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See detailFusariose disséminée chez un patient immunodéprimé
QUATRESOOZ, Pascale ULg; Meiers, I.; ARRESE ESTRADA, Jorge ULg et al

in Revue de l’Association Belge des Technologues de Laboratoire = Tijdschrift van de Belgische Vereniging van Laboratoriumtechnologen (2001), 28

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See detailFusarioses sur blé d'hiver au Grand-Duché de Luxembourg
Giraud, Frédéric; Pasquali, Matias; Vrancken, Carine et al

in Phytoma - la Défense des Végétaux (2009), 622-623

Au Grand-Duché de Luxembourg, la campagne 2006-2007 a été caractérisée par un hiver relativement doux et un printemps pluvieux. Ces conditions météorologiques ont permis le développement de nombreuses ... [more ▼]

Au Grand-Duché de Luxembourg, la campagne 2006-2007 a été caractérisée par un hiver relativement doux et un printemps pluvieux. Ces conditions météorologiques ont permis le développement de nombreuses maladies cryptogamiques sur le blé d’hiver, dont la fusariose. Cette maladie a été suivie sur 17 sites couvrant le G-D de Luxembourg par des mesures de prévalence (pourcentage moyen d’épis visuellement infectés) et de sévérité (pourcentage moyen d’épillets atteints par épi). Des valeurs moyennes de 8,9± +/- 15,5 % pour la prévalence et de 21,0± +/- 17,8 % pour la sévérité ont été enregistrées avec des différences significatives entre les cantons nord et sud pour la sévérité. Plus de 600 souches isolées des 17 sites ont été identifiées suivant des critères morphologiques et l’emploi d’outils moléculaires. 5 espèces semblent associées à la fusariose : Fusarium graminearum (23,5 %), F. culmorum (12,8 %), F. poae (19,4 %) (3 espèces potentiellement productrices de mycotoxines), F. avenaceum (20 %) et Microdochium nivale (18,7 %). Cette étude est la première du genre à avoir été faite au Grand-Duché de Luxembourg. [less ▲]

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See detailFusarium head blight and associated mycotoxin occurrence on winter wheat in Luxembourg in 2007/2008
Giraud, Frédéric; Pasquali, Matias; El Jarroudi, Moussa ULg et al

in Food Additives & Contaminants (2010), 27

Fusarium head blight (FHB) is among the major causes of reduced quality in winter wheat and its products. In addition, the causal fungi produce a variety of toxins. A relatively high FHB infection rate in ... [more ▼]

Fusarium head blight (FHB) is among the major causes of reduced quality in winter wheat and its products. In addition, the causal fungi produce a variety of toxins. A relatively high FHB infection rate in winter wheat was observed in 2007 and 2008 in Luxembourg. A fusariotoxin survey was carried out in 17 different geographical locations. Three groups of Fusarium mycotoxins (trichothecenes A and B and zearalenone) were analysed by a multi-detection HPLC–MS/MS method. Fusarium strains were also investigated by morphological and molecular methods. In addition, questionnaires relating to cultural practices were sent to the farmers managing the 17 fields investigated. FHB prevalence ranged from 0.3 to 65.8% (mean: 8.5%) in 2007 and from 0 to 24.5% (mean: 8.3%) in 2008. Results of morphological and molecular identification showed that the most common species isolated from diseased wheat spikes was F. graminearum (33.1%), followed by F. avenaceum (20.3%) and F. poae (17.8%). The chemical analysis revealed that 75% of the investigated fields were contaminated by deoxynivalenol (DON, range 0–8111 mg/kg). The preceding crop was highly and significantly correlated to the number of grains infected and had a significant impact on disease prevalence ( p¼0.025 and 0.017, respectively, Fisher’s F-test). A trend was found for maize as the preceding crop ( p¼0.084, Tukey’s test) to predict the amount of DON in the fields. This is the first report on the occurrence of DON and ZON in naturally infected wheat grains sampled from Luxembourg. [less ▲]

