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6. Crystal structure of thermostabilised full-length GLP-1R in complex with a truncated peptide agonist at 3.7 A resolution

7. Crystal structure of a thermostabilised human protease-activated receptor-2 (PAR2) in ternary complex with Fab3949 and AZ7188 at 4.0 angstrom resolution

8. Crystal structure of a thermostabilised human protease-activated receptor-2 (PAR2) in complex with AZ3451 at 3.6 angstrom resolution

9. Crystal structure of a thermostabilised human protease-activated receptor-2 (PAR2) in complex with AZ8838 at 2.8 angstrom resolution

10. Screening for high-yielding Pichia pastoris clones: the production of G protein-coupled receptors as a case study

12. Large-scale functional expression of WT and truncated human adenosine A2A receptor in Pichia pastoris bioreactor cultures

13. Production of membrane proteins in industry: The example of GPCRs.

14. Agonists and Antagonists of Protease-Activated Receptor 2 Discovered within a DNA-Encoded Chemical Library Using Mutational Stabilization of the Target.

16. Structures of Human A 1 and A 2A Adenosine Receptors with Xanthines Reveal Determinants of Selectivity.

17. Crystal structure of the GLP-1 receptor bound to a peptide agonist.

18. Structural insight into allosteric modulation of protease-activated receptor 2.

19. An Alternative Thiol-Reactive Dye to Analyze Ligand Interactions with the Chemokine Receptor CXCR2 Using a New Thermal Shift Assay Format.

20. Biosensor-based affinities and binding kinetics of small molecule antagonists to the adenosine A(2A) receptor reconstituted in HDL like particles.

21. HDL-like discs for assaying membrane proteins in drug discovery.

22. Screening for high-yielding Pichia pastoris clones: the production of G protein-coupled receptors as a case study.

23. Large-scale production of membrane proteins in Pichia pastoris: the production of G protein-coupled receptors as a case study.

24. Structure of Mycobacterium tuberculosis Rv2714, a representative of a duplicated gene family in Actinobacteria.

25. A novel, generic and effective method for the rapid purification of G protein-coupled receptors.

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