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See detailEntanglement of random localized and multifractal states
Martin, John ULg; Giraud, Olivier; Georgeot, Bertrand

Conference (2009, August)

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See detailEnteral nutrition-associated incretin effect in the critically ill
Preiser, JC; Jamaludin, U; Docherty, P et al

in Proceedings of the 33rd Congress of Clinical Nutrition and Metabolism (ESPEN 2011) (2011)

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See detailEnteritis and enterotoxaemia in rabbits
Marlier, Didier ULg

in Duchesnes, C.; Menozzi, M. G.; Pelkonen, S. (Eds.) et al Diagnosis and typing of clostridia in medical and food microbiology (2006)

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See detailThe Enterococcus Hirae R40 Penicillin-Binding Protein 5 and the Methicillin-Resistant Staphylococcus Aureus Penicillin-Binding Protein 2' Are Similar
el Kharroubi, Aboubaker; Jacques, Philippe; Piras, Graziella et al

in Biochemical Journal (1991), 280(Pt 2), 463-469

The penicillin-resistant Enterococcus hirae R40 has a typical profile of membrane-bound penicillin-binding proteins (PBPs) except that the 71 kDa PBP5 of low penicillin affinity represents about 50% of ... [more ▼]

The penicillin-resistant Enterococcus hirae R40 has a typical profile of membrane-bound penicillin-binding proteins (PBPs) except that the 71 kDa PBP5 of low penicillin affinity represents about 50% of all the PBPs present. Water-soluble tryptic-digest peptides were selectively produced from PBP5, their N-terminal regions were sequenced and synthetic oligonucleotides were used as primers to generate a 476 bp DNA fragment by polymerase chain reaction. On the basis of these data, the PBP5-encoding gene was cloned in Escherichia coli by using pBR322 as vector. The gene, included in a 7.1 kb insert, had the information for a 678-amino acid-residue protein. PBP5 shows similarity, in the primary structure, with the high-molecular-mass PBPs of class B. In particular, amino acid alignment of the enterococcal PBP5 and the methicillin-resistant staphylococcal PBP2' generates scores that are 30, for the N-terminal domains, and 53, for the C-terminal domains, standard deviations above that expected for a run of 20 randomized pairs of proteins having the same amino acid compositions as the two proteins under consideration. [less ▲]

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See detailL’Entérocolite Epizootique du Lapin
Marlier, Didier ULg; Vindevogel, Henri ULg

in Annales de Médecine Vétérinaire (1998), 142

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See detailLes entérocoques : avantages et inconvénients en biotechnologie (synthèse bibliographique)
Aguilar Galvez, A.; Dubois Dauphin, Robin ULg; Destain, Jacqueline ULg et al

in Biotechnologie, Agronomie, Société et Environnement = Biotechnology, Agronomy, Society and Environment [=BASE] (2012), 16(1), 67-76

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See detailEnterohaemolysin and Shiga-like toxin genes in E.coli.
Pohl, P.; Liintermans, P.; Mainil, Jacques ULg et al

in Veterinary Record : Journal of the British Veterinary Association (1990)

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See detailEnterohaemorrhagic Escherichia coli (EHEC) isolated from 2 months old Southamerican camelid (Lamea guanacoe) with diarrhoea.
Mercado, E.C.; Rodriguez, Sabrina ULg; Parreño, V. et al

Poster (2002, November 10)

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See detailEnterohaemorrhagic Escherichia coli serogroup O111 inhibits NF-(kappa)B-dependent innate responses in a manner independent of a type III secreted OspG orthologue.
Nobe, Rika; Nougayrede, Jean*-Philippe; Taieb, Frederic et al

in Microbiology (2009), 155(Pt 10), 3214-25

Enterohaemorrhagic and enteropathogenic Escherichia coli (EHEC and EPEC) inject a repertoire of effector proteins into host cells via a type III secretion system (T3SS) encoded by the locus of enterocyte ... [more ▼]

