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See detailPEGylated and Functionalized Aliphatic Polycarbonate Polyplex Nanoparticles for Intravenous Administration of HDAC5 siRNA in Cancer Therapy
Frère, Antoine ULg; Baroni, Alexandra; Hendrick, Elodie ULg et al

in ACS Applied Materials and Interfaces (2017), 25(9(3)), 2181-2195

Guanidine and morpholine functionalized aliphatic polycarbonate polymers are able to efficiently deliver histone deacetylase 5 (HDAC5) siRNA into the cytoplasm of cancer cells in vitro leading to a ... [more ▼]

Guanidine and morpholine functionalized aliphatic polycarbonate polymers are able to efficiently deliver histone deacetylase 5 (HDAC5) siRNA into the cytoplasm of cancer cells in vitro leading to a decrease of cell proliferation were previously developed. To allow these biodegradable and biocompatible polyplex nanoparticles to overcome the extracellular barriers and be effective in vivo after an intravenous injection, polyethylene glycol chains (PEG750 or PEG2000) were grafted on the polymer structure. These nanoparticles, showed an average size of about 150 nm and a slightly positive zeta potential with complete siRNA complexation. Behavior of PEGylated and non-PEGylated polyplexes were investigated in the presence of serum, in terms of siRNA complexation (Fluorescence Correlation Spectroscopy), size (Dynamic Light Scattering and Single-Particle Tracking), interaction with proteins (Isothermal Titration Calorimetry) and cellular uptake. Surprisingly, both PEGylated and non-PEGylated formulations presented relatively good behavior in the presence of fetal bovine serum (FBS). Hemocompatibility tests showed no effect of these polyplexes on hemolysis and coagulation. In vivo biodistribution in mice was performed and showed a better siRNA accumulation at the tumor site for PEGylated polyplexes. However, cellular uptake in protein-rich conditions showed that PEGylated polyplex lost their ability to interact with biological membranes and enter into cells, showing the importance to perform in vitro investigations in physiological conditions closed to in vivo situation. In vitro, the efficiency of PEGylated nanoparticles decreases compared to non-PEGylated particles, leading to the loss of the antiproliferative effect on cancer cells. [less ▲]

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See detailDeciphering the factors defining the pH-dependence of a commercial glycoside hydrolase family 8 enzyme
Barroca, M.; Santos, G.; Johansson, B. et al

in Enzyme and Microbial Technology (2017), 96

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See detailActivity-stability relationships revisited in blue oxidases catalyzing electron transfer at extreme temperatures
Roulling, F.; Godin, Amandine ULg; Cipolla, A. et al

in Extremophiles : Life Under Extreme Conditions (2016), 20

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See detailA single amino acid substitution toggles chloride dependence of the alpha-amylase paralog Amyrel in Drosophila melanogaster and Drosophila virilis species
Claisse, G.; Feller, Georges ULg; Bonneau, M. et al

in Insect Biochemistry and Molecular Biology (2016), 75

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See detailProduction, purification and characterization of a novel cold-active superoxide dismutase from the Antarctic strain Aspergillus glaucus 363
Abrashev, R.; Feller, Georges ULg; Kostadinova, N. et al

in Fungal Biology (2016), 120

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See detailAnti-biofilm activities from marine cold adapted bacteria against staphylococci and Pseudomonas aeruginosa
Papa, R.; Selan, L.; Parrilli, E. et al

in Frontiers in Microbiology (2015), 6

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See detailMultiple disulfide bridges modulate conformational stability and flexibility in hyperthermophilic archaeal purine nucleoside phosphorylase
Bagarolo; Porcelli, M; Martino et al

in Biochimica et Biophysica Acta-Proteins and Proteomics (2015), 1854

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See detailFunctional adaptations of the bacterial chaperone trigger factor to extreme environmental temperatures
Godin-Roulling, Amandine ULg; Schmidpeter, P.A.M.; Schmid, F.X. et al

in Environmental Microbiology (2015), 17(7), 2407-2420

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See detailProtein folding at extreme temperatures: current issues
Feller, Georges ULg

in Biophysical Journal (2015), 108(2 suppl. 1), 358

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See detailFunctional adaptations of the bacterial chaperone trigger factor to extreme environmental temperatures
Godin, Amandine ULg; Schmidpeter, P.; Schmid, F.X. et al

Poster (2014)

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See detailThermal adaptation of the ribosomal chaperone trigger factor
Godin, Amandine ULg; Schmidpeter, Phillip; Schmid, Franz et al

Poster (2013, June)

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See detailThermal adaptation of the ribosomal chaperone trigger factor
Godin, Amandine ULg; Schmidpeter, Phillip; Schmid, Franz et al

Poster (2013, May)

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See detailEnergetics of protein stability at extreme environmental temperatures in bacterial trigger factors
Struvay, Caroline ULg; Negro, Sonia; Matagne, André ULg et al

in Biochemistry (2013), 52

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See detailCold Adaptations in Proteins from Psychrophiles
Feller, Georges ULg

Conference (2013)

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See detailEnzymatic characterization of recombinant alpha-amylase in the Drosophila melanogaster species subgroup: is there an effect of specialization on digestive enzyme?
Commin, Céline; Aumont-Nicaise, Magali; Claisse, Gaëlle et al

in Genes & Genetic Systems (2013), 88

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See detailThermal adaptation of the ribosomal chaperone trigger factor
Godin, Amandine ULg; Schmidpeter, P.; Schmid, F.X. et al

Poster (2013)

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See detailThe Cold-Active M1 Aminopeptidase from the Arctic Bacterium Colwellia psychrerythraea
Bauvois, Cédric; Huston, Adrienne; Feller, Georges ULg

in Rawlings, Neil D.; Salvesen, Guy S. (Eds.) Handbook of Proteolytic Enzymes (Third Ed) (2013)

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See detailPsychrophilic enzymes: from folding to function and biotechnology
Feller, Georges ULg

in Scientifica (2013), 2013(Article ID 512840), 1-28

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See detailLife in the cold: proteomics of the Antarctic bacterium Pseudoalteromonas haloplanktis
Piette, Florence ULg; Struvay, Caroline ULg; Godin, Amandine ULg et al

in Heazlewood, J. L.; Petzold, C. J. (Eds.) Proteomic Applications in Biology (2012)

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