two chromosomal beta-lactamases: a clavulanic acid-sensitive class A (L2) and a tetrameric carbapenemase (L1 or BlaS). We screened 40 S. maltophilia multidrug-resistant clinical isolates recovered between 1995 and 1998 in the Varese Hospital (Italy) for the presence of the metallo-beta-lactamase. The isolates were investigated by phenotypic profiling (enzymatic activity and antibiotic resistance pattern) and molecular methods such as PCR and pulsed-field gel electrophoresis (PFGE) to reveal intraspecies diversity. For the tested S. maltophilia strains, we showed that the beta-lactamase production could be induced by the presence of imipenem (50 mug/ml) in the culture media. Addition of 1 mM dipicolinic acid completely inhibited the hydrolysis of imipenem but decreased that nitrocefin in a strain-dependent manner. Full activity of crude extract towards imipenem could be restored by addition of 1 mM ZnCl2. Finally, the gene encoding the carbapenem-hydrolyzing beta-lactamase from S. maltophilia ULA-511 and 39/95, a clinical strain, were isolated and sequenced. These two strains have a different profile of multidrug resistance. The two metallo-beta-lactamases were found to be isologous. The difference of sensitivity of these two strains was associated to the level of production of the metallo-beta-lactamase. [less ▲]

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See detailCloned Human Polyomavirus JC Can Transform Human Amnion Cells
Howley, P. M.; Rentier-Delrue, Françoise ULg; Heilman, C. A. et al

in Journal of Virology (1980), 36

The genome of the human polyomavirus JC (Mad-1 strain) was molecularly cloned in Escherichia coli by using the plasmid vector pBR322. Recombinant DNA molecules were constructed with the entire JC genome ... [more ▼]

The genome of the human polyomavirus JC (Mad-1 strain) was molecularly cloned in Escherichia coli by using the plasmid vector pBR322. Recombinant DNA molecules were constructed with the entire JC genome inserted either at its unique EcoRI site at 0.0 map units or at its unique BamHI site at 0.51 map units. Viral DNA from each of these recombinant plasmids was capable of transforming human amnion cells, and cell lines established from transformed foci were positive for JC tumor antigen as assayed by indirect immunofluorescence. [less ▲]

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See detailThe Clones’ Apprenticeship: Ishiguro’s Never Let Me Go as a Bildungsroman
Guesse, Carole ULg

in Anglica : An International Journal of English Studies (2016), 25(1), 155-169

This article considers as a Bildungsroman the 2005 novel Never Let Me Go by Kazuo Ishiguro, which depicts the education of young clones in a boarding school in a 1990s uchronic England. It studies the ... [more ▼]

This article considers as a Bildungsroman the 2005 novel Never Let Me Go by Kazuo Ishiguro, which depicts the education of young clones in a boarding school in a 1990s uchronic England. It studies the main theoretical works about this type of writing in order to isolate some of its defining characteristics and then evaluate the possibility of an analogy between the fictional developments of humans and clones. It concludes that, even though the Bildunsgroman has strong ties with the changing nineteenth-century society, it has been adapted to other – even non-existing – environments. [less ▲]

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See detailClonidine and ketanserin both are effective treatment for postanesthetic shivering.
Joris, Jean ULg; Banache, Maryse; Bonnet, Francis et al

in Anesthesiology (1993), 79(3), 532-9

BACKGROUND: Although meperidine is an effective treatment of postanesthetic shivering, its mechanism of action remains unknown. Investigation of other drugs might help clarify the mechanisms by which ... [more ▼]

