Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Jacques Coyette"'
Autor:
Séverine Hallut, Noureddine Rhazi, André Piette, Colette Duez, Fabrice Bouillenne, Ana Amoroso, Jacques Coyette, Séverine Hubert
Publikováno v:
Journal of Bacteriology. 186:4412-4416
A soluble derivative of the Enterococcus faecalis JH2-2 class A PBP1 ( * PBP1) was overproduced and purified. It exhibited a glycosyltransferase activity on the Escherichia coli 14 C-labeled lipid II precursor. As a dd- peptidase, it could hydrolyze
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::504cac990ae1a4e7bb37f3ff0c253746
https://doi.org/10.1128/jb.186.13.4412-4416.2004
https://doi.org/10.1128/jb.186.13.4412-4416.2004
Autor:
Lynn E. Hancock, Jacques Coyette
Walls of the enterococci may represent 27 to 38% of the dry cell weight (exponential and stationary phase cells, respectively). Three main constituents are generally reported: peptidoglycan (PG), teichoic acid, and polysaccharide. Sometimes, proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30de189874b3a211dba97b27be6bb890
https://doi.org/10.1128/9781555817923.ch5
https://doi.org/10.1128/9781555817923.ch5
Autor:
Willy Zorzi, Ana Maria Amoroso, Iris Thamm, Frédéric Sapunaric, Jacques Coyette, Colette Duez
Publikováno v:
Microbiology. 147:2561-2569
A penicillin-resistant mutant, JH2-2r (MIC 75 μg ml−1), was isolated from Enterococcus faecalis JH2-2 (MIC 5 μg ml−1) by successive passages on plates containing increasing concentrations of benzylpenicillin. A comparison of the penicillin-bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd0c03afeafe4d3a688ae525f3e832dc
https://doi.org/10.1099/00221287-147-9-2561
https://doi.org/10.1099/00221287-147-9-2561
Publikováno v:
Journal of Chemical Technology & Biotechnology. 70:45-50
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8a1754fc5f4317a38fce6f7fc63c0343
https://doi.org/10.1002/(sici)1097-4660(199709)70:1<45::aid-jctb737>3.0.co
https://doi.org/10.1002/(sici)1097-4660(199709)70:1<45::aid-jctb737>3.0.co
Publikováno v:
Molecular Microbiology. 57:871-873
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6418b5bb07b727876ee1f8778190b3e5
https://doi.org/10.1111/j.1365-2958.2005.04715.x
https://doi.org/10.1111/j.1365-2958.2005.04715.x
Publikováno v:
The Biochemist. 27:46-48
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cea94cee369e4d287acbf4bd130c89b7
https://doi.org/10.1042/bio02702046
https://doi.org/10.1042/bio02702046
Autor:
Oliver Verlaine, Xavier Henry, Ana Maria Amoroso, Jacques Coyette, Jean-Marie Frère, Bernard Joris
Publikováno v:
Antimicrobial agents and chemotherapy. 57(12)
The opportunistic human pathogen Enterococcus faecium overproduces the low-affinity PBP5. In clinical strains, mutations in PBP5 further reduce its acylation rate by β-lactams. Previous studies have reported that ceftaroline had poor inhibitory acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15f19e4dba15a32786a0b2011c4ced20
https://pubmed.ncbi.nlm.nih.gov/24060866
https://pubmed.ncbi.nlm.nih.gov/24060866
Autor:
Jacques Coyette, J. Pierre, D. Raze, Xiang Yang Zhou, Olivier Dardenne, L. Gutmann, J. Lamotte, Willy Zorzi
Publikováno v:
Journal of Bacteriology. 178:4948-4957
Among its penicillin-binding proteins (PBPs), Enterococcus faecium possesses a low-affinity PBP5, PBP5fm, which is the main target involved in beta-lactam resistance. A 7.7-kb EcoRI chromosomal fragment of E. faecium D63r containing the pbp5fm gene w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e743013ff86816cc6c86c13b9bc2c36
https://doi.org/10.1128/jb.178.16.4948-4957.1996
https://doi.org/10.1128/jb.178.16.4948-4957.1996
Autor:
Antonio Gálvez, Manuel Martínez-Bueno, Jacques Coyette, Mercedes Maqueda, Eva Valdivia, B Samyn, J. Van Beeumen
Publikováno v:
Journal of Bacteriology. 176:6334-6339
The structural gene of the enterococcal peptide antibiotic AS-48 (as-48) has been identified and cloned by using two degenerate 17-mer DNA oligonucleotides on the basis of the amino acid sequences of two peptides obtained by digestion of the antibiot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6a84c77ad9f6dda1e641c29e903bc3b
https://doi.org/10.1128/jb.176.20.6334-6339.1994
https://doi.org/10.1128/jb.176.20.6334-6339.1994
Autor:
Mercedes Maqueda, Bart Devreese, Eva Valdivia, Manuel Martínez-Bueno, Bart Samyn, Jacques Coyette, Antonio Gálvez, Jozef Van Beeumen
Publikováno v:
FEBS Letters. 352:87-90
The complete primary structure of the peptide antibiotic AS-48 produced by Enterococcus faecalis has been determined by chemical degradation analysis. The cyclic nature of this 70 residues containing peptide was demonstrated by plasma desorption mass
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01798068aa9d67ccb67497085916498a
https://doi.org/10.1016/0014-5793(94)00925-2
https://doi.org/10.1016/0014-5793(94)00925-2