References of "Crowet, Jean-Marc"
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See detailGROMPALA: a membrane-implicit modelling method to screen lipid-interacting molecules
Steinhauer, Sven; Crowet, Jean-Marc ULg; Brasseur, Robert ULg et al

in Software and techniques for Bio-molecular modeling (2016)

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See detailModeling of the cyclic lipodepsipeptide Pseudodesmin A self-assembly through molecular dynamic simulations
Crowet, Jean-Marc ULg; Sinnaeve, Davy; Fehér, Kristina et al

Poster (2016, April)

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See detailInteractions of sugar-based bolaamphiphiles with biomimetic systems of plasma membranes
Nasir, Mehmet Nail ULg; Crowet, Jean-Marc ULg; Lins, Laurence ULg et al

in Biochimie (2016), In Press

Glycolipids constitute a class of molecules with various biological activities. Among them, sugar-based bolaamphiphiles characterized by their biocompatibility, biodegradability and lower toxicity, became ... [more ▼]

Glycolipids constitute a class of molecules with various biological activities. Among them, sugar-based bolaamphiphiles characterized by their biocompatibility, biodegradability and lower toxicity, became interesting for the development of efficient and low cost lipid-based drug delivery systems. Their activity seems to be closely related to their interactions with the lipid components of the plasma membrane of target cells. Despite many works devoted to the chemical synthesis and characterization of sugar-based bolaamphiphiles, their interactions with plasma membrane have not been completely elucidated. In this work, two sugar-based bolaamphiphiles differing only at the level of their sugar residues were chemically synthetized. Their interactions with membranes have been investigated using model membranes containing or not sterol and with in silico approaches. Our findings indicate that the nature of sugar residues has no significant influence for their membrane interacting properties, while the presence of sterol attenuates the interactions of both bolaamphiphiles with the membrane systems. The understanding of this distinct behavior of bolaamphiphiles towards sterol-containing membrane systems could be useful for their applications as drug delivery systems. [less ▲]

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See detailSimulation par dynamique moléculaire de membranes lipidiques complexes
Crowet, Jean-Marc ULg; Dauchez, Manuel

Scientific conference (2015, November 25)

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See detailModeling of the cyclic lipodepsipeptide Pseudodesmin A self- assembly through molecular dynamic simulations
Crowet, Jean-Marc ULg; Sinnaeve, Davy; Fehér, Kristina et al

Poster (2015, October)

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See detailExperimental and in silico approaches to study the interaction of Remorin with plant plasma membrane : specific interaction of the C-term domain with lipids
Deleu, Magali ULg; Nasir, Mehmet Nail ULg; Gronnier, Julien et al

Conference (2015, September 29)

The function of Remorins, a diverse family of plant-specific proteins (1) is far to be fully elucidated. One of them, StREM1.3 (for Solanum tuberosum Remorin from group 1, homolog 3) has been reported to ... [more ▼]

The function of Remorins, a diverse family of plant-specific proteins (1) is far to be fully elucidated. One of them, StREM1.3 (for Solanum tuberosum Remorin from group 1, homolog 3) has been reported to regulate cell-to-cell propagation of the potato virus X (2). It was also shown to be localized to the inner leaflet of plasma membranes (PMs) and along plasmodesmata, bridges connecting neighbor cells essential for cell-to-cell communication in plants (3). The mechanisms driving StREM1.3 association with PM is still an open question. It was shown recently that a domain of 28 residues at the C-terminus of the potato (RemCA) is required and sufficient for anchoring to the PM (4). Here we combined experimental and in silico biophysics to unravel the molecular bases of RemCA membrane binding. Biomimetic membrane models of plant PM such as monolayers and liposomes were used with various biophysical techniques (Langmuir monolayer technique, Fourier-transformed infrared spectroscopy, circular dichroïsm) and modeling tools (home-made methods and molecular dynamics) (5) to answer to three questions: (i) What is the conformation adopted by RemCA within a membrane?, (ii) Is there any membrane lipid specificity in the RemCA-membrane binding? (iii) What is the role of the two different RemCA domains in the interaction? Results show that RemCA displays a preference for plant phosphoinositide and sitosterol-enriched inner leaflet plasma membrane rafts. Within the membrane, the C-terminal and the N-terminal domains adopt a random coil and a -helical conformation respectively. The C-terminal domain acts as a driver to bind RemCA to the membrane while the N-terminal domain stabilizes the peptide at the membrane. Lysine residues have a crucial importance in this interaction. References (1) Raffaele et al., Plant Physiol., 2007, 145: 593–600 (2) Raffaela et al., Plant Cell, 2009, 21: 1541–1555. (3) Maule, Curr. Opin. Plant Biol., 2008, 11: 680–686. (4) Perraki et al., Plant Physiology, 2012, 160 : 624-637. (5) Deleu et al., Biochim. Biophys. Acta – Biomembranes, 2014, 1838 : 3171-3190. [less ▲]

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See detailSurfactin: a receptor-independent bacterial elicitor of plant immunity?
Luzuriaga Loaiza, Walter ULg; Legras, Aurelien; Crowet, Jean-Marc ULg et al

Poster (2015, May 13)

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See detailStructure predictions of membrane domains of proteins from the Divisome and BlaR
Crowet, Jean-Marc ULg; Dony, Nicolas; Joris, Bernard ULg et al

Poster (2014, November 28)

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