Nanobodies

Structure of PINK1 in complex with its substrate ubiquitin.

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

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

Che, T., Majumdar S., Zaidi S. A., Ondachi P., McCorvy J. D., Wang S., Mosier P. D., Uprety R., Vardy E., Krumm B. E., 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.

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

Lee, S., Choi J., Mohanty J., Sousa L. P., Tome F., Pardon E., Steyaert J., Lemmon M. A., Lax I., and Schlessinger J., "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.

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

Chevillard, F., Rimmer H., Betti C., Pardon E., Ballet S., van Hilten N., Steyaert J., Diederich W. E., and Kolb P., "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.

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

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

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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., Meyrath M., Reynders N., Counson M., Hanson J., Steyaert J., and Chevigné A., "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.

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

Köhler, M., Neff C., Perez C., Brunner C., Pardon E., Steyaert J., Schneider G., Locher K. P., and Zenobi R., "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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Correction to Discovery, Structure-Activity Relationship, and Binding Mode of an Imidazo[1,2- a]pyridine Series of Autotaxin Inhibitors.

Joncour, A., Desroy N., Housseman C., Bock X., Bienvenu N., Cherel L., Labeguere V., Peixoto C., Annoot D., Lepissier L., et al., "Correction to Discovery, Structure-Activity Relationship, and Binding Mode of an Imidazo[1,2- a]pyridine Series of Autotaxin Inhibitors.", J Med Chem, vol. 61, issue 9, pp. 4270, 2018 May 10.

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A Genetically Encoded Biosensor Reveals Location Bias of Opioid Drug Action.

Stoeber, M., Jullié D., Lobingier B. T., Laeremans T., Steyaert J., Schiller P. W., Manglik A., and von Zastrow M., "A Genetically Encoded Biosensor Reveals Location Bias of Opioid Drug Action.", Neuron, vol. 98, issue 5, pp. 963-976.e5, 2018 Jun 06.

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Crystal Structure of a ligand-bound LacY-Nanobody Complex.

Kumar, H., Finer-Moore J. S., Jiang X., Smirnova I., Kasho V., Pardon E., Steyaert J., H Kaback R., and Stroud R. M., "Crystal Structure of a ligand-bound LacY-Nanobody Complex.", Proc Natl Acad Sci U S A, vol. 115, issue 35, pp. 8769-8774, 2018 08 28.

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