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Recombinant proteins: A molecular tool to understand marine adhesion and to advance biomaterials. <i>Advanced Healthcare Materials 15(3)</i>: e02340. <a href=\"https://dx.doi.org/10.1002/adhm.202502340\" target=\"_blank\">https://dx.doi.org/10.1002/adhm.202502340</a>","AutID":423594,"MonDate":null,"AnaDate":2026,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":361744,"RR":"<b>Algrain, M.; Hennebert, E.; Bertemes, P.; Wattiez, R.; Flammang, P.; Lengerer, B.</b> (2022). In the footsteps of sea stars: deciphering the catalogue of proteins involved in underwater temporary adhesion. <i>Open Biology 12(8)</i>: 220103. <a href=\"https://dx.doi.org/10.1098/rsob.220103\" target=\"_blank\">https://dx.doi.org/10.1098/rsob.220103</a>","AutID":537825,"MonDate":null,"AnaDate":2022,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":355783,"RR":"<b>Bonneel, M.; Hennebert, E.; Aranko, A.S.; Hwang, D.S.; Lefevre, M.; Pommier, V.; Wattiez, R.; Delroisse, J.; Flammang, P.</b> (2022). Molecular mechanisms mediating stiffening in the mechanically adaptable connective tissues of sea cucumbers. <i>Matrix Biology 108</i>: 39-54. <a href=\"https://dx.doi.org/10.1016/j.matbio.2022.02.006\" target=\"_blank\">https://dx.doi.org/10.1016/j.matbio.2022.02.006</a>","AutID":537825,"MonDate":null,"AnaDate":2022,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":337324,"RR":"<b>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.</b> (2021). Omics-based molecular analyses of adhesion by aquatic invertebrates. <i>Biol. Rev. 96(3)</i>: 1051-1075. <a href=\"https://hdl.handle.net/10.1111/brv.12691\" target=\"_blank\">https://hdl.handle.net/10.1111/brv.12691</a>","AutID":537825,"MonDate":null,"AnaDate":2021,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":353191,"RR":"<b>Lefevre, M.; Ederth, T.; Masai, T.; Wattiez, R.; Leclère, P.; Flammang, P.; Hennebert, E.</b> (2021). Disentangling the roles of functional domains in the aggregation and adsorption of the multimodular sea star adhesive protein Sfp1. <i>Mar. Biotechnol. 23(5)</i>: 724-735. <a href=\"https://dx.doi.org/10.1007/s10126-021-10059-y\" target=\"_blank\">https://dx.doi.org/10.1007/s10126-021-10059-y</a>","AutID":537825,"MonDate":null,"AnaDate":2021,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":353583,"RR":"<b>Lefevre, M.; Tran, T.Q.; De Muijlder, T.; Pittenger, B.; Flammang, P.; Hennebert, E.; Leclère, P.</b> (2021). On the nanomechanical and viscoelastic properties of coatings made of recombinant sea star adhesive proteins. <i>Frontiers of Mechanical Engineering 7</i>: 667491. <a href=\"https://dx.doi.org/10.3389/fmech.2021.667491\" target=\"_blank\">https://dx.doi.org/10.3389/fmech.2021.667491</a>","AutID":495378,"MonDate":null,"AnaDate":2021,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":337771,"RR":"<b>Choi, J.; Hennebert, E.; Flammang, P.; Hwang, D.S.</b> (2020). A sugar-lectin rich interface between soft tissue and the stiff byssus of <i>Atrina pectinata</i>. <i>Biomaterials Science 8(13)</i>: 3751-3759. <a href=\"https://hdl.handle.net/10.1039/c9bm01932d\" target=\"_blank\">https://hdl.handle.net/10.1039/c9bm01932d</a>","AutID":455221,"MonDate":null,"AnaDate":2020,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":328503,"RR":"<b>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.</b> (2020). Sea star-inspired recombinant adhesive proteins self-assemble and adsorb on surfaces in aqueous environments to form cytocompatible coatings. <i>Acta Biomaterialia 112</i>: 62-74. <a href=\"https://dx.doi.org/10.1016/j.actbio.2020.05.036\" target=\"_blank\">https://dx.doi.org/10.1016/j.actbio.2020.05.036</a>","AutID":537825,"MonDate":null,"AnaDate":2020,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":322894,"RR":"<b>Lengerer, B.; Algrain, M.; Lefevre, M.; Delroisse, J.; Hennebert, E.; Flammang, P.