References of "Lakaye, Bernard"
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See detailMolecular Basis of Neuronal Biorhythms and Paroxysms
Grisar, Thierry ULg; Lakaye, Bernard ULg; Thomas, Elizabeth

in Archives of Physiology & Biochemistry (1996), 104(6), 770-4

The molecular basis of the biorhythms are evoked in relation to cerebral EEG rhythms and paroxysms. Basic oscillatory phenomena have been well shown and modeled in systems such as the glycolytic pathway ... [more ▼]

The molecular basis of the biorhythms are evoked in relation to cerebral EEG rhythms and paroxysms. Basic oscillatory phenomena have been well shown and modeled in systems such as the glycolytic pathway, the oscillations of cAMP in amoebas and rhythms of the intracellular cycline during mitosis. In excitable cells the intracellular calcium and cAMP oscillations exhibit a signalling system with many advantages. Thus the question arises: to what extent can the EEG paroxysms observed in epileptic syndrome be due to disturbances in such basic molecular pathways that underlie intracellular molecular oscillations? The usefulness of the absence-rat-model and the implication the T type Ca(2+)-channel of the thalamic nuclei in the pathophysiology of this epileptic syndrome are discussed. [less ▲]

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See detailSaturation of Penicillin-Binding Protein 1 by Beta-Lactam Antibiotics in Growing Cells of Bacillus Licheniformis
Lepage, Sylvie ULg; Lakaye, Bernard ULg; Galleni, Moreno ULg et al

in Molecular Microbiology (1995), 16(2), 365-72

With the help of a new highly sensitive method allowing the quantification of free penicillin-binding proteins (PBPs) and of an integrated mathematical model, the progressive saturation of PBP1 by various ... [more ▼]

With the help of a new highly sensitive method allowing the quantification of free penicillin-binding proteins (PBPs) and of an integrated mathematical model, the progressive saturation of PBP1 by various beta-lactam antibiotics in growing cells of Bacillus licheniformis was studied. Although the results confirmed PBP1 as a major lethal target for these compounds, they also underlined several weaknesses in our present understanding of this phenomenon. In growing cells, but not in resting cells, the penicillin target(s) appeared to be somewhat protected from the action of the inactivators. In vitro experiments indicated that amino acids, peptides and depsipeptides mimicking the peptide moiety of the nascent peptidoglycan significantly interfered with the acylation of PBP1 by the antibiotics. In addition, the level of PBP1 saturation at antibiotic concentrations corresponding to the minimum inhibitory concentrations was not constant, suggesting that additional, presently undiscovered, factors might be necessary to account for the experimental observations. [less ▲]

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See detailKinetic properties of the Bacillus licheniformis Penicillin-binding proteins
Lepage, Sophie; Galleni, Moreno ULg; Lakaye, Bernard ULg et al

in Biochemical Journal (1995), 309

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See detailSerine-Type D-Ala-D-Ala Peptidases and Penicillin-Binding Proteins
Granier, Benoît; Jamin, Marc; Adam, Maggy et al

in Methods in Enzymology (1994), 244

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See detailSynthesis, purification and kinetic properties of fluorescein-labelled penicillins
Lakaye, Bernard ULg; Damblon, Christian ULg; Jamin, Marc et al

in Biochemical Journal (1994), 300

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See detailA New, Highly Sensitive Method for the Detection and Quantification of Penicillin-Binding Proteins
Galleni, Moreno ULg; Lakaye, Bernard ULg; Lepage, Sophie et al

in Biochemical Journal (1993), 291((Pt 1)), 19-21

A new method for the identification and quantification of penicillin-binding proteins is described which uses fluorescein-coupled penicillins. It allows the rapid detection of 0.2 pmol with the naked eye ... [more ▼]

A new method for the identification and quantification of penicillin-binding proteins is described which uses fluorescein-coupled penicillins. It allows the rapid detection of 0.2 pmol with the naked eye and 2 fmol with the help of an A.L.F. automatic DNA sequencer. Direct labelling can also be performed on whole bacterial cells. [less ▲]

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See detailCloning, Nucleotide Sequence and Amplified Expression of the Gene Encoding the Extracellular Metallo (Zn) Dd-Peptidase of Streptomyces Albus G
Duez, Colette ULg; Lakaye, Bernard ULg; Houba, Simone et al

in FEMS Microbiology Letters (1990), 71(1-2), 215-219

The gene encoding the extracellular metallo (Zn) DD-peptidase of Streptomyces albus G has been cloned in Escherichia coli DH5 alpha MCR via pBR322 or 325, and then transferred into Streptomyces lividans ... [more ▼]

The gene encoding the extracellular metallo (Zn) DD-peptidase of Streptomyces albus G has been cloned in Escherichia coli DH5 alpha MCR via pBR322 or 325, and then transferred into Streptomyces lividans TK24 via pIJ486, with substantial amplification of the expressed DD-peptidase. The gene has the information for the synthesis of a 255 amino acid precursor, the amino terminal region of which has the characteristic features of a signal peptide. The primary structure as deduced from nucleotide sequencing confirms that previously determined by chemical methods except for the occurrence of an Asp instead of Asn at position 1 and an additional Ala immediately downstream of Pro67. [less ▲]

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