BACKGROUND: Although meperidine is an effective treatment of postanesthetic shivering, its mechanism of action remains unknown. Investigation of other drugs might help clarify the mechanisms by which shivering can be controlled. Accordingly, we investigated the efficacy of clonidine, an alpha 2-adrenergic agonist, and ketanserin, a 5-hydroxytryptamine antagonist, in treating postanesthetic shivering. METHODS: First, 54 patients shivering after general anesthesia were allocated randomly to receive an intravenous bolus of saline, 150 micrograms clonidine, or 10 mg ketanserin. A second study explored the dose-dependence of clonidine. Forty shivering patients were given saline or clonidine, 37.5, 75, or 150 micrograms. RESULTS: The duration of shivering was significantly shorter in those given clonidine (2.1 +/- 0.9 min) than in the other two groups and shorter in the ketanserin group (4.3 +/- 0.9 min) than in the saline group (12.0 +/- 1.6 min). Clonidine and ketanserin significantly decreased systolic arterial blood pressure when compared to saline. Core rewarming was significantly slower in the clonidine group. In the second study, 37.5 micrograms clonidine was no more effective than saline. Two minutes after treatment, 150 micrograms obliterated shivering in all patients. Five minutes after treatment, all patients given 75 micrograms had stopped shivering. Systolic arterial pressure and heart rate decreased significantly in patients given 75 and 150 micrograms clonidine. CONCLUSIONS: Clonidine (150 micrograms) and ketanserin (10 mg) both are effective treatment for postanesthetic shivering. The effect of clonidine on shivering is dose-dependent: whereas 37.5 micrograms had no effect, 75 micrograms clonidine stopped shivering within 5 min. [less ▲]

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See detailClonidine test and MMPI scales in major depression
Hansenne, Michel ULg; PITCHOT, William ULg; Gonzalez, Moreno et al

in European Psychiatry (1992), 7

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See detailThe clonidine test in posttraumatic stress disorder.
Hansenne, Michel ULg; Pitchot, William ULg; Ansseau, Marc ULg

in American Journal of Psychiatry (The) (1991), 148(6), 810-1

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See detailCloning and amplified expression in Streptomyces lividans of a gene encoding extracellular β-lactamase from Streptomyces albus G
Dehottay, Philippe; Dusart, Jean; Duez, Colette ULg et al

in Gene (1986), 42(1), 31-36

A 4.9-kb DNA fragment containing the bla gene for the extracellular beta-lactamase (BLA) of Streptomyces albus G was cloned in Streptomyces lividans using the conjugative, low-copy-number plasmid pIJ61 as ... [more ▼]

A 4.9-kb DNA fragment containing the bla gene for the extracellular beta-lactamase (BLA) of Streptomyces albus G was cloned in Streptomyces lividans using the conjugative, low-copy-number plasmid pIJ61 as vector. No expression of bla was observed when this DNA fragment was introduced into Escherichia coli HB101 on a plasmid vector. A 1.5-kb PstI-SstI fragment containing the bla gene was cloned in S. lividans on the nonconjugative, high-copy-number plasmid pIJ702. A tenfold higher yield of BLA was obtained from S. lividans carrying this plasmid than from S. albus G grown under optimal production conditions. The BLA from the clone reacts with beta-iodopenicillanate according to a branched pathway which is characteristic of the original S. albus G BLA enzyme. [less ▲]

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See detailCloning and amplified expression in Streptomyces lividans of the gene encoding the extracellular β-lactamase from Streptomyces cacaoi
Lenzini, Mauro V; Nojima, Shiego; Dusart, Jean et al

in Journal of General Microbiology (1987), 133(10), 2915-2920

A 19 kb SphI DNA fragment containing the gene for the extracellular active-site serine beta-lactamase of Streptomyces cacaoi KCC-SO352 was cloned in Streptomyces lividans TK24 using the high-copy-number ... [more ▼]

A 19 kb SphI DNA fragment containing the gene for the extracellular active-site serine beta-lactamase of Streptomyces cacaoi KCC-SO352 was cloned in Streptomyces lividans TK24 using the high-copy-number plasmid pIJ702 as vector. A 30-fold higher yield of beta-lactamase was obtained from S. lividans strain ML1, carrying the recombinant plasmid pDML51, than from S. cacaoi grown under optimal production conditions. In all respects (molecular mass, isoelectric point, kinetics of inhibition by beta-iodopenicillanate) the overproduced S. lividans ML1 beta-lactamase was identical to the original S. cacaoi enzyme. A considerable reduction of beta-lactamase production was caused by elimination of a 12.8 kb portion of the 19 kb DNA fragment by cleavage at an internal SphI site located more than 3 kb upstream of the beta-lactamase structural gene. The beta-lactamase gene was located within a 1.8 NcoI-BclI fragment but when this fragment was cloned in S. lividans pIJ702, the resulting strain produced hardly any more beta-lactamase than the original S. cacaoi. [less ▲]

