{"personrec":{"StatusID":1,"PersStatus":null,"Status":"Valid","PersID":15566,"PersName":"Feller, Georges","PublicFlag":1,"CheckedFlag":0,"Surname":"Feller","Firstname":"Georges","Initials":"G.","AddressedAs":null,"Function":null,"DateLastModified":{"date":"2023-05-02 10:08:18.393000","timezone_type":1,"timezone":"+00:00"},"PersTitle":null,"PersStatusID":null,"AbstractEnglish":null,"AbstractOtherLang":null,"AbstractLangCode":null,"AbstractLangID":null,"AutID":75559,"ND":"2007-08-29","UD":"2007-08-29"},"loaninfo":null,"pictures":[],"institutes":[{"instituterec":{"OrderNr":1,"Acronym":"ULG","ENFunction":null,"InsIDtmp":467,"OrigNameLangCode":null,"OrigNameLangID":null,"FullOrigName":null,"InsID":467,"Function":null,"BeginDay":null,"BeginMonth":null,"BeginYear":null,"Begindate":"","Enddate":"","PIAdrID":136705,"AdrID":111546,"Line1":null,"Line2":null,"Line3":null,"Line4":null,"Phone":"+32-(0)4-366 33 43","GSM":null,"Email":"gfeller@ulg.ac.be","EnvName":"Belgium","EncAddress":"Sart Tilman B5, 4000 Liège, Belgium","FullStandardName":"Université de Liège","DirectorFlag":null,"MarineSciFlag":null,"SpecializedFlag":null},"parent":null,"institutes":null,"references":null,"conferences":null,"datasets":null,"persons":null,"pastpers":null,"subpers":null,"projects":null,"urls":null,"pictures":null,"published":null,"affrefs":null,"collections":null,"thesterms":null,"taxterms":null,"geoterms":null,"thestermsFRIS":null,"nXtins":null,"previns":null,"spcols":null,"resmessage":"no id specified","complete":0,"participantrec":null,"peerrevs":null,"urlmaps":null}],"pastins":[],"projects":[{"ProID":3282,"Acronym":"BE_POLES","Progress":"Completed","StandardTitle":"Belgian Polar Research Cluster","BeginYear":2003,"EndYear":2006},{"ProID":2147,"Acronym":"BE-POLES","Progress":"Completed","StandardTitle":"OA-CL-016 BE-POLES: Belgische Polaire onderzoekscluster","BeginYear":2003,"EndYear":2006}],"datasets":null,"references":{"A1":[{"BRefID":311464,"RR":"<b>Feller, G.</b> (2018). Protein folding at extreme temperatures: current issues. <i>Seminars in Cell & Developmental Biology 84</i>: 129-137. <a href=\"https://dx.doi.org/10.1016/j.semcdb.2017.09.003\" target=\"_blank\">https://dx.doi.org/10.1016/j.semcdb.2017.09.003</a>","AutID":378412,"MonDate":null,"AnaDate":2018,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280655,"RR":"<b>Godin-Roulling, A.; Schmidpeter, P.A.M.; Schmid, F.X.; Feller, G.</b> (2015). Functional adaptations of the bacterial chaperone trigger factor to extreme environmental temperatures. <i>Environ. Microbiol. 17(7)</i>: 2407-2420. <a href=\"http://dx.doi.org/10.1111/1462-2920.12707\" target=\"_blank\">dx.doi.org/10.1111/1462-2920.12707</a>","AutID":219792,"MonDate":null,"AnaDate":2015,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":256767,"RR":"<b>Papa, R; Selan, L; Parrilli, E; Tilotta, M; Sannino, F; Feller, G.; Tutino, L; Artini, M</b> (2015). Anti-biofilm activities from marine cold adapted bacteria against Staphylococci and <i>Pseudomonas aeruginosa</i>. <i>Front. Microbiol. 6</i>: 10 pp. <a href=\"http://dx.doi.org/10.3389/fmicb.2015.01333\" target=\"_blank\">dx.doi.org/10.3389/fmicb.2015.01333</a>","AutID":219792,"MonDate":null,"AnaDate":2015,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":280688,"RR":"<b>Struvay, C.; Negro, S.; Matagne, A.; Feller, G.