Franse naam: Service de Biologie Cellulaire
Overkoepelend instituut: Université de Mons; Research Institute for Biosciences (Umons-IBS), meer
Adres: Bâtiment Pentagone
Avenue du Champ de Mars, 6 7000 Mons België
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1 Directeur: Hoofd van de onderzoeksgroep/afdeling 2 Mariene onderzoeker: Is werkzaam in deze groep en treedt op als (co)auteur in minstens één mariene publicatie in de laatste 5 jaar. 3 Gespecialiseerd personeel: Levert administratieve of technische ondersteuning aan het zeewetenschappelijk onderzoek.
Publicaties (12) |
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( 12 peer reviewed ) opsplitsen filter
Tilbury, M.A.; Tran, T.Q.; Shingare, D.; Lefevre, M.; Power, A.M.; Leclère, P.; Wall, J.G. (2023). Self-assembly of a barnacle cement protein into intertwined amyloid fibres and determination of their adhesive and viscoelastic properties. J. R. Soc. Interface 20(205): 20230332. https://dx.doi.org/10.1098/rsif.2023.0332, meer
Algrain, M.; Hennebert, E.; Bertemes, P.; Wattiez, R.; Flammang, P.; Lengerer, B. (2022). In the footsteps of sea stars: deciphering the catalogue of proteins involved in underwater temporary adhesion. Open Biology 12(8): 220103. https://dx.doi.org/10.1098/rsob.220103, meer
Bonneel, M.; Hennebert, E.; Aranko, A.S.; Hwang, D.S.; Lefevre, M.; Pommier, V.; Wattiez, R.; Delroisse, J.; Flammang, P. (2022). Molecular mechanisms mediating stiffening in the mechanically adaptable connective tissues of sea cucumbers. Matrix Biology 108: 39-54. https://dx.doi.org/10.1016/j.matbio.2022.02.006, meer
Davey, P.A.; Power, A.M.; Santos, R.; Bertemes, P.; Ladurner, P.; Palmowski, P.; Clarke, J.; Flammang, P.; Lengerer, B.; Hennebert, E.; Rothbächer, U.; Pjeta, R.; Wunderer, J.; Zurovec, M.; Aldred, N. (2021). Omics-based molecular analyses of adhesion by aquatic invertebrates. Biol. Rev. 96(3): 1051-1075. https://hdl.handle.net/10.1111/brv.12691, meer
Lefevre, M.; Ederth, T.; Masai, T.; Wattiez, R.; Leclère, P.; Flammang, P.; Hennebert, E. (2021). Disentangling the roles of functional domains in the aggregation and adsorption of the multimodular sea star adhesive protein Sfp1. Mar. Biotechnol. 23(5): 724-735. https://dx.doi.org/10.1007/s10126-021-10059-y, meer
Lefevre, M.; Tran, T.Q.; De Muijlder, T.; Pittenger, B.; Flammang, P.; Hennebert, E.; Leclère, P. (2021). On the nanomechanical and viscoelastic properties of coatings made of recombinant sea star adhesive proteins. Frontiers of Mechanical Engineering 7: 667491. https://dx.doi.org/10.3389/fmech.2021.667491, meer
Choi, J.; Hennebert, E.; Flammang, P.; Hwang, D.S. (2020). A sugar-lectin rich interface between soft tissue and the stiff byssus of Atrina pectinata. Biomaterials Science 8(13): 3751-3759. https://hdl.handle.net/10.1039/c9bm01932d, meer
Lefevre, M.; Flammang, P.; Aranko, A.S.; Linder, M.B.; Scheibel, T.; Humenik, M.; Leclercq, M.; Surin, M.; Tafforeau, L.; Wattiez, R.; Leclère, P.; Hennebert, E. (2020). Sea star-inspired recombinant adhesive proteins self-assemble and adsorb on surfaces in aqueous environments to form cytocompatible coatings. Acta Biomaterialia 112: 62-74. https://dx.doi.org/10.1016/j.actbio.2020.05.036, meer
Lengerer, B.; Algrain, M.; Lefevre, M.; Delroisse, J.; Hennebert, E.; Flammang, P. (2019). Interspecies comparison of sea star adhesive proteins. Phil. Trans. R. Soc. Lond. (B Biol. Sci.) 374(1784): 20190195. https://dx.doi.org/10.1098/rstb.2019.0195, meer
Hennebert, E.; Gregorowicz, E.; Flammang, P. (2018). Involvement of sulfated biopolymers in adhesive secretions produced by marine invertebrates. Biology Open 7(11): bio037358. https://dx.doi.org/10.1242/bio.037358, meer
Lengerer, B.; Bonneel, M.; Lefevre, M.; Hennebert, E.; Leclère, P.; Gosselin, E.; Ladurner, P.; Flammang, P. (2018). The structural and chemical basis of temporary adhesion in the sea star Asterina gibbosa. Beilstein Journal of Nanotechnology 9: 2071-2086. https://dx.doi.org/10.3762/bjnano.9.196, meer
Brasseur, L.; Hennebert, E.; Fievez, L.; Caulier, G.; Bureau, F.; Tafforeau, L.; Flammang, P.; Gerbaux, P.; Eeckhaut, I. (2017). The roles of spinochromes in four shallow water tropical sea urchins and their potential as bioactive pharmacological agents. Mar. Drugs 15(6): 179. https://dx.doi.org/10.3390/md15060179, meer
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