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Feller, Georges

Institute	Top \| Institute \| Publications \| Projects
Université de Liège (ULG), more Direct contact at institute: Tel.: +32-(0)4-366 33 43 Fax: +32-(0)4-366 33 64 E-mail:

Projects (2)	Top \| Institute \| Publications \| Projects
Belgian Polar Research Cluster, more OA-CL-016 BE-POLES: Belgische Polaire onderzoekscluster, more

Publications (42)	Top \| Institute \| Publications \| Projects
A1 Publications (37) [show]
Feller, G. (2018). Protein folding at extreme temperatures: current issues. Seminars in Cell & Developmental Biology 84: 129-137. https://dx.doi.org/10.1016/j.semcdb.2017.09.003, more Godin-Roulling, A.; Schmidpeter, P.A.M.; Schmid, F.X.; Feller, G. (2015). Functional adaptations of the bacterial chaperone trigger factor to extreme environmental temperatures. Environ. Microbiol. 17(7): 2407-2420. dx.doi.org/10.1111/1462-2920.12707, more Papa, R; Selan, L; Parrilli, E; Tilotta, M; Sannino, F; Feller, G.; Tutino, L; Artini, M (2015). Anti-biofilm activities from marine cold adapted bacteria against Staphylococci and Pseudomonas aeruginosa. Front. Microbiol. 6: 10 pp. dx.doi.org/10.3389/fmicb.2015.01333, more Struvay, C.; Negro, S.; Matagne, A.; Feller, G. (2013). Energetics of protein stability at extreme environmental temperatures in bacterial trigger factors. Biochemistry (Wash.) 52(17): 2982-2990. dx.doi.org/10.1021/bi4002387, more Piette, F.; Leprince, P.; Feller, G. (2012). Is there a cold shock response in the Antarctic psychrophile Pseudoalteromonas haloplanktis? Extremophiles 16(4): 681-683. https://dx.doi.org/10.1007/s00792-012-0456-x, more Struvay, C.; Feller, G. (2012). Optimization to low temperature activity in psychrophilic enzymes. International Journal of Molecular Sciences 13(9): 11643-11665. https://dx.doi.org/10.3390/ijms130911643, more Piette, F.; Struvay, C.; Feller, G. (2011). The protein folding challenge in psychrophiles: facts and current issues. Environ. Microbiol. 13(8): 1924-1933. dx.doi.org/10.1111/j.1462-2920.2011.02436.x, more Piette, F.; D'Amico, S.; Mazzucchelli, G.; Danchin, A.; Leprince, P.; Feller, G. (2011). Life in the cold: a proteomic study of cold-repressed proteins in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125. Appl. Environ. Microbiol. 77(11): 3881-3883. dx.doi.org/10.1128/AEM.02757-10, more Wilmes, B.; Kock, H.; Glagla, S.; Albrecht, D.; Voigt, B.; Markert, S.; Gardebrecht, A.; Bode, R.; Danchin, A.; Feller, G.; Hecker, M.; Schweder, T. (2011). Cytoplasmic and periplasmic signatures of exponentially growing cells of the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125. Appl. Environ. Microbiol. 77(4): 1276-1283. https://dx.doi.org/10.1128/AEM.01750-10, more Margesin, R.; Feller, G. (2010). Biotechnological applications of psychrophiles. Environ. Technol. 31(8-9): 835-844. https://dx.doi.org/10.1080/09593331003663328, more Piette, F.; D'Amico, S.; Struvay, C.; Mazzucchelli, G.; Renaut, J.; Tutino, M.L.; Danchin, A.; Leprince, P.; Feller, G. (2010). Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125. Mol. Microbiol. 76(1): 120-132. dx.doi.org/10.1111/j.1365-2958.2010.07084.x, more Huston, A.L.; Haeggstrom, J.; Feller, G. (2008). Cold adaptation of enzymes: Structural, kinetic and microcalorimetric characterizations of an aminopeptidase from the Arctic psychrophile Colwellia psychrerythraea and of human leukotriene A₄ hydrolase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1784(11): 1865-1872. https://dx.doi.org/10.1016/j.bbapap.2008.06.002, more Marx, J.-C.; Collins, T.; D'Amico, S.; Feller, G.; Gerday, C. (2007). Cold-adapted enzymes from marine Antarctic microorganisms. Mar. Biotechnol. 9(3): 293-304. dx.doi.org/10.1007/s10126-006-6103-8, more Srimathi, S.; Jayaraman, G.; Feller, G.; Danielsson, B.; Narayanan, P.R. (2007). Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis. Extremophiles 11(3): 505-515. https://dx.doi.org/10.1007/s00792-007-0062-5, more De Vos, D.; Collins, T.; Nerinckx, W.; Savvides, S.N.; Claeyssens, M.; Gerday, C.; Feller, G.; Van Beeumen, J. (2006). Oligosaccharide binding in family 8 glycosidases: Crystal structures of active-site mutants of the β-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product. Biochemistry (Wash.) 45(15): 4797-4807. https://dx.doi.org/10.1021/bi052193e, more Siddiqui, K.S.; Poljak, A.; Guilhaus, M.; De Francisci, D.; Curmi, P.M.G.; Feller, G.; D'Amico, S.; Gerday, C.; Uversky, V.N.; Cavicchioli, R. (2006). Role of lysine versus arginine in enzyme cold-adaptation: modifying lysine to homo-arginine stabilizes the cold-adapted α-amylase from Pseudoalteramonas haloplanktis. Proteins-Structure Function and Bioinformatics 64(2): 486-501. https://dx.doi.org/10.1002/prot.20989, more Médigue, C.; Krin, E.; Pascal, G.; Barbe, V.; Bernsel, A.; Bertin, P.N.; Cheung, F.; Cruveiller, S.; D'Amico, S.; Duilio, A.; Fang, G.; Feller, G.; Ho, C.; Mangenot, S.; Marino, G.; Nilsson, J.; Parrilli, E.; Rocha, E.P.C.; Rouy, Z.; Sekowska, A.; Tutino, M.L.; Vallenet, D.; von Heijne, G.; Danchin, A. (2005). Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125. Genome Research 15(10): 1325-1335. dx.doi.org/10.1101/gr.4126905, more Siddiqui, K.S.; Feller, G.; D'Amico, S.; Gerday, C.; Giaquinto, L.; Cavicchioli, R. (2005). The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted α-amylase. J. Bacteriol. 187(17): 6197-6205. dx.doi.org/10.1128/JB.187.17.6197-6205.2005, more Siddiqui, K.S.; Poljak, A.; Guilhaus, M.; Feller, G.; D'Amico, S.; Gerday, C.; Cavicchioli, R. (2005). Role of disulfide bridges in the activity and stability of a cold-active α-amylase. J. Bacteriol. 187(17): 6206-6212. dx.doi.org/10.1128/JB.187.17.6206-6212.2005, more Violot, S.; Aghajari, N.; Czjzek, M.; Feller, G.; Sonan, G.K.; Gouet, P.; Gerday, C.; Haser, R.; Receveur-Bréchot, V. (2005). Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering. J. Mol. Biol. 348(5): 1211-1224. https://dx.doi.org/10.1016/j.jmb.2005.03.026, more Garsoux, G.; Lamotte, J.; Gerday, C.; Feller, G. (2004). Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis. Biochem. J. 384(2): 247-253. https://dx.doi.org/10.1042/BJ20040325, more Claverie, P.; Vigano, C.; Ruysschaert, J.-M.; Gerday, C.; Feller, G. (2003). The precursor of a psychrophilic α-amylase: structural characterization and insights into cold adaptation. Biochimica et Biophysica Acta-Proteins and Proteomics 1649(2): 119-122. https://dx.doi.org/10.1016/S1570-9639(03)00184-5, more Van Petegem, F.; Collins, T.; Meuwis, M.-A.; Gerday, C.; Feller, G.; Van Beeumen, J. (2003). The structure of a cold-adapted family 8 xylanase at 1.3 angstrom resolution - Structural adaptations to cold and investigation of the active site. J. Biol. Chem. 278(9): 7531-7539. https://dx.doi.org/10.1074/jbc.M206862200, more Violot, S.; Haser, R.; Sonan, G.; Georlette, D.; Feller, G.; Aghajari, N. (2003). Expression, purification, crystallization and preliminary X-ray crystallographic studies of a psychrophilic cellulase from Pseudoalteromonas haloplanktis. Acta Crystallographica Section D-Structural Biology 59: 1256-1258. dx.doi.org/10.1107/S0907444903008849, more Xu, Y.; Feller, G.; Gerday, C.; Glansdorff, N. (2003). Moritella cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature? J. Bacteriol. 185(18): 5519-5526. dx.doi.org/10.1128/JB.185.18.5519-5526.2003, more Aghajari, N.; Feller, G.; Gerday, C.; Haser, R. (2002). Structural basis of α-amylase activation by chloride. Protein Sci. 11(6): 1435-1441. dx.doi.org/10.1110/ps.0202602, more Collins, T.; Meuwis, M.-A.; Stals, I.; Claeyssens, M.; Feller, G.; Gerday, C. (2002). A novel family 8 xylanase, functional and physicochemical characterization. J. Biol. Chem. 277(38): 35133-35139. https://dx.doi.org/10.1074/jbc.M204517200, more D'Amico, S.; Claverie, P.; Collins, T.; Georlette, D.; Gratia, E.; Hoyoux, A.; Meuwis, M.