</b> (2013). Energetics of protein stability at extreme environmental temperatures in bacterial trigger factors. <i>Biochemistry (Wash.) 52(17)</i>: 2982-2990. <a href=\"http://dx.doi.org/10.1021/bi4002387\" target=\"_blank\">dx.doi.org/10.1021/bi4002387</a>","AutID":219792,"MonDate":null,"AnaDate":2013,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280712,"RR":"<b>Piette, F.; Leprince, P.; Feller, G.</b> (2012). Is there a cold shock response in the Antarctic psychrophile <i>Pseudoalteromonas haloplanktis</i>? <i>Extremophiles 16(4)</i>: 681-683. <a href=\"https://dx.doi.org/10.1007/s00792-012-0456-x\" target=\"_blank\">https://dx.doi.org/10.1007/s00792-012-0456-x</a>","AutID":240699,"MonDate":null,"AnaDate":2012,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280707,"RR":"<b>Struvay, C.; Feller, G.</b> (2012). Optimization to low temperature activity in psychrophilic enzymes. <i>International Journal of Molecular Sciences 13(9)</i>: 11643-11665. <a href=\"https://dx.doi.org/10.3390/ijms130911643\" target=\"_blank\">https://dx.doi.org/10.3390/ijms130911643</a>","AutID":219792,"MonDate":null,"AnaDate":2012,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":280731,"RR":"<b>Piette, F.; Struvay, C.; Feller, G.</b> (2011). The protein folding challenge in psychrophiles: facts and current issues. <i>Environ. Microbiol. 13(8)</i>: 1924-1933. <a href=\"http://dx.doi.org/10.1111/j.1462-2920.2011.02436.x\" target=\"_blank\">dx.doi.org/10.1111/j.1462-2920.2011.02436.x</a>","AutID":219792,"MonDate":null,"AnaDate":2011,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280736,"RR":"<b>Piette, F.; D'Amico, S.; Mazzucchelli, G.; Danchin, A.; Leprince, P.; Feller, G.</b> (2011). Life in the cold: a proteomic study of cold-repressed proteins in the Antarctic bacterium <i>Pseudoalteromonas haloplanktis</i> TAC125. <i>Appl. Environ. Microbiol. 77(11)</i>: 3881-3883. <a href=\"http://dx.doi.org/10.1128/AEM.02757-10\" target=\"_blank\">dx.doi.org/10.1128/AEM.02757-10</a>","AutID":219792,"MonDate":null,"AnaDate":2011,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":296035,"RR":"<b>Wilmes, B.; Kock, H.; Glagla, S.; Albrecht, D.; Voigt, B.; Markert, S.; Gardebrecht, A.; Bode, R.; Danchin, A.; Feller, G.; Hecker, M.; Schweder, T.</b> (2011). Cytoplasmic and periplasmic signatures of exponentially growing cells of the psychrophilic bacterium <i>Pseudoalteromonas haloplanktis</i> TAC125. <i>Appl. Environ. Microbiol. 77(4)</i>: 1276-1283. <a href=\"https://dx.doi.org/10.1128/AEM.01750-10\" target=\"_blank\">https://dx.doi.org/10.1128/AEM.01750-10</a>","AutID":328550,"MonDate":null,"AnaDate":2011,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":280775,"RR":"<b>Margesin, R.; Feller, G.</b> (2010). Biotechnological applications of psychrophiles. <i>Environ. Technol. 31(8-9)</i>: 835-844. <a href=\"https://dx.doi.org/10.1080/09593331003663328\" target=\"_blank\">https://dx.doi.org/10.1080/09593331003663328</a>","AutID":219792,"MonDate":null,"AnaDate":2010,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280771,"RR":"<b>Piette, F.; D'Amico, S.; Struvay, C.; Mazzucchelli, G.; Renaut, J.; Tutino, M.L.; Danchin, A.; Leprince, P.; Feller, G.</b> (2010). Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium <i>Pseudoalteromonas haloplanktis</i> TAC125. <i>Mol. Microbiol. 