B
Bernard Joris
Researcher at University of Liège
Publications - 167
Citations - 9368
Bernard Joris is an academic researcher from University of Liège. The author has contributed to research in topics: Peptidoglycan & Penicillin binding proteins. The author has an hindex of 43, co-authored 164 publications receiving 8768 citations. Previous affiliations of Bernard Joris include Université catholique de Louvain.
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A standard numbering scheme for the class A beta-lactamases.
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Bacterial peptidoglycan (murein) hydrolases.
TL;DR: The current view on the regulation of autolysins and on the role of cytoplasm hydrolases in peptidoglycan recycling and induction of beta-lactamase is reviewed.
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Surfactin and fengycin lipopeptides of Bacillus subtilis as elicitors of induced systemic resistance in plants
Marc Ongena,Emmanuel Jourdan,A. Adam,Michel Paquot,Alain Brans,Bernard Joris,Jean-Louis Arpigny,Philippe Thonart +7 more
TL;DR: Experiments conducted on bean and tomato plants showed that overexpression of both surfactin and fengycin biosynthetic genes in the naturally poor producer Bacillus subtilis strain 168 was associated with a significant increase in the potential of the derivatives to induce resistance.
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Bacillus amyloliquefaciens GA1 as a source of potent antibiotics and other secondary metabolites for biocontrol of plant pathogens
Anthony Arguelles-Arias,Marc Ongena,Badre Halimi,Yannick Lara,Alain Brans,Bernard Joris,Patrick Fickers +6 more
TL;DR: The production of all of these antibiotic compounds highlights B. amyloliquefaciens GA1 as a good candidate for the development of biocontrol agents.
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The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.
Bernard Joris,J M Ghuysen,Georges Dive,A Renard,Otto Dideberg,Paulette Charlier,Jean-Marie Frère,Judith A. Kelly,J C Boyington,Paul C. Moews +9 more
TL;DR: Though the evolutionary distance may vary considerably, all these penicillin-interactive proteins and domains appear to be members of a single superfamily of active-site-serine enzymes distinct from the classical trypsin or subtilisin families.