References of "Feller, Georges"
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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 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 (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 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 detailCold Adaptations in Proteins from Psychrophiles
Feller, Georges ULg

Scientific conference (2013)

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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 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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See detailAdaptation des protéines aux basses températures chez les psychrophiles
Feller, Georges ULg

Scientific conference (2012)

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See detailOptimization to low temperature activity in psychrophilic enzymes
Struvay, Caroline ULg; Feller, Georges ULg

in International Journal of Molecular Sciences (2012), 13(9), 11643-11665

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See detailIs there a cold shock response in the Antarctic psychrophile Pseudoalteromonas haloplanktis?
Piette, Florence ULg; Leprince, Pierre ULg; Feller, Georges ULg

in Extremophiles : Life Under Extreme Conditions (2012), 16

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See detailDecoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability
Pauwels, Kris; Sanchez del Pino, Manuel M.; Feller, Georges ULg et al

in PLoS ONE (2012), 7(5), 36999

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See detailPolar Microoganisms and Biotechnology
Feller, Georges ULg; Margesin, Rosa

in Miller, R. V.; Whyte, L. G. (Eds.) Polar Microbiology: Life in a Deep Freeze (2012)

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See detailActivity-Flexibility and Stability Relationships as revealed by multiple mutants of a psychrophilic alpha-Amylase
Cipolla, Alexandre ULg; D'Amico, Salvino ULg; Feller, Georges ULg

Poster (2011, May 23)

Permanently cold environments, like polar regions, have been colonized by a great variety of psychrophilic organisms producing enzymes adapted to function efficiently at low temperatures. We have ... [more ▼]

Permanently cold environments, like polar regions, have been colonized by a great variety of psychrophilic organisms producing enzymes adapted to function efficiently at low temperatures. We have investigated the role of weak interactions in thermal adaptation of proteins by site-directed mutagenesis of the psychrophilc alpha-amylase (AHA) from the Antarctic bacterium Pseudoalteromonas haloplanktis. Two stabilized multiple-mutants (Mut5 and Mut5CC) have been constructed. The single mutations were selected by comparison of the presence of weak interactions in a mesophilic homolog from pig pancreas, PPA. The three enzymes AHA, Mut5 and Mut5CC have been analyzed by differential scanning calorimetry, thermal and chemical denaturation. The flexibility has been studied by acrylamide-induced fluorescence quenching. In order to investigate the kinetic origin of the gain in stability, the kinetics of unfolding and refolding in GdmCl have been monitored at 15°C. The newly introduced weak interactions stabilized the mutants, protected them against heat and chemical unfolding and also induced an effective loss of flexibility. In addition, the two multiple-mutants exhibit an increased optimum temperature for activity. The first results of kinetic studies show a similar refolding phase but differences between the three amylases in the unfolding phase. These results unambiguously support the capital role of weak interactions in the balance between activity, flexibility and stability and provide a better knowledge of the adaptation of enzymes to cold temperatures. [less ▲]

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See detailBiophysical studies of trigger factors adapted to extreme biological temperatures
Struvay, Caroline; Piette, Florence; Feller, Georges ULg

Poster (2011)

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