</b> (2019). Interspecies comparison of sea star adhesive proteins. <i>Phil. Trans. R. Soc. Lond. (B Biol. Sci.) 374(1784)</i>: 20190195. <a href=\"https://dx.doi.org/10.1098/rstb.2019.0195\" target=\"_blank\">https://dx.doi.org/10.1098/rstb.2019.0195</a>","AutID":537823,"MonDate":null,"AnaDate":2019,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":310434,"RR":"<b>Hennebert, E.; Gregorowicz, E.; Flammang, P.</b> (2018). Involvement of sulfated biopolymers in adhesive secretions produced by marine invertebrates. <i>Biology Open 7(11)</i>: bio037358. <a href=\"https://dx.doi.org/10.1242/bio.037358\" target=\"_blank\">https://dx.doi.org/10.1242/bio.037358</a>","AutID":537823,"MonDate":null,"AnaDate":2018,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":307945,"RR":"<b>Lengerer, B.; Bonneel, M.; Lefevre, M.; Hennebert, E.; Leclère, P.; Gosselin, E.; Ladurner, P.; Flammang, P.</b> (2018). The structural and chemical basis of temporary adhesion in the sea star <i>Asterina gibbosa</i>. <i>Beilstein Journal of Nanotechnology 9</i>: 2071-2086. <a href=\"https://dx.doi.org/10.3762/bjnano.9.196\" target=\"_blank\">https://dx.doi.org/10.3762/bjnano.9.196</a>","AutID":537823,"MonDate":null,"AnaDate":2018,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":293710,"RR":"<b>Brasseur, L.; Hennebert, E.; Fievez, L.; Caulier, G.; Bureau, F.; Tafforeau, L.; Flammang, P.; Gerbaux, P.; Eeckhaut, I.</b> (2017). The roles of spinochromes in four shallow water tropical sea urchins and their potential as bioactive pharmacological agents. <i>Mar. Drugs 15(6)</i>: 179. <a href=\"https://dx.doi.org/10.3390/md15060179\" target=\"_blank\">https://dx.doi.org/10.3390/md15060179</a>","AutID":318727,"MonDate":null,"AnaDate":2017,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":310497,"RR":"<b>Demeuldre, M.; Hennebert, E.; Bonneel, M.; Lengerer, B.; Van Dyck, S.; Wattiez, R.; Ladurner, P.; Flammang, P.</b> (2017). Mechanical adaptability of sea cucumber Cuvierian tubules involves a mutable collagenous tissue. <i>J. Exp. Biol. 220(11)</i>: 2108-2119. <a href=\"https://dx.doi.org/10.1242/jeb.145706\" target=\"_blank\">https://dx.doi.org/10.1242/jeb.145706</a>","AutID":374265,"MonDate":null,"AnaDate":2017,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":285574,"RR":"<b>Lengerer, B.; Hennebert, E.; Flammang, P.; Salvenmoser, W.; Ladurner, P.</b> (2016). Adhesive organ regeneration in <i>Macrostomum lignano</i>. <i>Bmc Developmental Biology 16</i>: 16 pp. <a href=\"https://dx.doi.org/10.1186/s12861-016-0121-1\" target=\"_blank\">https://dx.doi.org/10.1186/s12861-016-0121-1</a>","AutID":256995,"MonDate":null,"AnaDate":2016,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":285587,"RR":"<b>Yoo, H.Y.; Iordachescu, M.; Huang, J.; Hennebert, E.; Kim, S.; Rho, S.; Foo, M.; Flammang, P.; Zeng, H.; Hwang, D.; Waite, J.H.; Hwang, D.S.</b> (2016). Sugary interfaces mitigate contact damage where stiff meets soft. <i>Nature Comm. 7</i>: 8 pp. <a href=\"https://dx.doi.org/10.1038/ncomms11923\" target=\"_blank\">https://dx.doi.org/10.1038/ncomms11923</a>","AutID":196292,"MonDate":null,"AnaDate":2016,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":256823,"RR":"<b>Demeyer, M.; Wisztorski, M.; Decroo, C.; De Winter, J.; Caulier, G.; Hennebert, E.; Eeckhaut, I.; Fournier, I.; Flammang, P.; Gerbaux, P.</b> (2015). Inter- and intra-organ spatial distributions of sea star saponins by MALDI imaging. <i>Anal. Bioanal. Chem. 407(29)</i>: 8813-8824. <a href=\"https://dx.doi.org/10.1007/s00216-015-9044-0\" target=\"_blank\">https://dx.doi.org/10.1007/s00216-015-9044-0</a>","AutID":220265,"MonDate":null,"AnaDate":2015,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":301291,"RR":"<b>Hennebert, E.; Maldonado, B.; Ladurner, P.; Flammang, P.; Santos, R.</b> (2015). Experimental strategies for the identification and characterization of adhesive proteins in animals: a review. <i>Interface Focus 5(1)</i>: 20140064. <a href=\"https://dx.doi.org/10.1098/rsfs.2014.0064\" target=\"_blank\">https://dx.doi.org/10.1098/rsfs.2014.0064</a>","AutID":256995,"MonDate":null,"AnaDate":2015,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":280649,"RR":"<b>Hennebert, E.; Leroy, B.; Wattiez, R.; Ladurner, P.