| Institute |
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Katholieke Universiteit Leuven; Departement Chemie; Afdeling biochemie, moleculaire en structurele biologie, more
Institutional address:
Celestijnenlaan 200G
3001 Heverlee
Belgium
Tel.: +32-(0)16-32 73 42
Fax: +32-(0)16-32 79 74
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| Publications (11) |
Top | Institute | Publications |
| A1 Publications (9) [show] |
- Idakieva, K.; Raynova, Y.; Meersman, F.; Gielens, C. (2013). Phenoloxidase activity and thermostability of Cancer pagurus and Limulus polyphemus hemocyanin. Comp. Biochem. Physiol. (B Biochem. Mol. Biol.) 164(3): 201-209. https://dx.doi.org/10.1016/j.cbpb.2012.12.007, more
- Idakieva, K.; Meersman, F.; Gielens, C. (2012). Reversible heat inactivation of copper sites precedes thermal unfolding of molluscan (Rapana thomasiana) hemocyanin. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1824(5): 731-738. dx.doi.org/10.1016/j.bbapap.2012.03.002, more
- Idakieva, K.; Siddiqui, N.I.; Meersman, F.; De Maeyer, M.; Chakarska, I.; Gielens, C. (2009). Influence of limited proteolysis, detergent treatment and lyophilization on the phenoloxidase activity of Rapana thomasiana hemocyanin. International Journal of Biological Macromolecules 45(2): 181-187. https://dx.doi.org/10.1016/j.ijbiomac.2009.04.022, more
- Gielens, C.; Idakieva, K.; De Maeyer, M.; Van den Bergh, V.; Siddiqui, N.I.; Compernolle, F. (2007). Conformational stabilization at the active site of molluskan (Rapana thomasiana) hemocyanin by a cysteine-histidine thioether bridge - A study by mass spectrometry and molecular modeling. Peptides (New York, NY : 1980) 28(4): 790-797. https://dx.doi.org/10.1016/j.peptides.2006.12.004, more
- Siddiqui, N.I.; Idakieva, K.; Demarsin, B.; Doumanova, L.; Compernolle, F.; Gielens, C. (2007). Involvement of glycan chains in the antigenicity of Rapana thomasiana hemocyanin. Biochem. Biophys. Res. Commun. 361(3): 705-711. https://dx.doi.org/10.1016/j.bbrc.2007.07.098, more
- Gielens, C.; Idakieva, K.; Van den Bergh, V.; Siddiqui, N.I.; Parvanova, K.; Compernolle, F. (2005). Mass spectral evidence for N-glycans with branching on fucose in a molluscan hemocyanin. Biochem. Biophys. Res. Commun. 331(2): 562-570. https://dx.doi.org/10.1016/j.bbrc.2005.03.217, more
- Gielens, C.; De Geest, N.; Compernolle, F.; Préaux, G. (2004). Glycosylation sites of hemocyanins of Helix pomatia and Sepia officinalis. Micron 35(1-2): 99-100. https://dx.doi.org/10.1016/j.micron.2003.10.031, more
- Lamy, J.; Gielens, C.; Lambert, O.; Taveau, J.C.; Motta, G.; Loncke, P.; Degeest, N.; Preaux, G. (1993). Further approaches to the quaternary structure of Octopus hemocyanin: a model based on immunoelectron microscopy and image processing. Arch. Biochem. Biophys. 305(1): 17-29. https://dx.doi.org/10.1006/abbi.1993.1388, more
- Wichertjes, T.; Gielens, C.; Schutter, W.G.; Préaux, G.; Lontie, R.; van Bruggen, E.F.J. (1986). The quaternary structure of Sepia officinalis haemocyanin. Biochim. Biophys. Acta 872(3): 183-194. https://dx.doi.org/10.1016/0167-4838(86)90270-0, more
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| Peer reviewed publications (2) [show] |
- Bosman, F.; Gielens, C.; Preaux, G.; Lontie, R. (1982). Limited proteolysis of haemocyanin of Sepia officinalis. Arch. Int. Phys. Bioch. 90(3): B94-B95. http://dx.doi.org/10.3109/13813458209070573, more
- Lips, D.; Gielens, C.; Preaux, G.; Lontie, R. (1982). Evidence for two types of polypeptide chains in the haemocyanin of Buccinum undatum. Arch. Int. Phys. Bioch. 90(3): B128-B128. http://dx.doi.org/10.3109/13813458209070573, more
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