Nanobodies

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.

• Read more about Binding-Site Compatible Fragment Growing Applied to the Design of β-Adrenergic Receptor Ligands.
• Log in to post comments
• Google Scholar
• PubMed
• DOI

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.

• Read more about 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.
• Log in to post comments
• Google Scholar
• PubMed
• DOI

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.

• Read more about Binding Specificities of Nanobody•Membrane Protein Complexes Obtained from Chemical Cross-Linking and High-Mass MALDI Mass Spectrometry.
• Log in to post comments
• Google Scholar
• PubMed
• DOI

Correction to Discovery, Structure-Activity Relationship, and Binding Mode of an Imidazo[1,2- a]pyridine Series of Autotaxin Inhibitors.

Joncour, A., N. Desroy, C. Housseman, X. Bock, N. Bienvenu, L. Cherel, V. Labeguere, C. Peixoto, D. Annoot, L. Lepissier, 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.

• Read more about Correction to Discovery, Structure-Activity Relationship, and Binding Mode of an Imidazo[1,2- a]pyridine Series of Autotaxin Inhibitors.
• Log in to post comments
• Google Scholar
• PubMed
• DOI

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

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

• Read more about A Genetically Encoded Biosensor Reveals Location Bias of Opioid Drug Action.
• Log in to post comments
• Google Scholar
• PubMed
• DOI

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

Kumar, H., J. S. Finer-Moore, X. Jiang, I. Smirnova, V. Kasho, E. Pardon, J. Steyaert, R. H Kaback, and R. M. Stroud, "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.

• Read more about Crystal Structure of a ligand-bound LacY-Nanobody Complex.
• Log in to post comments
• Google Scholar
• PubMed
• DOI

Pages