Zobrazeno 1 - 10
of 38
pro vyhledávání: '"E. Fonze"'
Autor:
Georges Dive, Astrid Zervosen, Frédéric Kerff, Bernard Joris, Raphaël Herman, Eric Sauvage, Rex Pratt, Paulette Charlier, Ana Maria Amoroso, E. Fonze, André Luxen
Publikováno v:
Journal of the American Chemical Society. 131:15262-15269
6-Beta-halogenopenicillanates are powerful, irreversible inhibitors of various beta-lactamases and penicillin-binding proteins. Upon acylation of these enzymes, the inhibitors are thought to undergo a structural rearrangement associated with the depa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69610335764befb7d78529d2a27beff6
https://doi.org/10.1021/ja9051526
https://doi.org/10.1021/ja9051526
Publikováno v:
Antimicrobial Agents and Chemotherapy. 50:2516-2521
Mycobacteria are important causes of infectious diseases. Although Mycobacterium tuberculosis and Mycobacterium leprae, two slow-growing species, are responsible for the most serious diseases, some fast-growing species, such as Mycobacterium avium, M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9cffc922d7dc0779058edc24a332d9b5
https://doi.org/10.1128/aac.01226-05
https://doi.org/10.1128/aac.01226-05
Publikováno v:
Cellular and Molecular Life Sciences. 60(8):1764-1773
The structures of the class C beta-lactamase from Enterobacter cloacae 908R alone and in complex with a boronic acid transition-state analogue were determined by X-ray crystallography at 2.1 and 2.3 A, respectively. The structure of the enzyme resemb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d9a36c9ef2a8e0e02d75f1578cbe9a2
https://researchportal.unamur.be/en/publications/6a0268d8-bd16-4e5b-b36b-f7abedc5f1cf
https://researchportal.unamur.be/en/publications/6a0268d8-bd16-4e5b-b36b-f7abedc5f1cf
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77e6fda124861f4f9d0c52b354cf6315
https://doi.org/10.1007/s00018-002-8500-0
https://doi.org/10.1007/s00018-002-8500-0
Publikováno v:
Biochemistry. 41:1877-1885
The Bacillus licheniformis BS3 beta-lactamase catalyzes the hydrolysis of the beta-lactam ring of penicillins, cephalosporins, and related compounds. The production of beta-lactamases is the most common and thoroughly studied cause of antibiotic resi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f3abc8f4160423f85590061653df3ba
https://doi.org/10.1021/bi015789k
https://doi.org/10.1021/bi015789k
Publikováno v:
Journal of Biological Chemistry. 274:21853-21860
The serine DD-transpeptidase/penicillin-binding protein of Streptomyces K15 catalyzes peptide bond formation in a way that mimics the penicillin-sensitive peptide cross-linking reaction involved in bacterial cell wall peptidoglycan assembly. The Stre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::310c5f4f8f5beb509ada3eea9a1380c8
https://doi.org/10.1074/jbc.274.31.21853
https://doi.org/10.1074/jbc.274.31.21853
Publikováno v:
Cellular and Molecular Life Sciences CMLS. 54:353-358
The technique of X-ray diffraction has been successfully applied to enzymes associated with peptidoglycan biosynthesis. The technique has taught us a great deal about the structures and catalytic mechanisms of penicillin-binding proteins and beta-lac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c04796ab189c70371113a4103ec10de
https://doi.org/10.1007/s000180050163
https://doi.org/10.1007/s000180050163
Autor:
Lu-Yun Lian, E. Fonze, Josette Lamotte-Brasseur, Christian Damblon, Xavier Raquet, Paulette Charlier, Gordon C. K. Roberts, Jean-Marie Frère
Publikováno v:
Proceedings of the National Academy of Sciences. 93:1747-1752
Beta-Lactamases are widespread in the bacterial world, where they are responsible for resistance to penicillins, cephalosporins, and related compounds, currently the most widely used antibacterial agents. Detailed structural and mechanistic understan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8614cd2091bdabcf42e4c93113071e6
https://doi.org/10.1073/pnas.93.5.1747
https://doi.org/10.1073/pnas.93.5.1747
TEM1 β-lactamase structure solved by molecular replacement and refined structure of the S235A mutant
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 51:682-694
beta-Lactamases are bacterial enzymes which catalyse the hydrolysis of the beta-lactam ring of penicillins, cephalosporins and related compounds, thus inactivating these antibiotics. The crystal structure of the TEM1 beta-lactamase has been determine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2262b53fc29c07a4973d4dcabdefee9
https://doi.org/10.1107/s0907444994014496
https://doi.org/10.1107/s0907444994014496
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography. 57(1):162-164
Crystals have been obtained of the Enterobacter cloacae 908R β-lactamase and two point mutants by the vapour-diffusion method using similar conditions [pH 9.0, polythylene glycol (Mr= 6000) as precipitant]. The three crystal forms belong to the orth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::754eec2320b29a22e5e86ed918dce86a
https://researchportal.unamur.be/en/publications/42e90584-81a6-42bb-99f0-c901e66db093
https://researchportal.unamur.be/en/publications/42e90584-81a6-42bb-99f0-c901e66db093