Aurélie Badillo

发表

Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus

B. Meier, F. Penin, R. Bartenschlager, 2016, Journal of Biomolecular NMR.

Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic α-Helical Propensity and Is a Substrate of Cyclophilin A*

F. Penin, I. Landrieu, J. Wieruszeski, 2011, The Journal of Biological Chemistry.

Wheat germ cell-free expression: Two detergents with a low critical micelle concentration allow for production of soluble HCV membrane proteins.

B. Meier, F. Penin, R. Bartenschlager, 2015, Protein expression and purification.

Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A.

S. Ricard-Blum, F. Penin, G. Lippens, 2017, Biochemistry.

Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B*

F. Penin, I. Landrieu, J. Wieruszeski, 2009, Journal of Biological Chemistry.

Structural Studies of Self-Assembled Subviral Particles: Combining Cell-Free Expression with 110 kHz MAS NMR Spectroscopy.

B. Meier, P. André, R. Bartenschlager, 2018, Angewandte Chemie.

Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus

B. Meier, F. Penin, R. Bartenschlager, 2016, Journal of biomolecular NMR.

Wheat Germ Cell-Free Overexpression for the Production of Membrane Proteins.

F. Penin, A. Böckmann, A. Badillo, 2017, Methods in molecular biology.

The domain 2 of the HCV NS5A protein is intrinsically unstructured.

F. Penin, G. Lippens, X. Hanoulle, 2010, Protein and peptide letters.

Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded.

F. Penin, J. Wieruszeski, G. Lippens, 2009, Biochemical and biophysical research communications.

The Domain 2 of the HCV NS5A Protein Is Intrinsically Unstructured

F. Penin, G. Lippens, X. Hanoulle, 2010 .

Structural Studies of Self-Assembled Subviral Particles: Combining Cell-Free Expression with 110 kHz MAS NMR Spectroscopy.

B. Meier, P. André, R. Bartenschlager, 2018, Angewandte Chemie.

Towards structural studies of self-assembled subviral particles: combining cell-free expression with 100 kHz MAS NMR.

R. Montserret, Anja Böckmann, Beat H. Meier, 2018 .

Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus

B. Meier, F. Penin, R. Bartenschlager, 2016, Journal of Biomolecular NMR.