Enterohaemorrhagic and enteropathogenic Escherichia coli (EHEC and EPEC) inject a repertoire of effector proteins into host cells via a type III secretion system (T3SS) encoded by the locus of enterocyte effacement (LEE). OspG is an effector protein initially identified in Shigella that was shown to inhibit the host innate immune response. In this study, we found ospG homologues in EHEC (mainly of serogroup O111) and in Yersinia enterocolitica. The T3SS encoded by the LEE was able to inject these different OspG homologues into host cells. Infection of HeLa cells with EHEC O111 inhibited the NF-kappaB-dependent innate immune response via a T3SS-dependent mechanism. However, an EHEC O111 ospG mutant was still able to inhibit NF-kappaB p65 transfer to the nucleus in infected cells stimulated by tumour necrosis factor alpha (TNF-alpha). In addition, no difference in the inflammatory response was observed between wild-type EHEC O111 and the isogenic ospG mutant in the rabbit ligated intestinal loop model. These results suggest that OspG is not the sole effector protein involved in the inactivation of the host innate immune system during EHEC O111 infection. [less ▲]

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See detailL'Entéropathie Epizootique du Lapin (EEL) : étude du rôle des infections par clostridium perfringens dans l’étio-pathogénie de ce syndrome
Dewrée, Roxane; Licois, Dominique; Coudert, Pierre et al

in Proceedings of the 10èmes Journées de la Recherche Cunicole (2003, November 20)

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See detailL'Entéropathie Epizootique du Lapin (EEL) : un bilan provisoire des résultats après 20 mois de recherches
Marlier, Didier ULg; Dewrée, Roxane; Licois, Dominique et al

in Proceedings of the 10èmes Journées de la Recherche Cunicole (2003, November 20)

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See detailEnteropathogenic (EPEC), enterohaemorragic (EHEC) and verotoxigenic (VTEC) Escherichia coli in wild cervids
Bardiau, Marjorie ULg; Grégoire, Fabien ULg; Muylaert, Adeline ULg et al

in Journal of Applied Microbiology (2010), 109(6), 2214-2222

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See detailEnteropathogenic and enterohaemorrhagic Escherichia coli deliver a novel effector called Cif, which blocks cell cycle G(2)/M transition
Marches, O.; Ledger, T. N.; Boury, M. et al

in Molecular Microbiology (2003), 50(5), 1553-1567

Enteropathogenic Escherichia coli (EPEC) and enterohaemorrhagic E. coli (EHEC) are closely related pathogens. Both use a type III secretion system (TTSS) encoded by the 'locus of enterocyte effacement ... [more ▼]

Enteropathogenic Escherichia coli (EPEC) and enterohaemorrhagic E. coli (EHEC) are closely related pathogens. Both use a type III secretion system (TTSS) encoded by the 'locus of enterocyte effacement' (LEE) to subvert and attach to epithelial cells through the injection of a repertoire of effector molecules. Here, we report the identification of a new TTSS translocated effector molecule called Cif, which blocks cell cycle G(2)/M transition and induces the formation of stress fibres through the recruitment of focal adhesions. Cif is not encoded by the LEE but by a lambdoid prophage present in EPEC and EHEC. A cif mutant causes localized effacement of microvilli and intimately attaches to the host cell surface, but is defective in the ability to block mitosis. When expressed in TTSS competent LEE-positive pathogens, Cif is injected into the infected epithelial cells. These cells arrested at the G(2)/M phase displayed accumulation of inactive phosphorylated Cdk1. In conclusion, Cif is a new member of a growing family of bacterial cyclomodulins that subvert the host eukaryotic cell cycle. [less ▲]

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See detailEnterotoxaemia in foods animals
Linden, A.; Manteca, C.; Daube, G. et al

Conference (2004)

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See detailEnterotoxaemia-like syndrome and Clostridium perfringens in veal calves
Muylaert, Adeline ULg; Lebrun, M.; Duprez, Jean-Noël ULg et al

in Veterinary Record : Journal of the British Veterinary Association (2010), 167

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See detailL'entérotoxémie bovine en Belgique. I. Introduction et contexte bibliographique.
Manteca, C.; Daube, Georges ULg

in Annales de Médecine Vétérinaire (1994), 138

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See detailL'entérotoxémie bovine en Belgique. II. Epizootiologie élémentaire et pathologie descriptive.
Manteca, Christophe; Daube, Georges ULg; Jauniaux, Thierry ULg et al

in Annales de Médecine Vétérinaire (2000), 145

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See detailLes entérotoxémies
Moreau, F.; Saegerman, Claude ULg

in Probio-Revue (1989)

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