Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Sophie Lepage"'
Autor:
W. Allen Howard, Joseph S. Warmus, Haile Tecle, Smith Yvonne Dorothy, Wilbur R. Leopold, Stephen Douglas Barrett, James H. Fergus, Amy M. Delaney, Dan Marston, Alan R. Saltiel, Alexander James Bridges, Sophie LePage, Annette M. Doherty, Cathlin Marie Flamme, Sally Przybranowski, Judith Sebolt-Leopold, Robert M. Kennedy, Keri Van Becelaere, David T. Dudley, Michael Kaufman
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 18:6501-6504
A novel series of benzhydroxamate esters derived from their precursor anthranilic acids have been prepared and have been identified as potent MEK inhibitors. 2-(2-Chloro-4-iodo-phenylamino)-N-cyclopropylmethoxy-3,4-difluoro-benzamide, CI-1040, was th
Autor:
Bernard Joris, Jean-Marie Frère, Benoit Granier, Christine Franssen, Alain Brans, Valérie Duval, Sophie Lepage, Marc Swinnen
Publikováno v:
Molecular Microbiology. 48:1553-1564
SummaryTo study the properties of the BlaR penicillinreceptor involved in the induction of the Bacillus licheniformis βlactamase, the watersoluble carboxy terminal domain of the protein (BlaRCTD) was overproduced in the periplasm of Escheric
Publikováno v:
Molecular Microbiology. 31:89-101
Summary By challenging the efficiency of some of our most useful antimicrobial weapons, bacterial antibiotic resistance is becoming an increasingly worrying clinical problem. A good antibiotic is expected to exhibit a high affinity for its target and
Autor:
Guo-Hua Zhao, Christine Forceille, Jean-Marie Frère, Daniel Klein, Sophie Lepage, Colette Duez, Jean-Marie Ghuysen, Noureddine Rhazi
Publikováno v:
Biochemical Journal. 327:377-381
The role of various residues in the conserved structural elements of the Actinomadura R39 penicillin-sensitive DD-peptidase has been studied by site-directed mutagenesis. Replacement of Ser-298 of the ‘SDN loop’ by Ala or Gly significantly decrea
Autor:
B. Granier, Jean-Marie Frère, Colette Duez, J. Van Beeumen, Jean Dusart, Sophie Lepage, J M Ghuysen, Otto Dideberg, Serge Englebert
Publikováno v:
Biochemical Journal. 282:781-788
As derived from gene cloning and sequencing, the 489-amino-acid DD-peptidase/penicillin-binding protein (PBP) produced by Actinomadura R39 has a primary structure very similar to that of the Escherichia coli PBP4 [Mottl, Terpstra & Keck (1991) FEMS M
Autor:
Valérie, Duval, Marc, Swinnen, Sophie, Lepage, Alain, Brans, Benoît, Granier, Christine, Franssen, Jean-Marie, Frère, Bernard, Joris
Publikováno v:
Molecular microbiology. 48(6)
To study the properties of the BlaR penicillin-receptor involved in the induction of the Bacillus licheniformisbeta-lactamase, the water-soluble carboxy terminal domain of the protein (BlaR-CTD) was overproduced in the periplasm of Escherichia coli J
Autor:
Sophie Lepage, Marc Jamin, Jean-Marie Frère, Moreno Galleni, Iris Thamm, Bernard Lakaye, Bernard Joris
Publikováno v:
Biochemical Journal. 291:19-21
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 and 2 fmol with the help of an A.L.F. automati
Autor:
Karin Hardt, Bernard Joris, Sophie Lepage, Anthony L. Fink, Robert Brasseur, J. Olivier Lampen, Jean-Marie Frère, Jean-Marie Ghuysen
Publikováno v:
Molecular microbiology. 23(5)
Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in Bacillus licheniformis, is embedded in the plas
In the analysis of the interactions between beta-lactam antibiotics and their target enzymes, it is often difficult to estimate the kinetic properties of the molecules which react rapidly with their targets and in consequence behave as the most effic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4044a6d82762d48bb896f00cf1bd06f
https://europepmc.org/articles/PMC1135798/
https://europepmc.org/articles/PMC1135798/
Autor:
Sophie Lepage, Jean-Marie Frère, Michel Crine, Iris Thamm, Sylvie Groslambert, Moreno Galleni, Bernard Lakaye
Publikováno v:
Molecular microbiology. 16(2)
Summary 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 β-lactam antibiotics in growing cell