Nanobodies

Nanobody production and applications

A lipid site shapes the agonist response of a pentameric ligand-gated ion channel.

Hénault, C. M., C. Govaerts, R. Spurny, M. Brams, A. Estrada-Mondragon, J. Lynch, D. Bertrand, E. Pardon, G. L. Evans, K. Woods, et al., "A lipid site shapes the agonist response of a pentameric ligand-gated ion channel.", Nat Chem Biol, vol. 15, issue 12, pp. 1156-1164, 2019 Dec.

Structure of an endosomal signaling GPCR-G protein-β-arrestin megacomplex.

Nguyen, A. H., A. R. B. Thomsen, T. J. Cahill, R. Huang, L-Y. Huang, T. Marcink, O. B. Clarke, S. Heissel, A. Masoudi, D. Ben-Hail, et al., "Structure of an endosomal signaling GPCR-G protein-β-arrestin megacomplex.", Nat Struct Mol Biol, vol. 26, issue 12, pp. 1123-1131, 2019 Dec.

Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion.

Abskharon, R., F. Wang, A. Wohlkonig, J. Ruan, S. Soror, G. Giachin, E. Pardon, W. Zou, G. Legname, J. Ma, et al., "Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion.", PLoS Pathog, vol. 15, issue 12, pp. e1008139, 2019 Dec.

Structures of β-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling.

Lee, S., J. Choi, J. Mohanty, L. P. Sousa, F. Tome, E. Pardon, J. Steyaert, M. A. Lemmon, I. Lax, and J. Schlessinger, "Structures of β-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling.", Nature, vol. 553, issue 7689, pp. 501-505, 2018 01 25.

Binding-Site Compatible Fragment Growing Applied to the Design of β-Adrenergic Receptor Ligands.

Chevillard, F., H. Rimmer, C. Betti, E. Pardon, S. Ballet, N. van Hilten, J. Steyaert, W. E. Diederich, and P. Kolb, "Binding-Site Compatible Fragment Growing Applied to the Design of β-Adrenergic Receptor Ligands.", J Med Chem, vol. 61, issue 3, pp. 1118-1129, 2018 Feb 08.

Mutational analysis of the extracellular disulphide bridges of the atypical chemokine receptor ACKR3/CXCR7 uncovers multiple binding and activation modes for its chemokine and endogenous non-chemokine agonists.

Szpakowska, M., M. Meyrath, N. Reynders, M. Counson, J. Hanson, J. Steyaert, and A. Chevigné, "Mutational analysis of the extracellular disulphide bridges of the atypical chemokine receptor ACKR3/CXCR7 uncovers multiple binding and activation modes for its chemokine and endogenous non-chemokine agonists.", Biochem Pharmacol, vol. 153, pp. 299-309, 2018 Jul.

Binding Specificities of Nanobody•Membrane Protein Complexes Obtained from Chemical Cross-Linking and High-Mass MALDI Mass Spectrometry.

Köhler, M., C. Neff, C. Perez, C. Brunner, E. Pardon, J. Steyaert, G. Schneider, K. P. Locher, and R. Zenobi, "Binding Specificities of Nanobody•Membrane Protein Complexes Obtained from Chemical Cross-Linking and High-Mass MALDI Mass Spectrometry.", Anal Chem, vol. 90, issue 8, pp. 5306-5313, 2018 Apr 17.

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