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See detailFused Multi-Sensor Image Mining for Feature Foundation Data
Streilein, William; Waxman, Allen M.; Ross et al

Conference (2000)

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See detailFusion alpha and proton diagnostics by thin layer activation
Chene, Grégoire ULg; Bonheure, George; Delhalle, René ULg et al

Conference (2012, September)

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See detailFusion d’images multi-résolution par égalisation de moyennes et variances locales. Comparaison avec la fusion par la méthode des ondelettes
de Bethune, Stanislas; Donnay, Jean-Paul ULg; Muller, Fabrice

in Actes des journées scientifiques du réseau de télédétection de l’UREF : La réalité de terrain : pratique et méthodes (1998)

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See detailLa fusion des communes : une réforme trentenaire
Lazzari, Mélanie; Verjans, Pierre ULg; Durviaux, Ann-Lawrence ULg

in Territoire(s) Wallon(s) (2008), hors série(Aout 2008), 27-34

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See detailLa fusion froide
Jaminon, Martine ULg

Article for general public (2001)

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See detailFusion Of Bovine Leukemia Virus With Target Cells Monitored By R18 Fluorescence And Pcr Assays
Zarkik, S.; Defrisequertain, F.; Portetelle, Daniel ULg et al

in Journal of Virology (1997), 71(1),

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See detailFusion of Multi- Sensor Passive and Active 3D Imagery
Fay, David A.; Verly, Jacques ULg; Braun, Michael I. et al

Conference (2001, April)

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See detailFusion of multispectral and panchromatic images by local mean and variance matching filtering techniques
de Bethune, Stanislas; Muller, Fabrice; Binard, Marc ULg et al

in Proceedings of the Second International Conference en Fusion of Earth Data (1998)

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See detailFusion of Visible, Infrared and 3D LADAR Imagery
Fay, David A.; Waxman, Allen M.; Verly, Jacques ULg et al

Conference (2001, August)

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See detailFusion proteins comprising the catalytic domain of mutansucrase and a starch-binding domain can alter the morphology of amylose-free potato starch granules during biosynthesis
Jacon, Géraldine ULg

in Transgenic Research (2007), 16

It has been shown previously that mutan can be co-synthesized with starch when a truncated mutansucrase (GtfICAT) is directed to potato tuber amyloplasts. The mutan seemed to adhere to the isolated starch ... [more ▼]

It has been shown previously that mutan can be co-synthesized with starch when a truncated mutansucrase (GtfICAT) is directed to potato tuber amyloplasts. The mutan seemed to adhere to the isolated starch granules, but it was not incorporated in the starch granules. In this study, GtfICAT was fused to the N- or C-terminus of a starch-binding domain (SBD). These constructs were introduced into two genetically different potato backgrounds (cv. Kardal and amf), in order to bring GtfICAT in more intimate contact with growing starch granules, and to facilitate the incorporation of mutan polymers in starch. Fusion proteins of the appropriate size were evidenced in starch granules, particularly in the amf back- ground. The starches from the various GtfICAT/ SBD transformants seemed to contain less mutan than those from transformants with GtfICAT alone, suggesting that the appended SBD might inhibit the activity of GtfICAT in the engineered fusion proteins. Scanning electron microscopy showed that expression of SBD-GtfICAT resulted in alterations of granule morphology in both genetic backgrounds. Surprisingly, the amf starches con- taining SBD-GtfICAT had a spongeous appearance, i.e., the granule surface contained many small holes and grooves, suggesting that this fusion protein can interfere with the lateral interactions of amylopectin sidechains. No differences in phys- ico-chemical properties of the transgenic starches were observed. Our results show that expression of granule-bound and ‘‘soluble’’ GtfICAT can affect starch biosynthesis differently. [less ▲]

