Zobrazeno 1 - 10
of 133
pro vyhledávání: '"J, Coyette"'
Autor:
J. Dumas, D Prevost, B. Schoot, P. Stefanic, Y Taburet, J P Marquette, Raphaël Herman, Eric Sauvage, Frédéric Kerff, E. Fonze, Paulette Charlier, G. Leonard, J. Coyette
Publikováno v:
Cellular and Molecular Life Sciences (CMLS). 59:1223-1232
Penicillin-binding proteins (PBPs) are membrane proteins involved in the final stages of peptidoglycan synthesis and represent the targets of beta-lactam antibiotics. Enterococci are naturally resistant to these antibiotics because they produce a PBP
Autor:
J. Coyette, R. Hakenbeck
Publikováno v:
Cellular and Molecular Life Sciences CMLS. 54:332-340
Low-affinity penicillin-binding proteins (PBPs), which participate in the beta-lactam resistance of several pathogenic bacteria, have different origins. Natural transformation and recombination events with DNA acquired from neighbouring intrinsically
Publikováno v:
DNA sequence : the journal of DNA sequencing and mapping. 9(3)
A chromosomal 10355-bp segment of Enterococcus hirae S185 contains nine orfs which occur in the same order as the MraW-, FtsL-, PBP3-, MraY-, MurD-, MurG-, FtsQ-, FtsA- and FtsZ-encoding genes of the division and cell wall clusters of Escherichia col
Autor:
J. L. Arpigny, J. Coyette, S. Davail, G. Feller, E. Fonzé, E. C. Foulkes, J.-M. Frère, R. Fujii, S. Génicot, Ch. Gerday, B. Joris, J. Lamotte-Brasseur, J. N. Maina, E. Narinx, M. Nguyen-Disteche, N. Oshima, A. Viarengo, Z. Zekhnini
Publikováno v:
Advances in Comparative and Environmental Physiology ISBN: 9783642786006
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5baa1f1f4df2673c1bdba38c8084b51d
https://doi.org/10.1007/978-3-642-78598-6
https://doi.org/10.1007/978-3-642-78598-6
Publikováno v:
Advances in Comparative and Environmental Physiology ISBN: 9783642758997
The chance discovery by Fleming in 1928 of a metabolite produced by Penicillium notatum which exhibited bacteriolytic properties was followed by the heroic efforts of the Oxford group of Chain and Florey to isolate and identify the active molecule. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e7bc01aa3b8cfc47fa9ea474bcd1855
https://doi.org/10.1007/978-3-642-78598-6_5
https://doi.org/10.1007/978-3-642-78598-6_5
Publikováno v:
The Chemistry of β-Lactams ISBN: 9789401053006
The introduction of penicillins as antibacterial agents fifty years aga was one of the major breakthroughs in chemotherapy. The heroic efforts of the Oxford group to prepare and elucidate the structure of these molecules paved the way for a tremendou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2ecc2a3a88dfcdb537f1714cf1243c00
https://doi.org/10.1007/978-94-011-2928-2_5
https://doi.org/10.1007/978-94-011-2928-2_5
Publikováno v:
Journal of Bacteriology. 154:916-923
The effects of variations in growth conditions on the penicillin response of Streptococcus faecium ATCC 9790 were studied. Changes in the growth temperature and medium composition were found to cause striking changes in the bacterial generation time,
Publikováno v:
Journal of Biological Chemistry. 250:1348-1353
Exponentially growing cultures of Lactobacillus acidophilus strain 60AM Gasser were previously shown to lose about one-third of their cell wall peptidoglycan per generation via turnover (Boothby, D., Daneo-Moore, L., Higgins, M. L., Coyette, J., and
Publikováno v:
Journal of Biological Chemistry. 248:2161-2169
The cell wall peptidoglycan of Lactobacillus acidophilus strain 63 AM Gasser has been shown to turn over rapidly during balanced exponential growth and recovery from amino acid deprivation. In contrast, turnover of either pulse-labeled or extensively
Publikováno v:
Journal of Bacteriology. 116:1375-1382
Ultrastructural changes which occur during cellular autolysis of Lactobacillus acidophilus strain 63AM Gasser in 0.05 M citrate buffer, pH 5.0, were examined. Early in the process, randomly distributed electron-dense patches were seen on the wall sur