76(1)</i>: 120-132. <a href=\"http://dx.doi.org/10.1111/j.1365-2958.2010.07084.x\" target=\"_blank\">dx.doi.org/10.1111/j.1365-2958.2010.07084.x</a>","AutID":219792,"MonDate":null,"AnaDate":2010,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":257995,"RR":"<b>Huston, A.L.; Haeggstrom, J.; Feller, G.</b> (2008). Cold adaptation of enzymes: Structural, kinetic and microcalorimetric characterizations of an aminopeptidase from the Arctic psychrophile <i>Colwellia psychrerythraea</i> and of human leukotriene A<sub>4</sub> hydrolase. <i>Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1784(11)</i>: 1865-1872. <a href=\"https://dx.doi.org/10.1016/j.bbapap.2008.06.002\" target=\"_blank\">https://dx.doi.org/10.1016/j.bbapap.2008.06.002</a>","AutID":228270,"MonDate":null,"AnaDate":2008,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":113496,"RR":"<b>Marx, J.-C.; Collins, T.; D'Amico, S.; Feller, G.; Gerday, C.</b> (2007). Cold-adapted enzymes from marine Antarctic microorganisms. <i>Mar. Biotechnol. 9(3)</i>: 293-304. <a href=\"http://dx.doi.org/10.1007/s10126-006-6103-8\" target=\"_blank\">dx.doi.org/10.1007/s10126-006-6103-8</a>","AutID":75559,"MonDate":null,"AnaDate":2007,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280847,"RR":"<b>Srimathi, S.; Jayaraman, G.; Feller, G.; Danielsson, B.; Narayanan, P.R.</b> (2007). Intrinsic halotolerance of the psychrophilic alpha-amylase from <i>Pseudoalteromonas haloplanktis</i>. <i>Extremophiles 11(3)</i>: 505-515. <a href=\"https://dx.doi.org/10.1007/s00792-007-0062-5\" target=\"_blank\">https://dx.doi.org/10.1007/s00792-007-0062-5</a>","AutID":242495,"MonDate":null,"AnaDate":2007,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280896,"RR":"<b>De Vos, D.; Collins, T.; Nerinckx, W.; Savvides, S.N.; Claeyssens, M.; Gerday, C.; Feller, G.; Van Beeumen, J.</b> (2006). Oligosaccharide binding in family 8 glycosidases: Crystal structures of active-site mutants of the β-1,4-xylanase pXyl from <i>Pseudoaltermonas haloplanktis</i> TAH3a in complex with substrate and product. <i>Biochemistry (Wash.) 45(15)</i>: 4797-4807. <a href=\"https://dx.doi.org/10.1021/bi052193e\" target=\"_blank\">https://dx.doi.org/10.1021/bi052193e</a>","AutID":242619,"MonDate":null,"AnaDate":2006,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280888,"RR":"<b>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.</b> (2006). Role of lysine versus arginine in enzyme cold-adaptation: modifying lysine to homo-arginine stabilizes the cold-adapted α-amylase from <i>Pseudoalteramonas haloplanktis</i>. <i>Proteins-Structure Function and Bioinformatics 64(2)</i>: 486-501. <a href=\"https://dx.doi.org/10.1002/prot.20989\" target=\"_blank\">https://dx.doi.org/10.1002/prot.20989</a>","AutID":242495,"MonDate":null,"AnaDate":2006,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280923,"RR":"<b>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.</b> (2005). Coping with cold: the genome of the versatile marine Antarctica bacterium <i>Pseudoalteromonas haloplanktis</i> TAC125. <i>Genome Research 15(10)</i>: 1325-1335. <a href=\"http://dx.doi.org/10.1101/gr.4126905\" target=\"_blank\">dx.doi.org/10.1101/gr.4126905</a>","AutID":242495,"MonDate":null,"AnaDate":2005,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280927,"RR":"<b>Siddiqui, K.S.; Feller, G.; D'Amico, S.; Gerday, C.; Giaquinto, L.; Cavicchioli, R.</b> (2005). The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted α-amylase. <i>J. Bacteriol. 