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See detailCloning and amplified expression in Streptomyces lividans of the gene encoding the extracellular β-lactamase of Actinomadura R39
Fraipont, Claudine ULg; Duez, Colette ULg; Matagne, André ULg et al

in Biochemical Journal (1989), 262(3), 849-854

By using the promoter-probe plasmid pIJ424, genomic DNA fragments of Actinomadura R39 were shown to have promoter activity in Streptomyces lividans. The same 100-200-copy-number plasmid was used to clone ... [more ▼]

By using the promoter-probe plasmid pIJ424, genomic DNA fragments of Actinomadura R39 were shown to have promoter activity in Streptomyces lividans. The same 100-200-copy-number plasmid was used to clone in S. lividans TK24, the gene that encodes the Actinomadura R39, β-lactamase. Gene cloning resulted in an amplified expression of the , β lactamase when compared with the amounts of enzyme produced by the original strain (1 mg versus 0.008 mg . litre of culture-1). [less ▲]

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See detailCloning and characterisation of the primary structure of the sheep lymphocyte function-associated antigen-1 alpha subunit
Fett, Thomas ULg; Zecchinon, Laurent ULg; Baise, Etienne ULg et al

in Molecular Immunology (2005), 42(12), 1503-1508

The leukocyte integrins play a critical role in a number of cellular adhesive interactions during the immune response. The ovine cDNA encoding CD1 1a, the predominant a subunit of the beta(2)-integrin ... [more ▼]

The leukocyte integrins play a critical role in a number of cellular adhesive interactions during the immune response. The ovine cDNA encoding CD1 1a, the predominant a subunit of the beta(2)-integrin family, was sequenced and compared with the human, bovine and murine sequences. Despite some focal differences, it shares all the main characteristics of its known mammalian homologues. Along with the ovine CD18-encoding cDNA, which is available for a few months, the sequence data provided here will allow the Ovis aries beta(2)-integrin CD1 1a/CD18 (LEA-1, alpha(L)beta 2) expression in vitro as a tool to examine the specificities of inflammation in the ovine species. (c) 2005 Elsevier Ltd. All rights reserved. [less ▲]

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See detailCloning and characterization of a cDNA encoding the beta-subunit of the bovine insulin-like growth factor-1 receptor.
Sneyers, M.; Kettmann, Richard ULg; Massart, Serge et al

in DNA Sequence : The Journal of DNA Sequencing & Mapping (1991), 1(6),

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See detailCloning and characterization of a cDNA encoding the bovine insulin-like growth factor binding protein 1 (bIGFBP-1).
Sneyers, M.; Kettmann, Richard ULg; Massart, Serge et al

in DNA Sequence : The Journal of DNA Sequencing & Mapping (1991), 1(6),

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See detailCloning and characterization of a cDNA encoding the bovine insulin-like growth factor binding protein I (bIGF-I)
Sneyers, Myriam; Kettmann, Richard ULg; Massart, Serge et al

in III Inter Symp on Molecular and Cell Biol of Insulin and IGF's (1990)

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See detailCloning and characterization of a cDNA encoding the ß-subunit of the bovine insulin-like growth factor-I receptor.
Sneyers, Myriam; Kettmann, Richard ULg; Massart, Serge et al

Poster (1991)

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See detailCloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3.
Colige, Alain ULg; Vandenberghe, Isabel; Thiry, Marc ULg et al

in Journal of Biological Chemistry (2002), 277(8), 5756-66

The processing of amino- and carboxyl-propeptides of fibrillar collagens is required to generate collagen monomers that correctly assemble into fibrils. Mutations in the ADAMTS2 gene, the ... [more ▼]

