Publications

Found 7 results
Filters: Keyword is Camels and Author is Pardon, Els  [Clear All Filters]
2014
Pardon, E., T. Laeremans, S. Triest, S. G. F. Rasmussen, A. Wohlkonig, A. Ruf, S. Muyldermans, W. G. J. Hol, B. K. Kobilka, and J. Steyaert, "A general protocol for the generation of Nanobodies for structural biology.", Nat Protoc, vol. 9, issue 3, pp. 674-93, 2014 Mar.
2013
Sohier, J. S., C. Laurent, A. Chevigné, E. Pardon, V. Srinivasan, U. Wernery, P. Lassaux, J. Steyaert, and M. Galleni, "Allosteric inhibition of VIM metallo-β-lactamases by a camelid nanobody.", Biochem J, vol. 450, issue 3, pp. 477-86, 2013 Mar 15.
2012
Pellis, M., E. Pardon, K. Zolghadr, U. Rothbauer, C. Vincke, J. Kinne, I. Dierynck, K. Hertogs, H. Leonhardt, J. Messens, et al., "A bacterial-two-hybrid selection system for one-step isolation of intracellularly functional Nanobodies.", Arch Biochem Biophys, vol. 526, issue 2, pp. 114-23, 2012 Oct 15.
2011
Domanska, K., S. Vanderhaegen, V. Srinivasan, E. Pardon, F. Dupeux, J. A. Marquez, S. Giorgetti, M. Stoppini, L. Wyns, V. Bellotti, et al., "Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant.", Proc Natl Acad Sci U S A, vol. 108, issue 4, pp. 1314-9, 2011 Jan 25.
2008
Chan, P-H., E. Pardon, L. Menzer, E. De Genst, J. R. Kumita, J. Christodoulou, D. Saerens, A. Brans, F. Bouillenne, D. B. Archer, et al., "Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils.", Biochemistry, vol. 47, issue 42, pp. 11041-54, 2008 Oct 21.
2005
Saerens, D., M. Pellis, R. Loris, E. Pardon, M. Dumoulin, A. Matagne, L. Wyns, S. Muyldermans, and K. Conrath, "Identification of a universal VHH framework to graft non-canonical antigen-binding loops of camel single-domain antibodies.", J Mol Biol, vol. 352, issue 3, pp. 597-607, 2005 Sep 23.
Dumoulin, M., D. Canet, A. M. Last, E. Pardon, D. B. Archer, S. Muyldermans, L. Wyns, A. Matagne, C. V. Robinson, C. Redfield, et al., "Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.", J Mol Biol, vol. 346, issue 3, pp. 773-88, 2005 Feb 25.