187(17)</i>: 6197-6205. <a href=\"http://dx.doi.org/10.1128/JB.187.17.6197-6205.2005\" target=\"_blank\">dx.doi.org/10.1128/JB.187.17.6197-6205.2005</a>","AutID":242495,"MonDate":null,"AnaDate":2005,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280928,"RR":"<b>Siddiqui, K.S.; Poljak, A.; Guilhaus, M.; Feller, G.; D'Amico, S.; Gerday, C.; Cavicchioli, R.</b> (2005). Role of disulfide bridges in the activity and stability of a cold-active α-amylase. <i>J. Bacteriol. 187(17)</i>: 6206-6212. <a href=\"http://dx.doi.org/10.1128/JB.187.17.6206-6212.2005\" target=\"_blank\">dx.doi.org/10.1128/JB.187.17.6206-6212.2005</a>","AutID":242495,"MonDate":null,"AnaDate":2005,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280940,"RR":"<b>Violot, S.; Aghajari, N.; Czjzek, M.; Feller, G.; Sonan, G.K.; Gouet, P.; Gerday, C.; Haser, R.; Receveur-Bréchot, V.</b> (2005). Structure of a full length psychrophilic cellulase from <i>Pseudoalteromonas haloplanktis</i> revealed by X-ray diffraction and small angle X-ray scattering. <i>J. Mol. Biol. 348(5)</i>: 1211-1224. <a href=\"https://dx.doi.org/10.1016/j.jmb.2005.03.026\" target=\"_blank\">https://dx.doi.org/10.1016/j.jmb.2005.03.026</a>","AutID":242495,"MonDate":null,"AnaDate":2005,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280965,"RR":"<b>Garsoux, G.; Lamotte, J.; Gerday, C.; Feller, G.</b> (2004). Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium <i>Pseudoalteromonas haloplanktis</i>. <i>Biochem. J. 384(2)</i>: 247-253. <a href=\"https://dx.doi.org/10.1042/BJ20040325\" target=\"_blank\">https://dx.doi.org/10.1042/BJ20040325</a>","AutID":242495,"MonDate":null,"AnaDate":2004,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281026,"RR":"<b>Claverie, P.; Vigano, C.; Ruysschaert, J.-M.; Gerday, C.; Feller, G.</b> (2003). The precursor of a psychrophilic α-amylase: structural characterization and insights into cold adaptation. <i>Biochimica et Biophysica Acta-Proteins and Proteomics 1649(2)</i>: 119-122. <a href=\"https://dx.doi.org/10.1016/S1570-9639(03)00184-5\" target=\"_blank\">https://dx.doi.org/10.1016/S1570-9639(03)00184-5</a>","AutID":242495,"MonDate":null,"AnaDate":2003,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281039,"RR":"<b>Van Petegem, F.; Collins, T.; Meuwis, M.-A.; Gerday, C.; Feller, G.; Van Beeumen, J.</b> (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. <i>J. Biol. Chem. 278(9)</i>: 7531-7539. <a href=\"https://dx.doi.org/10.1074/jbc.M206862200\" target=\"_blank\">https://dx.doi.org/10.1074/jbc.M206862200</a>","AutID":242495,"MonDate":null,"AnaDate":2003,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281027,"RR":"<b>Violot, S.; Haser, R.; Sonan, G.; Georlette, D.; Feller, G.; Aghajari, N.</b> (2003). Expression, purification, crystallization and preliminary X-ray crystallographic studies of a psychrophilic cellulase from <i>Pseudoalteromonas haloplanktis</i>. <i>Acta Crystallographica Section D-Structural Biology 59</i>: 1256-1258. <a href=\"http://dx.doi.org/10.1107/S0907444903008849\" target=\"_blank\">dx.doi.org/10.1107/S0907444903008849</a>","AutID":242619,"MonDate":null,"AnaDate":2003,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281022,"RR":"<b>Xu, Y.; Feller, G.; Gerday, C.; Glansdorff, N.</b> (2003). <i>Moritella</i> cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature? <i>J. Bacteriol. 