</b> (2015). An integrated transcriptomic and proteomic analysis of sea star epidermal secretions identifies proteins involved in defense and adhesion. <i>J. Proteomics 128</i>: 83-91. <a href=\"http://dx.doi.org/10.1016/j.jprot.2015.07.002\" target=\"_blank\">dx.doi.org/10.1016/j.jprot.2015.07.002</a>","AutID":196292,"MonDate":null,"AnaDate":2015,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":246992,"RR":"<b>Demeuldre, M.; Ngo, T.C.; Hennebert, E.; Wattiez, R.; Leclère, P.; Flammang, P.</b> (2014). Instantaneous adhesion of Cuvierian tubules in the sea cucumber <i>Holothuria forskali</i>. <i>Biointerphases 9(2)</i>. <a href=\"https://dx.doi.org/10.1116/1.4875731\" target=\"_blank\">https://dx.doi.org/10.1116/1.4875731</a>","AutID":196126,"MonDate":null,"AnaDate":2014,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":247017,"RR":"<b>Hennebert, E.; Wattiez, R.; Demeuldre, M.; Ladurner, P; Hwang, S; Waite, H; Flammang, P.</b> (2014). Sea star tenacity mediated by a protein that fragments, then aggregates. <i>Proc. Natl. Acad. Sci. U.S.A. 111(17)</i>: 6317-6322. <a href=\"http://dx.doi.org/10.1073/pnas.1400089111\" target=\"_blank\">dx.doi.org/10.1073/pnas.1400089111</a>","AutID":196292,"MonDate":null,"AnaDate":2014,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":238619,"RR":"<b>Hennebert, E.; Wattiez, R.; Waite, J.H.; Flammang, P.</b> (2012). Characterization of the protein fraction of the temporary adhesive secreted by the tube feet of the sea star <i>Asterias rubens</i>. <i>Biofouling (Print) 28(3)</i>: 289-303. <a href=\"https://dx.doi.org/10.1080/08927014.2012.672645\" target=\"_blank\">https://dx.doi.org/10.1080/08927014.2012.672645</a>","AutID":181667,"MonDate":null,"AnaDate":2012,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":211224,"RR":"<b>Hennebert, E.; Wattiez, R.; Flammang, P.</b> (2011). Characterisation of the carbohydrate fraction of the temporary adhesive secreted by the tube feet of the sea star <i>Asterias rubens</i>. <i>Mar. Biotechnol. 13(3)</i>: 484-495. <a href=\"http://dx.doi.org/10.1007/s10126-010-9319-6\" target=\"_blank\">dx.doi.org/10.1007/s10126-010-9319-6</a>","AutID":162228,"MonDate":null,"AnaDate":2011,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":226665,"RR":"<b>Hennebert, E.; Haesaerts, D.; Dubois, P.; Flammang, P.</b> (2010). Evaluation of the different forces brought into play during tube foot activities in sea stars. <i>J. Exp. Biol. 213(7)</i>: 1162-1174. <a href=\"http://dx.doi.org/10.1242/jeb.037903\" target=\"_blank\">http://dx.doi.org/10.1242/jeb.037903</a>","AutID":162248,"MonDate":null,"AnaDate":2010,"PeerRev":1,"outputType":"1_A1","OpenAcc":1},{"BRefID":228923,"RR":"<b>Flammang, P.; Lambert, A.; Bailly, P.; Hennebert, E.</b> (2009). Polyphosphoprotein-containing marine adhesives. <i>J. 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Characterization of adhesive secretions from sea star tube feet, <b><i>in</i></b>: Anderson, G. (Ed.) <i>Proceedings of the 32nd Annual Meeting of The Adhesion Society, Inc., Savannah, Georgia, February 15-18, 2009.</i> pp. 200-202","AutID":162321,"MonDate":null,"AnaDate":2009,"PeerRev":0,"outputType":"4_BookChap","OpenAcc":1},{"BRefID":226721,"RR":"<b>Santos, R.; Hennebert, E.; Coelho, A.V.; Flammang, P.</b> (2009). The Echinoderm tube foot and its role in temporary underwater adhesion, <b><i>in</i></b>: Gorb, S.N. <i>Functional surfaces in biology. Adhesion related phenomena volume 2.</i> pp. 9-41. <a href=\"https://dx.doi.org/10.1007/978-1-4020-6695-5_2\" target=\"_blank\">https://dx.doi.org/10.1007/978-1-4020-6695-5_2</a>","AutID":162321,"MonDate":null,"AnaDate":2009,"PeerRev":0,"outputType":"4_BookChap","OpenAcc":0}],"OtherRef":[{"BRefID":228920,"RR":"<b>Hennebert, E.; Santos, R.; Flammang, P.</b> (2012). 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