-A.; Feller, G.; Gerday, C. (2002). Molecular basis of cold adaptation. Phil. Trans. R. Soc. Lond. (B Biol. Sci.) 357(1423): 917-924. dx.doi.org/10.1098/rstb.2002.1105, more D'Amico, S.; Gerday, C.; Feller, G. (2002). Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted α-amylase. J. Biol. Chem. 277(48): 46110-46115. https://dx.doi.org/10.1074/jbc.M207253200, more Tutino, M.L.; Parrilli, E.; Giaquinto, L.; Duilio, A.; Sannia, G.; Feller, G.; Marino, G. (2002). Secretion of α-amylase from Pseudoalteromonas haloplanktis TAB23: two different pathways in different hosts. J. Bacteriol. 184(20): 5814-5817. dx.doi.org/10.1128/JB.184.20.5814-5817.2002, more Van Petegem, F.; Collins, T.; Meuwis, M.A.; Gerday, C.; Feller, G.; Van Beeumen, J. (2002). Crystallization and preliminary X-ray analysis of a xylanase from the psychrophile Pseudoalteromonas haloplanktis. Acta Crystallographica Section D-Structural Biology 58: 1494-1496. dx.doi.org/10.1107/S0907444902011666, more Hoyoux, A.; Jennes, I.; Dubois, P.; Genicot, S.; Dubail, F.; François, J.-M.; Baise, E.; Feller, G.; Gerday, C. (2001). Cold-adapted β-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis. Appl. Environ. Microbiol. 67(4): 1529-1535. dx.doi.org/10.1128/AEM.67.4.1529-1535.2001, more Feller, G.; Gerday, C. (1997). Adaptations of the hemoglobinless Antarctic icefish (Channichthyidae) to hypoxia tolerance. Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. 118(4): 981-987. https://dx.doi.org/10.1016/S0300-9629(97)86786-2, more Laforet, C.; Feller, G.; Narinx, E.; Gerday, C. (1991). Parvalbumin in the cardiac muscle of normal and haemoglobin-myoglobin-free antarctic fish. Journal of Muscle Research and Cell Motility 12(5): 472-478. https://dx.doi.org/10.1007/BF01738332, more Feller, G.; Gerday, C. (1987). Metabolic pattern of the heart of haemoglobin- and myoglobin-free Antarctic fish Channichthys rhinoceratus. Polar Biol. 7(4): 225-229. https://dx.doi.org/10.1007/BF00287418, more Feller, G.; Goessens, G.; Gerday, C.; Bassleer, R. (1985). Heart structure and ventricular ultrastructure of hemoglobin- and myoglobin-free icefish Channichthys rhinoceratus. Cell Tissue Res. 242(3): 669-676. https://dx.doi.org/10.1007/BF00225436, more Feller, G.; Bassleer, R.; Goessens, G.; Hamoir, G. (1983). Relative size and myocardial structure of the heart of an Antarctic fish devoid of haemoglobin and myoglobin, Channichthys rhinoceratus. J. Zool. (1987) 199(1): 51-57. https://dx.doi.org/10.1111/j.1469-7998.1983.tb06116.x, more
Peer reviewed publications (5) [show]
Feller, G.; Poncin, A.; Aittaleb, M.; Schyns, R.; Gerday, C. (1994). The blood proteins of the Antarctic icefish Channichthys rhinoceratus: biological significance and purification of the two main components. Comp. Biochem. Physiol., B Comp. Biochem. 109(1): 89-97. https://dx.doi.org/10.1016/0305-0491(94)90145-7, more Feller, G.; D'Haese, J.; Gerday, C. (1990). Tropomyosin from the striated muscles of carp (Cyprinus carpio) and of icefish (Channichthys rhinoceratus). Arch. Int. Phys. Bioch. 98(2): 297-305. https://dx.doi.org/10.3109/13813459009113990, more Feller, G.; Gerday, C. (1989). Troponin C of the Antarctic icefish (Champsocephalus gunnari) white muscle. Comp. Biochem. Physiol., B Comp. Biochem. 94(4): 769-773. https://dx.doi.org/10.1016/0305-0491(89)90163-6, more Genicot, S.; Feller, G.; Gerday, C. (1988). Trypsin from Antarctic fish (Paranotothenia magellanica forster) as compared with trout (Salmo gairdneri) trypsin. Comp. Biochem. Physiol., B Comp. Biochem. 90(3): 601-609. https://dx.doi.org/10.1016/0305-0491(88)90301-X, more Feller, G.; Pequeux, A.; Hamoir, G. (1981). La présence d'anhydrase carbonique chez 2 poissons de l'archipel des Kerguelen, Channichthys rhinoceratus exempt d'hémoglobine er Notothenia magellanica de formule sanguine normale. C. R. Acad. Sci., Sér. 3 Sci. Vie 293(7): 395-397, more

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