| Entry ID |
Data summary |
Entry Title |
Citation Title |
Authors |
| 26702 |
Chemical Shifts: 4 sets
|
Partial assignments of full-length (deltaAH)-NS5A protein from Hepatitis C Virus (Con1) produced in wheat germ cell-free system |
Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A
|
Anja Bockmann, Aurelie Badillo, Francois Penin, Francois-Xavier X Cantrelle, Frederic Delolme, Guy Lippens, Jennifer Molle, Marie-Laure L Fogeron, Ralf Bartenschlager, Roland Montserret, Stephane Sarrazin, Sylvie Ricard-Blum, Veronique Receveur-Brechot, Volker Lohmann, Xavier Hanoulle |
| 19059 |
Chemical Shifts: 1 set
|
ns5a308 |
ns5a308
|
Aurelie Badillo, Francois Penin, Guy Lippens, Roland Montserret, Xavier Hanoulle |
| 19055 |
Chemical Shifts: 1 set
|
ns5a D2 con1 |
ns5a D2 con1
|
Aurelie Badillo, Francois Penin, Xavier Hanoulle |
| 16800 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (Con1) in presence of 50%TFE |
Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A.
|
Arnaud Leroy, Aurelie Badillo, Dries Verdegem, Francois Penin, Guy Lippens, Isabelle Landrieu, Jean-Michel Wieruszeski, Ralf Bartenschlager, Xavier Hanoulle |
| 16798 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (JFH-1) |
Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A.
|
Arnaud Leroy, Aurelie Badillo, Dries Verdegem, Francois Penin, Guy Lippens, Isabelle Landrieu, Jean-Michel Wieruszeski, Ralf Bartenschlager, Xavier Hanoulle |
| 16799 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (JFH-1) in presence of 50%TFE |
Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A.
|
Arnaud Leroy, Aurelie Badillo, Dries Verdegem, Francois Penin, Guy Lippens, Isabelle Landrieu, Jean-Michel Wieruszeski, Ralf Bartenschlager, Xavier Hanoulle |
| 16165 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of domain 2 (D2) of the non-structural 5A protein (NS5A) from the JFH1 Hepatitis C virus (HCV) strain. |
Hepatitis C Virus NS5A protein is a substrate for the Peptidyl-Prolyl cis/trans Isomerase activity of Cyclophilins A and B.
|
Aurelie Badillo, Dries Verdegem, Francois Penin, Guy Lippens, Isabelle Landrieu, Jean-Michel Wieruszeski, Ralf Bartenschlager, Xavier Hanoulle |
| 16166 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (Con1) |
Domain 3 of non structural protein 5A from hepatitis C virus is natively unfolded
|
Aurelie Badillo, Dries Verdegem, Francois Penin, Guy Lippens, Jean-Michel Wieruszeski, Xavier Hanoulle |
