| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 17945 |
2011-10-28 |
Chemical Shifts: 1 set
|
NMR backbone assignment of a Tau protein fragment |
Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein.
|
Arnaud Leroy, Caroline Fauquant, Dries Verdegem, Guy Lippens, Isabelle Huvent, Isabelle Landrieu, Jean-Michel Wieruszeski, Laziza Amniai, Nathalie Sibille |
| 16798 |
2011-05-02 |
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 |
2011-05-02 |
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 |
| 16800 |
2011-05-02 |
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 |
| 16165 |
2009-03-20 |
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 |
2009-03-20 |
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 |