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See detailLes fusions de communes en Belgique : Nouvelles communes, nouveaux territoires de projets ?
Schmitz, Serge ULg

in Territoires prescrits, territoires vécus : inter-territorialité au coeur des recompositions des espaces ruraux : ARF, Toulouse 25-27 octobre 2000 (2000)

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See detailFusions des communes et redistribution du revenu: quelques aspects du problème
Jurion, Bernard ULg

in Recherches économiques de Louvain (1975)

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See detailFusogenic Alzheimer'S Peptide Fragment A Beta (29-42) In Interaction With Lipid Bilayers: Secondary Structure, Dynamics, And Specific Interaction With Phosphatidyl Ethanolamine Polar Heads As Revealed By Solid-State Nmr
Ravault, S.; Soubias, O.; Saurel, O. et al

in Protein Science : A Publication of the Protein Society (2005), 14(5), 1181-9

The interaction of the native Alzheimer's peptide C-terminal fragment Abeta (29-42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and POPE in a 9:1 molar ratio was investigated ... [more ▼]

The interaction of the native Alzheimer's peptide C-terminal fragment Abeta (29-42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and POPE in a 9:1 molar ratio was investigated by solid-state NMR. This fragment and the lipid composition were selected because they represent the minimum requirement for the fusogenic activity of the Alzheimer's peptide. The chemical shifts of alanine methyl isotropic carbon were determined by MAS NMR, and they clearly demonstrated that the major form of the peptide equilibrated in membrane is not in a helical conformation. (2)H NMR, performed with acyl chain deuterated POPC, demonstrated that there is no perturbation of the acyl chain's dynamics and of the lipid phase transition temperature. (2)H NMR, performed with alanine methyl-deuterated peptide demonstrated that the peptide itself has a limited mobility below and above the lipid phase transition temperature (molecular order parameter equal to 0.94). MAS (31)P NMR revealed a specific interaction with POPE polar head as seen by the enhancement of POPE phosphorus nuclei T(2) relaxation. All these results are in favor of a beta-sheet oligomeric association of the peptide at the bilayer interface, preferentially recruiting phosphatidyl ethanolamine polar heads. [less ▲]

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See detailFusogenic Properties Of The C-Terminal Domain Of The Alzheimer Beta-Amyloid Peptide
Pillot, T.; Goethals, M.; Vanloo, B. et al

in Journal of Biological Chemistry (1996), 271(46), 28757-65

A series of natural peptides and mutants, derived from the Alzheimer beta-amyloid peptide, was synthesized, and the potential of these peptides to induce fusion of unilamellar lipid vesicles was ... [more ▼]

A series of natural peptides and mutants, derived from the Alzheimer beta-amyloid peptide, was synthesized, and the potential of these peptides to induce fusion of unilamellar lipid vesicles was investigated. These peptide domains were identified by computer modeling and correspond to respectively the C-terminal (e.g. residues 29-40 and 29-42) and a central domain (13-28) of the beta-amyloid peptide. The C-terminal peptides are predicted to insert in an oblique way into a lipid membrane through their N-terminal end, while the mutants are either parallel or perpendicular to the lipid bilayer. Peptide-induced vesicle fusion was demonstrated by several techniques, including lipid-mixing and core-mixing assays using pyrene-labeled vesicles. The effect of peptide elongation toward the N-terminal end of the entire beta-amyloid peptide was also investigated. Peptides corresponding to residues 22-42 and 12-42 were tested using the same techniques. Both the 29-40 and 29-42 beta-amyloid peptides were able to induce fusion of unilamellar lipid vesicles and calcein leakage, and the amyloid 29-42 peptide was the most potent fusogenic peptide. Neither the two mutants or the 13-28 beta-amyloid peptide had any fusogenic activity. Circular dichroism measurements showed an increase of the alpha-helical content of the two C-terminal peptides at increasing concentrations of trifluoroethanol, which was accompanied by an increase of the fusogenic potential of the peptides. Our data suggest that the alpha-helical content and the angle of insertion of the peptide into a lipid bilayer are critical for the fusogenic activity of the C-terminal domain of the amyloid peptide. The differences observed between the fusogenic capacity of the amyloid 29-40 and 29-42 peptides might result from differences in the degree of penetration of the peptides into the membrane and the resulting membrane destabilization. The longer peptides, residues 22-42 and 12-42, had decreased, but significant, fusogenic properties associated with perturbation of the membrane permeability. These data suggest that the fusogenic properties of the C-terminal domain of the beta-amyloid peptide might contribute to the cytotoxicity of the peptide by destabilizing the cell membrane. [less ▲]