The processing of amino- and carboxyl-propeptides of fibrillar collagens is required to generate collagen monomers that correctly assemble into fibrils. Mutations in the ADAMTS2 gene, the aminopropeptidase of procollagen I and II, result in the accumulation of non-fully processed type I procollagen, causing human Ehlers-Danlos syndrome type VIIC and animal dermatosparaxis. In this study, we show that the aminopropeptide of type I procollagen can be cleaved in vivo in absence of ADAMTS-2 activity and that this processing is performed at the cleavage site for ADAMTS-2. In an attempt to identify the enzyme responsible for this alternative aminoprocollagen peptidase activity, we have cloned the cDNA and determined the primary structure of human and mouse ADAMTS-14, a novel ADAMTS displaying striking homologies with ADAMTS-2 and -3. The structure of the human gene, which maps to 10q21.3, and the mechanisms of generation of the various transcripts are described. The existence of two sites of initiation of transcription, in two different promoter contexts, suggests that transcripts resulting from these two sites can be differently regulated. The tissue distribution of ADAMTS-14, the regulation of the gene expression by various cytokines and the activity of the recombinant enzyme are evaluated. The potential function of ADAMTS-14 as a physiological aminoprocollagen peptidase in vivo is discussed. [less ▲]

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See detailCloning and characterization of G protein-coupled receptors
Parmentier, M.; Libert, F.; Perret, J. et al

in Advances in Second Messenger and Phosphoprotein Research (1993), 28

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See detailCloning And Characterization Of Mn, A Human Tumor-Associated Protein With A Domain Homologous To Carbonic-Anhydrase And A Putative Helix-Loop-Helix Dna-Binding Segment
Pastorek, J.; Pastorekova, S.; Callebaut, I. et al

in Oncogene (1994), 9(10),

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See detailCloning and characterization of rainbow trout interleukin-17A/F2 (IL-17A/F2) and IL-17 receptor A: expression during infection and bioactivity of recombinant IL-17A/F2.
Mira Monte, Milena ULg; Wang, Tiehui; Holland, Jason W. et al

in Infection and Immunity (2013), 81(1), 340-53

Lower vertebrates have been found to possess genes that have similar homology to both interleukin (IL)-17A and IL-17F, which have been termed IL-17A/F. In fish species, several of these genes can be ... [more ▼]

Lower vertebrates have been found to possess genes that have similar homology to both interleukin (IL)-17A and IL-17F, which have been termed IL-17A/F. In fish species, several of these genes can be present, but, to date, very little is known about their functional activity. This article describes the discovery and sequence analysis of a rainbow trout (Oncorhynchus mykiss) IL-17A/F2 molecule and an IL-17RA receptor. In addition, the bioactivity of the trout IL-17A/F2 is investigated for the first time in any species. The predicted IL-17A/F2 and IL-17RA proteins consist of 146 and 966 amino acids (aa), respectively, with both molecules containing conserved family motifs. Expression analysis revealed high constitutive expression of trout IL-17A/F2 in mucosal tissues from healthy fish, suggesting a potential role in mucosal immunity. When the modulation of IL-17A/F2 and IL-17RA in vitro was analyzed, it was observed that the two molecules were similarly affected. The expression of IL-17A/F2 was also induced in head kidney during bacterial, parasitic, and viral infections, revealing a possible function in defense against such pathogens. However, downregulation of IL-17RA was seen in some tissues and infections. The recombinant IL-17A/F2 protein was produced in Escherichia coli and was found to affect the expression of an antimicrobial peptide and the proinflammatory cytokines IL-6 and IL-8 in splenocytes. Consistent with mammalian IL-17 homologues, our expression and bioactivity results imply that trout IL-17A/F2 plays an important role in promoting inflammatory and host innate immune responses directed against different pathogen groups. [less ▲]

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See detailCloning and distribution of steroid receptor coactivator SRC-1 in quail.
Charlier, Thierry ULg; Lakaye, Bernard ULg; Ball, Gregory F. et al

Poster (2001)

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