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NMR structure of antibiotics plipastatins A and B from Bacillus subtilis inhibitors of phospholipase A2
Plipastatins A and B are antifungal antibiotics belonging to a family of lipopeptides capable of inhibiting phospholipase A2 (PLA2) and are biosynthesised under certain circumstances by BacillusExpand
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Subcellular localization of 14-3-3 proteins in Toxoplasma gondii tachyzoites and evidence for a lipid raft-associated form.
A polyclonal antibody was raised against a Toxoplasma gondii 14-3-3-gluthatione S-transferase fusion protein obtained by cloning a 14-3-3 cDNA sequence determined from the T. gondii database. ThisExpand
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Structures of bacillomycin D and bacillomycin L peptidolipid antibiotics from Bacillus subtilis.
The complete structures of bacillomycin D and bacillomycin L were revised by FAB mass spectrometry and by Edman degradation of the derivatives resulting from the N-bromosuccinimide reaction. TheExpand
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Influence of the culture medium on the production of iturin A by Bacillus subtilis.
The production of iturin A by Bacillus subtilis was studied with respect to the composition of the culture medium. Increasing phosphate concentrations did not modify the antibiotic yield. Fructose,Expand
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Structure of bacillomycin D, a new antibiotic of the iturin group.
Bacillomycin D is an antifungal agent extracted from the culture medium of a strain of Bacillus subtilis. It is a mixture of two homologous lipopeptides: the lipid moiety consists ofExpand
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Bacillomycin F, a new antibiotic of iturin group: isolation and characterization.
Bacillomycin F, a new family of iturin group antibiotics, was isolated from Bacillus subtilis. It shows a potent antifungal activity and a narrow spectrum against bacteria. Acid hydrolysis gave aExpand
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Role of Calcium and Membrane Organization on Phospholipase D Localization and Activity
The phospholipase D (PLD) from Streptomyces chromofuscus is a soluble enzyme known to be activated by the phosphatidic acid-calcium complexes. PLD-catalyzed hydrolysis of phospholipids in aqueousExpand
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Streptomyces chromofuscus phospholipase D interaction with lipidic activators at the air-water interface.
The phospholipase D from Streptomyces chromofuscus (PLDSc) is a soluble enzyme that interacts with membranes to catalyse phosphatidylcholine (PC) transformation. In this work, we focused on theExpand
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A FTIR spectroscopy evidence of the interactions between wheat germ agglutinin and N‐acetylglucosamine residues
Wheat germ agglutinin (WGA), a lectin binding a N‐acetyl‐D‐neuraminic acid (NeuNAc) and/or N‐acetyl‐D‐glucosamine (GlcNAc) group, was studied by Fourier transform infrared (FTIR) spectroscopy.Expand
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Effect of amino acids on the biosynthesis of beta-amino acids, constituents of bacillomycins F.
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