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Phenoloxidase activity and thermostability of <i>Cancer pagurus</i> and <i>Limulus polyphemus</i> hemocyanin. <i>Comp. Biochem. Physiol. (B Biochem. Mol. Biol.) 164(3)</i>: 201-209. <a href=\"https://dx.doi.org/10.1016/j.cbpb.2012.12.007\" target=\"_blank\">https://dx.doi.org/10.1016/j.cbpb.2012.12.007</a>","AutID":225371,"MonDate":null,"AnaDate":2013,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":257490,"RR":"<b>Idakieva, K.; Meersman, F.; Gielens, C.</b> (2012). Reversible heat inactivation of copper sites precedes thermal unfolding of molluscan (<i>Rapana thomasiana</i>) hemocyanin. <i>Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1824(5)</i>: 731-738. <a href=\"http://dx.doi.org/10.1016/j.bbapap.2012.03.002\" target=\"_blank\">dx.doi.org/10.1016/j.bbapap.2012.03.002</a>","AutID":225371,"MonDate":null,"AnaDate":2012,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280784,"RR":"<b>Idakieva, K.; Siddiqui, N.I.; Meersman, F.; De Maeyer, M.; Chakarska, I.; Gielens, C.</b> (2009). Influence of limited proteolysis, detergent treatment and lyophilization on the phenoloxidase activity of <i>Rapana thomasiana</i> hemocyanin. <i>International Journal of Biological Macromolecules 45(2)</i>: 181-187. <a href=\"https://dx.doi.org/10.1016/j.ijbiomac.2009.04.022\" target=\"_blank\">https://dx.doi.org/10.1016/j.ijbiomac.2009.04.022</a>","AutID":241176,"MonDate":null,"AnaDate":2009,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280854,"RR":"<b>Gielens, C.; Idakieva, K.; De Maeyer, M.; Van den Bergh, V.; Siddiqui, N.I.; Compernolle, F.</b> (2007). Conformational stabilization at the active site of molluskan (<i>Rapana thomasiana</i>) hemocyanin by a cysteine-histidine thioether bridge - A study by mass spectrometry and molecular modeling. <i>Peptides (New York, NY : 1980) 28(4)</i>: 790-797. <a href=\"https://dx.doi.org/10.1016/j.peptides.2006.12.004\" target=\"_blank\">https://dx.doi.org/10.1016/j.peptides.2006.12.004</a>","AutID":239482,"MonDate":null,"AnaDate":2007,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280834,"RR":"<b>Siddiqui, N.I.; Idakieva, K.; Demarsin, B.; Doumanova, L.; Compernolle, F.; Gielens, C.</b> (2007). Involvement of glycan chains in the antigenicity of <i>Rapana thomasiana</i> hemocyanin. <i>Biochem. Biophys. Res. Commun. 361(3)</i>: 705-711. <a href=\"https://dx.doi.org/10.1016/j.bbrc.2007.07.098\" target=\"_blank\">https://dx.doi.org/10.1016/j.bbrc.2007.07.098</a>","AutID":239482,"MonDate":null,"AnaDate":2007,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280936,"RR":"<b>Gielens, C.; Idakieva, K.; Van den Bergh, V.; Siddiqui, N.I.; Parvanova, K.; Compernolle, F.</b> (2005). Mass spectral evidence for <i>N</i>-glycans with branching on fucose in a molluscan hemocyanin. <i>Biochem. Biophys. Res. Commun. 331(2)</i>: 562-570. <a href=\"https://dx.doi.org/10.1016/j.bbrc.2005.03.217\" target=\"_blank\">https://dx.doi.org/10.1016/j.bbrc.2005.03.217</a>","AutID":239482,"MonDate":null,"AnaDate":2005,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281006,"RR":"<b>Gielens, C.; De Geest, N.; Compernolle, F.; Préaux, G.</b> (2004). Glycosylation sites of hemocyanins of <i>Helix pomatia</i> and <i>Sepia officinalis</i>. <i>Micron 35(1-2)</i>: 99-100. <a href=\"https://dx.doi.org/10.1016/j.micron.2003.10.031\" target=\"_blank\">https://dx.doi.org/10.1016/j.micron.2003.10.031</a>","AutID":239482,"MonDate":null,"AnaDate":2004,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281152,"RR":"<b>Lamy, J.; Gielens, C.; Lambert, O.; Taveau, J.C.; Motta, G.; Loncke, P.; Degeest, N.; Preaux, G.</b> (1993). Further approaches to the quaternary structure of <i>Octopus</i> hemocyanin: a model based on immunoelectron microscopy and image processing. <i>Arch. Biochem. Biophys. 305(1)</i>: 17-29. <a href=\"https://dx.doi.org/10.1006/abbi.1993.1388\" target=\"_blank\">https://dx.doi.org/10.1006/abbi.1993.1388</a>","AutID":242771,"MonDate":null,"AnaDate":1993,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":262161,"RR":"<b>Wichertjes, T.; Gielens, C.; Schutter, W.G.; Préaux, G.; Lontie, R.; van Bruggen, E.F.J.</b> (1986). The quaternary structure of <i>Sepia officinalis</i> haemocyanin. <i>Biochim. Biophys. Acta 872(3)</i>: 183-194. <a href=\"https://dx.doi.org/10.1016/0167-4838(86)90270-0\" target=\"_blank\">https://dx.doi.org/10.1016/0167-4838(86)90270-0</a>","AutID":239482,"MonDate":null,"AnaDate":1986,"PeerRev":1,"outputType":"1_A1","OpenAcc":0}],"PeerRevRef":[{"BRefID":280356,"RR":"<b>Bosman, F.; Gielens, C.; Preaux, G.; Lontie, R.</b> (1982). Limited proteolysis of haemocyanin of <i>Sepia officinalis</i>. <i>Arch. Int. Phys. Bioch. 90(3)</i>: B94-B95. <a href=\"http://dx.doi.org/10.3109/13813458209070573\" target=\"_blank\">http://dx.doi.org/10.3109/13813458209070573</a>","AutID":242771,"MonDate":null,"AnaDate":1982,"PeerRev":1,"outputType":"2_PeerRevRef","OpenAcc":0},{"BRefID":280360,"RR":"<b>Lips, D.; Gielens, C.; Preaux, G.; Lontie, R.</b> (1982). Evidence for two types of polypeptide chains in the haemocyanin of <i>Buccinum undatum</i>. <i>Arch. Int. Phys. Bioch. 90(3)</i>: B128-B128. <a href=\"http://dx.doi.org/10.3109/13813458209070573\" target=\"_blank\">http://dx.doi.org/10.3109/13813458209070573</a>","AutID":242771,"MonDate":null,"AnaDate":1982,"PeerRev":1,"outputType":"2_PeerRevRef","OpenAcc":0}]},"urls":null,"spcols":null,"thesterms":null,"taxterms":null,"pub":1,"newses":{"SesID":83452,"LoginName":"VLIZ2000\\zohrab","LoginID":435,"DD":"2017-01-18"},"updses":{"SesID":83452,"LoginName":"VLIZ2000\\zohrab","LoginID":435,"DD":"2017-01-18"},"urlmaps":[],"resmessage":"no id specified","complete":1}