185(18)</i>: 5519-5526. <a href=\"http://dx.doi.org/10.1128/JB.185.18.5519-5526.2003\" target=\"_blank\">dx.doi.org/10.1128/JB.185.18.5519-5526.2003</a>","AutID":242495,"MonDate":null,"AnaDate":2003,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281067,"RR":"<b>Aghajari, N.; Feller, G.; Gerday, C.; Haser, R.</b> (2002). Structural basis of α-amylase activation by chloride. <i>Protein Sci. 11(6)</i>: 1435-1441. <a href=\"http://dx.doi.org/10.1110/ps.0202602\" target=\"_blank\">dx.doi.org/10.1110/ps.0202602</a>","AutID":242495,"MonDate":null,"AnaDate":2002,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281054,"RR":"<b>Collins, T.; Meuwis, M.-A.; Stals, I.; Claeyssens, M.; Feller, G.; Gerday, C.</b> (2002). A novel family 8 xylanase, functional and physicochemical characterization. <i>J. Biol. Chem. 277(38)</i>: 35133-35139. <a href=\"https://dx.doi.org/10.1074/jbc.M204517200\" target=\"_blank\">https://dx.doi.org/10.1074/jbc.M204517200</a>","AutID":242495,"MonDate":null,"AnaDate":2002,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281063,"RR":"<b>D'Amico, S.; Claverie, P.; Collins, T.; Georlette, D.; Gratia, E.; Hoyoux, A.; Meuwis, M.-A.; Feller, G.; Gerday, C.</b> (2002). Molecular basis of cold adaptation. <i>Phil. Trans. R. Soc. Lond. (B Biol. Sci.) 357(1423)</i>: 917-924. <a href=\"http://dx.doi.org/10.1098/rstb.2002.1105\" target=\"_blank\">dx.doi.org/10.1098/rstb.2002.1105</a>","AutID":242495,"MonDate":null,"AnaDate":2002,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281049,"RR":"<b>D'Amico, S.; Gerday, C.; Feller, G.</b> (2002). Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted α-amylase. <i>J. Biol. Chem. 277(48)</i>: 46110-46115. <a href=\"https://dx.doi.org/10.1074/jbc.M207253200\" target=\"_blank\">https://dx.doi.org/10.1074/jbc.M207253200</a>","AutID":242495,"MonDate":null,"AnaDate":2002,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281052,"RR":"<b>Tutino, M.L.; Parrilli, E.; Giaquinto, L.; Duilio, A.; Sannia, G.; Feller, G.; Marino, G.</b> (2002). Secretion of α-amylase from <i>Pseudoalteromonas haloplanktis</i> TAB23: two different pathways in different hosts. <i>J. Bacteriol. 184(20)</i>: 5814-5817. <a href=\"http://dx.doi.org/10.1128/JB.184.20.5814-5817.2002\" target=\"_blank\">dx.doi.org/10.1128/JB.184.20.5814-5817.2002</a>","AutID":242495,"MonDate":null,"AnaDate":2002,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281055,"RR":"<b>Van Petegem, F.; Collins, T.; Meuwis, M.A.; Gerday, C.; Feller, G.; Van Beeumen, J.</b> (2002). Crystallization and preliminary X-ray analysis of a xylanase from the psychrophile <i>Pseudoalteromonas haloplanktis</i>. <i>Acta Crystallographica Section D-Structural Biology 58</i>: 1494-1496. <a href=\"http://dx.doi.org/10.1107/S0907444902011666\" target=\"_blank\">dx.doi.org/10.1107/S0907444902011666</a>","AutID":242619,"MonDate":null,"AnaDate":2002,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281104,"RR":"<b>Hoyoux, A.; Jennes, I.; Dubois, P.; Genicot, S.; Dubail, F.; François, J.-M.; Baise, E.; Feller, G.; Gerday, C.</b> (2001). Cold-adapted β-galactosidase from the Antarctic psychrophile <i>Pseudoalteromonas haloplanktis</i>. <i>Appl. Environ. Microbiol. 