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.

Read more about A lipid site shapes the agonist response of a pentameric ligand-gated ion channel.
Log in to post comments
Google Scholar
PubMed
DOI

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.

Read more about Structure of an endosomal signaling GPCR-G protein-β-arrestin megacomplex.
Log in to post comments
Google Scholar
PubMed
DOI

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.

Structure of PINK1 in complex with its substrate ubiquitin.

Schubert, A. F., C. Gladkova, E. Pardon, J. L. Wagstaff, S. M. V. Freund, J. Steyaert, S. L. Maslen, and D. Komander, "Structure of PINK1 in complex with its substrate ubiquitin.", Nature, vol. 552, issue 7683, pp. 51-56, 2017 12 07.

Read more about Structure of PINK1 in complex with its substrate ubiquitin.
Log in to post comments
Google Scholar
PubMed
DOI

Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor.

Che, T., S. Majumdar, S. A. Zaidi, P. Ondachi, J. D. McCorvy, S. Wang, P. D. Mosier, R. Uprety, E. Vardy, B. E. Krumm, et al., "Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor.", Cell, vol. 172, issue 1-2, pp. 55-67.e15, 2018 Jan 11.

Read more about Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor.
Log in to post comments
Google Scholar
PubMed
DOI

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.

Read more about Structures of β-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling.
Log in to post comments
Google Scholar
PubMed
DOI

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.

Nanobody-Enabled Reverse Pharmacology on G-Protein-Coupled Receptors.

Pardon, E., C. Betti, T. Laeremans, F. Chevillard, K. Guillemyn, P. Kolb, S. Ballet, and J. Steyaert, "Nanobody-Enabled Reverse Pharmacology on G-Protein-Coupled Receptors.", Angew Chem Int Ed Engl, vol. 57, issue 19, pp. 5292-5295, 2018 May 04.

Read more about Nanobody-Enabled Reverse Pharmacology on G-Protein-Coupled Receptors.
Log in to post comments
Google Scholar
PubMed
DOI

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.

Pages