Lode Wyns
Affiliations: | Free University of Brussels, Bruxelles, Bruxelles, Belgium |
Google:
"Lode Wyns"
BETA: Related publications
See more...
Publications
|
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
| Vanwetswinkel S, Volkov AN, Sterckx YG, et al. (2014) Study of the structural and dynamic effects in the FimH adhesin upon α-d-heptyl mannose binding. Journal of Medicinal Chemistry. 57: 1416-27 |
| Roos G, Wellens A, Touaibia M, et al. (2013) Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of FimH. Acs Medicinal Chemistry Letters. 4: 1085-90 |
| De Genst E, Chan PH, Pardon E, et al. (2013) A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation. The Journal of Physical Chemistry. B. 117: 13245-58 |
| Guilliams T, El-Turk F, Buell AK, et al. (2013) Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages. Journal of Molecular Biology. 425: 2397-411 |
| Domanska K, Vanderhaegen S, Srinivasan V, et al. (2011) Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant. Proceedings of the National Academy of Sciences of the United States of America. 108: 1314-9 |
| De Genst EJ, Guilliams T, Wellens J, et al. (2010) Structure and properties of a complex of α-synuclein and a single-domain camelid antibody. Journal of Molecular Biology. 402: 326-43 |
| Garcia-Pino A, Balasubramanian S, Wyns L, et al. (2010) Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. Cell. 142: 101-11 |
| Roos G, Foloppe N, Van Laer K, et al. (2009) How thioredoxin dissociates its mixed disulfide. Plos Computational Biology. 5: e1000461 |
| De Jonge N, Garcia-Pino A, Buts L, et al. (2009) Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. Molecular Cell. 35: 154-63 |
| Van Molle I, Moonens K, Buts L, et al. (2009) The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces. Acta Crystallographica. Section D, Biological Crystallography. 65: 411-20 |