Articles dans des revues avec comité de lecture (40)
  1. 9. Satitsuksanoa, P., Kennedy, M. M., Gilis, D., Le Mignon, M., Suratannon, N., Wai, T. S., Wongpiyabovorn, J., Chatchatee, P., Vangveravong, M., Rerkpattanapipat, T., Sangasapaviliya, A., Piboonpocanun, S., Nony, E., Ruxrungtham, K., Jacquet, A., & Mite Allergy Research Cohort (MARC) study team, (2016). The minor house dust mite allergen Der p 13 is a fatty acid binding protein and an activator of a TLR2-mediated innate immune response. Allergy, 71(10), 1425-1434. doi:10.1111/all.12899
  2. 10. De Laet, M., Gilis, D., & Rooman, M. (2016). Stability strengths and weaknesses in protein structures detected by statistical potentials. Application to bovine seminal ribonuclease. Proteins, 84(1), 143–158. doi:10.1002/prot.24962
  3. 11. Pucci, F., Bernaerts, K., Teheux, F., Gilis, D., & Rooman, M. (2015). Symmetry principles in optimization problems: an application to protein stability prediction. IFAC-PapersOnLine, 48, 458-463. doi:10.1016/j.ifacol.2015.05.062
  4. 12. Dehouck, Y., Kwasigroch, J.-M., Rooman, M., & Gilis, D. (2013). BeAtMuSiC: prediction of changes in protein-protein binding affinity on mutations. Nucleic acids research, 41, 333-339. doi:10.1093/nar/gkt450
  5. 13. Moretti, R., Fleishman, S. S., Agius, R., Torchala, M., Bates, P. P., Kastritis, P. P., Rodrigues, J. J., Trellet, M., Bonvin, A. A., Gilis, D., Rooman, M., Dehouck, Y., et al. (2013). Community-wide evaluation of methods for predicting the effect of mutations on protein-protein interactions. Proteins, 81(11), 1980-1987. doi:10.1002/prot.24356
  6. 14. Bienert, G. P., Cavez, D., Besserer, A., Berny, M. C., Gilis, D., Rooman, M., & Chaumont, F. (2012). A conserved cysteine residue is involved in disulfide bond formation between plant plasma membrane aquaporin monomers. Biochemical journal, 445(1), 101-111. doi:10.1042/BJ20111704
  7. 15. Khemili, S., Kwasigroch, J.-M., Hamadouche, T., & Gilis, D. (2012). Modelling and bioinformatics analysis of the dimeric structure of house dust mite allergens from families 5 and 21: Der f 5 could dimerize as Der p 5. Journal of biomolecular structure & dynamics, 29(4), 663-675. doi:10.1080/073911012010525018
  8. 16. Saunders, H. M., Gilis, D., Rooman, M., Dehouck, Y., Robertson, A. L., & Bottomley, S. P. (2011). Flanking domain stability modulates the aggregation kinetics of a polyglutamine disease protein. Protein science, 20(10), 1675-1681. doi:10.1002/pro.698
  9. 17. Dehouck, Y., Kwasigroch, J.-M., Gilis, D., & Rooman, M. (2011). PoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimality. BMC bioinformatics, 12, 151. doi:10.1186/1471-2105-12-151
  10. 18. Chugunov, A. O., Simms, J., Poyner, D. R., Dehouck, Y., Rooman, M., Gilis, D., & Langer, I. (2010). Evidence that interaction between conserved residues in transmembrane helices 2, 3 and 7 are crucial for human VPAC1 receptor activation. Molecular pharmacology, 78(3), 394-401. doi:10.1124/mol.110.063578
  11. 19. van der Gulik, P., Massar, S., Gilis, D., Buhrman, H., & Rooman, M. (2009). The first peptides: the evolutionary transition between prebiotic amino acids and early proteins. Journal of theoretical biology, 261(4), 531-539. doi:10.1016/j.jtbi.2009.09.004
  12. 20. Dehouck, Y., Grosfils, A., Folch, B., Gilis, D., Bogaerts, P., & Rooman, M. (2009). Fast and accurate predictions of protein stability changes upon mutations using statistical potentials and neural networks: PoPMuSiC-2.0. Bioinformatics, 25(19), 2537-2543. doi:10.1093/bioinformatics/btp445
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