Willet, N., Bastin, F., Dorval, F., Huynen, C., Dumoulin, M., & Duwez, A.-S. (02 July 2015). AFM for monitoring the elongation of amyloid fibrils made of polyQ proteins [Paper presentation]. Journée du Département de Chimie, Liège, Belgium. |
  | Huynen, C. (2015). Model polyQ proteins based on the beta-lactamase BlaP: How non-polyQ regions influence the polyQ length-dependent aggregation process [Doctoral thesis, ULiège - Université de Liège]. ORBi-University of Liège. https://orbi.uliege.be/handle/2268/181589 |
 | Huynen, C. (13 May 2015). Role of non-polyQ regions on the aggregation process by polyQ proteins into amyloid fibrils [Poster presentation]. Bioforum, Liège, Belgium. |
 | Huynen, C., Willet, N., Buell, A. K., Duwez, A.-S., Jérôme, C., & Dumoulin, M. (2015). Influence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils. Biochimica et Biophysica Acta - Proteins and Proteomics, 1854, 239-248. doi:10.1016/j.bbapap.2014.12.002  Peer Reviewed verified by ORBi |
| Huynen, C. (28 November 2014). Role of the polyQ length and non-polyQ regions during the aggregation process into amyloid fibrils of polyQ proteins using a model polyQ protein [Paper presentation]. IAP 7/44 MEETING : Integrative Protein Science: from small molecules to complex biological systems - iPros, Liège, Belgium. |
| Huynen, C., Willet, N., Buell, A. K., Maritan, M., Duwez, A.-S., Jérôme, C., & Dumoulin, M. (26 November 2014). Role of the polyQ length and non-polyQ regions during the aggregation process into amyloid fibrils of model polyQ proteins [Poster presentation]. Science for Business - BioWin Day 2014, Louvain-La-Neuve, Belgium. |
| Huynen, C., Willet, N., Buell, A. K., Maritan, M., Duwez, A.-S., Jérôme, C., & Dumoulin, M. (18 October 2014). Role of non-polyQ regions on the aggregation process by polyQ proteins into amyloid fibrils [Poster presentation]. 25th Regensburger Faltertage, Regensburg, Germany. |
| Huynen, C., Willet, N., Buell, A. K., Maritan, M., Duwez, A.-S., Jérôme, C., & Dumoulin, M. (28 July 2014). Role of non-polyQ regions on the aggregation process by polyQ proteins into amyloid fibrils [Poster presentation]. Neurobiology of Brain Disorders, Neurodegeneration and Aging-Related Disorders of the Nervous System, Girona, Spain. |
| Huynen, C. (26 July 2014). Role of non-polyQ regions on the aggregation process by polyQ proteins into amyloid fibrils [Paper presentation]. Neurobiology of Brain Disorders, Neurodegeneration and Aging-Related Disorders of the Nervous System, Girona, Spain. |
| Vanden Broeck, A., Van Der Heiden, E., Sauvage, E., Rhazi, N., Huynen, C., Verlaine, O., Joris, B., & Duez, C. (23 April 2014). Studies of the Domains II and III of Bacillus subtilis PBP4a in relation with the protein localization [Poster presentation]. IAP Day - iPROS, Ghent, Belgium. |
 | Huynen, C. (20 March 2014). Structure-function relationship of oligomers in amyloidoses [Paper presentation]. séminaire de thèse, Liège, Belgium. |
Thorn, D., Pain, C., Scarafone, N., Huynen, C., Preumont, S., Menzer, L., Duez, C., & Dumoulin, M. (20 November 2013). Switching to the Dark Side: Repositioning of Polyglutamine Repeat Promotes Amyloid Fibril Formation by the Model Protein, β-Lactamase BlaP [Paper presentation]. 4th Scandinavian Meeting on Amyloid Proteins and Disease, Lund, Sweden. |
| Huynen, C. (15 November 2013). Role of non-polyQ regions on the different steps of amyloid fibril formation by polyQ proteins [Poster presentation]. 7th Anuual SFMBBM Doctoral School, Liège, Belgium. |
 | Huynen, C., Filée, P., Matagne, A., Galleni, M., & Dumoulin, M. (28 August 2013). Class A β -Lactamases as Versatile Scaffolds to Create Hybrid Enzymes: Applications from Basic Research to Medicine. BioMed Research International, 2013, 16. doi:10.1155/2013/827621 Peer Reviewed verified by ORBi |
| Huynen, C. (22 July 2013). Role of non-polyQ regions on the aggregation of polyQ proteins into amyloid fibrils triggered by polyQ expansions [Poster presentation]. 27th Annual Symposium of the Protein Society, Boston, United States. |
| Huynen, C. (21 July 2013). Role of non-polyQ regions on the aggregation of polyQ proteins into amyloid fibrils triggered by polyQ expansions [Paper presentation]. 27th Annual Symposium of the Protein Society, Boston, United States. |
| Huynen, C. (18 April 2013). Influence of the protein context in the aggregation of polyQ proteins into amyloid fibrils [Poster presentation]. One-day meeting between bio-industry and Ph.D students, Bioforum 2013. |
 | Huynen, C. (26 February 2013). Role of the protein context in the aggregation into amyloid fibrils of polyQ proteins [Poster presentation]. IAP 7/44 Meeting, Integrative Protein Science: from small molecules to complex biological systems - iPros, Liège, Belgium. |
 | Huynen, C. (16 November 2012). Influence of the protein context on the propensity of polyglutamine tracts to trigger amyloid fibril formation [Paper presentation]. Annual meeting of the doctoral school 'Structure and Function of Biological Macromolecules, Bioinformatics and Modeling, Louvain-la-Neuve, Belgium. |
 | Huynen, C. (13 September 2012). Influence of the protéin context on the propensity of polyglutamine tracts to trigger protein aggregation into amyloid fibrils [Paper presentation]. Sofia School of Protein Science: Structure and dynamics of Biological Macromolecules, Sofia, Bulgaria. |
 | Huynen, C. (10 September 2012). Influence of protein context on the propensity of polyglutamine tracts to trigger protein aggregation into amyloid fibrils [Poster presentation]. Sofia School of Protein Science: Structure and dynamics of Biological Macromolecules, Sofia, Bulgaria. |
 | Huynen, C. (18 April 2012). Influence of protein context on the propensity of polyglutamine tracts to induce protein aggregation into amyloid fibrils [Poster presentation]. Biomedica Summit, Liège, Belgium. |
Huynen, C. (2011). Production and characterization of the physico-chemical properties of the AB42 peptide (associated with Alzheimer's diease) replaced in a protein environment [Master’s dissertation, ULiège - Université de Liège]. ORBi-University of Liège. https://orbi.uliege.be/handle/2268/159462 |