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See detailFusogenic Segments Of Bovine Leukemia-Virus And Simian Immunodeficiency Virus Are Interchangeable And Mediate Fusion By Means Of Oblique Insertion In The Lipid Bilayer Of Their Target-Cells
Voneche, V.; Portetelle, Daniel ULg; Kettmann, Richard ULg et al

in Proceedings of the National Academy of Sciences of the United States of America (1992), 89(9),

Modified bovine leukemia virus (BLV) glycoproteins were expressed by using vaccinia virus recombinants, and their fusogenic capacities were examined by a syncytia-formation assay. This analysis indicates ... [more ▼]

Modified bovine leukemia virus (BLV) glycoproteins were expressed by using vaccinia virus recombinants, and their fusogenic capacities were examined by a syncytia-formation assay. This analysis indicates that (i) both BLV envelope glycoproteins gp51 and gp30 are necessary for cell fusion; (ii) insertion of the N-terminal segment of gp30 (fusion peptide) into the lipid bilayer in an oblique orientation, as predicted by computer conformational analysis, results in fusogenic capacities higher than insertion in a perpendicular or parallel orientation; and (iii) replacement of the BLV fusion peptide with its simian immunodeficiency virus counterpart does not modify the fusogenic capacity of the BLV glycoprotein. [less ▲]

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See detailFusogenic Tilted Peptides Induce Nanoscale Holes In Supported Phosphatidylcholine Bilayers
El Kirat, K.; Lins, Laurence ULg; Brasseur, Robert ULg et al

in Langmuir (2005), 21(7), 3116-21

Tilted peptides are known to insert in lipid bilayers with an oblique orientation, thereby destabilizing membranes and facilitating membrane fusion processes. Here, we report the first direct ... [more ▼]

Tilted peptides are known to insert in lipid bilayers with an oblique orientation, thereby destabilizing membranes and facilitating membrane fusion processes. Here, we report the first direct visualization of the interaction of tilted peptides with lipid membranes using in situ atomic force microscopy (AFM) imaging. Phase-separated supported dioleoylphosphatidylcholine/dipalmitoylphosphatidylcholine (DOPC/DPPC) bilayers were prepared by fusion of small unilamellar vesicles and imaged in buffer solution, in the absence and in the presence of the simian immunodeficiency virus (SIV) peptide. The SIV peptide was shown to induce the rapid appearance of nanometer scale bilayer holes within the DPPC gel domains, while keeping the domain shape unaltered. We attribute this behavior to a local weakening and destabilization of the DPPC domains due to the oblique insertion of the peptide molecules. These results were directly correlated with the fusogenic activity of the peptide as determined using fluorescently labeled DOPC/DPPC liposomes. By contrast, the nontilted ApoE peptide did not promote liposome fusion and did not induce bilayer holes but caused slight erosion of the DPPC domains. In conclusion, this work provides the first direct evidence for the production of stable, well-defined nanoholes in lipid bilayer domains by the SIV peptide, a behavior that we have shown to be specifically related to the tilted character of the peptide. A molecular mechanism underlying spontaneous insertion of the SIV peptide within lipid bilayers and the subsequent removal of bilayer patches is proposed, and its relevance to membrane fusion processes is discussed. [less ▲]

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