67(4)</i>: 1529-1535. <a href=\"http://dx.doi.org/10.1128/AEM.67.4.1529-1535.2001\" target=\"_blank\">dx.doi.org/10.1128/AEM.67.4.1529-1535.2001</a>","AutID":242619,"MonDate":null,"AnaDate":2001,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":261842,"RR":"<b>Feller, G.; Gerday, C.</b> (1997). Adaptations of the hemoglobinless Antarctic icefish (Channichthyidae) to hypoxia tolerance. <i>Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. 118(4)</i>: 981-987. <a href=\"https://dx.doi.org/10.1016/S0300-9629(97)86786-2\" target=\"_blank\">https://dx.doi.org/10.1016/S0300-9629(97)86786-2</a>","AutID":242495,"MonDate":null,"AnaDate":1997,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":262059,"RR":"<b>Laforet, C.; Feller, G.; Narinx, E.; Gerday, C.</b> (1991). Parvalbumin in the cardiac muscle of normal and haemoglobin-myoglobin-free antarctic fish. <i>Journal of Muscle Research and Cell Motility 12(5)</i>: 472-478. <a href=\"https://dx.doi.org/10.1007/BF01738332\" target=\"_blank\">https://dx.doi.org/10.1007/BF01738332</a>","AutID":242619,"MonDate":null,"AnaDate":1991,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":262139,"RR":"<b>Feller, G.; Gerday, C.</b> (1987). Metabolic pattern of the heart of haemoglobin- and myoglobin-free Antarctic fish <i>Channichthys rhinoceratus</i>. <i>Polar Biol. 7(4)</i>: 225-229. <a href=\"https://dx.doi.org/10.1007/BF00287418\" target=\"_blank\">https://dx.doi.org/10.1007/BF00287418</a>","AutID":242619,"MonDate":null,"AnaDate":1987,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":262188,"RR":"<b>Feller, G.; Goessens, G.; Gerday, C.; Bassleer, R.</b> (1985). Heart structure and ventricular ultrastructure of hemoglobin- and myoglobin-free icefish <i>Channichthys rhinoceratus</i>. <i>Cell Tissue Res. 242(3)</i>: 669-676. <a href=\"https://dx.doi.org/10.1007/BF00225436\" target=\"_blank\">https://dx.doi.org/10.1007/BF00225436</a>","AutID":242495,"MonDate":null,"AnaDate":1985,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280352,"RR":"<b>Feller, G.; Bassleer, R.; Goessens, G.; Hamoir, G.</b> (1983). Relative size and myocardial structure of the heart of an Antarctic fish devoid of haemoglobin and myoglobin, <i>Channichthys rhinoceratus</i>. <i>J. Zool. (1987) 199(1)</i>: 51-57. <a href=\"https://dx.doi.org/10.1111/j.1469-7998.1983.tb06116.x\" target=\"_blank\">https://dx.doi.org/10.1111/j.1469-7998.1983.tb06116.x</a>","AutID":242619,"MonDate":null,"AnaDate":1983,"PeerRev":1,"outputType":"1_A1","OpenAcc":0}],"PeerRevRef":[{"BRefID":261975,"RR":"<b>Feller, G.; Poncin, A.; Aittaleb, M.; Schyns, R.; Gerday, C.</b> (1994). The blood proteins of the Antarctic icefish <i>Channichthys rhinoceratus</i>: biological significance and purification of the two main components. <i>Comp. Biochem. Physiol., B Comp. 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La présence d'anhydrase carbonique chez 2 poissons de l'archipel des Kerguelen, <i>Channichthys rhinoceratus</i> exempt d'hémoglobine er <i>Notothenia magellanica</i> de formule sanguine normale. <i>C. R. Acad. Sci., Sér. 3 Sci. Vie 293(7)</i>: 395-397","AutID":242495,"MonDate":null,"AnaDate":1981,"PeerRev":1,"outputType":"2_PeerRevRef","OpenAcc":0}]},"urls":null,"spcols":null,"thesterms":null,"taxterms":null,"pub":1,"newses":{"SesID":28209,"LoginName":"VLIZ2000\\ruthv","LoginID":79,"DD":"2007-08-29"},"updses":{"SesID":28209,"LoginName":"VLIZ2000\\ruthv","LoginID":79,"DD":"2007-08-29"},"urlmaps":[],"resmessage":"no id specified","complete":1}