| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 52006 |
2024-02-14 |
Chemical Shifts: 1 set
|
Assignment of Lipidic amyloid-b (1-40) fibril |
Cryo-EM structures of lipidic fibrils of amyloid-b (1-40)
|
Benedikt Frieg, Christian Dienemann, Christian Griesinger, Dietmar Riedel, Gunnar F Schroeder, Karin Giller, Loren B Andreas, Mookyoung Han, Stefan Becker |
| 34694 |
2022-03-14 |
Chemical Shifts: 1 set
|
Magic-angle spinning NMR structure of the human voltage-dependent anion channel 1 (E73V/C127A/C232S) in DMPC lipid bilayers |
Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer.
|
C Griesinger, E E Najbauer, K Giller, K Tekwani Movellan, L B Andreas, R Benz, S Becker |
| 50846 |
2022-03-15 |
Chemical Shifts: 1 set
|
Imino resonance assignment of murine Ox40 mRNA 3'UTR |
NMR-derived secondary structure of the full-length Ox40 mRNA 3'UTR and its multivalent binding to the immunoregulatory RBP Roquin
|
Andreas Schlundt, Francois McNicoll, Jan-Niklas N Tants, Lea Marie M Becker, Michaela Muller-McNicoll |
| 50585 |
2021-06-30 |
Chemical Shifts: 1 set
|
Assignment of alpha-synuclein fibrils in the presence of anionic phospholipids |
Insights into the molecular mechanism of amyloid filament formation: Segmental folding of alpha-synuclein on lipid membranes
|
Christian Griesinger, Claudia Steinem, Dietmar Riedel, Ingo Mey, Kumar Tekwani Movellan, Leif Antonschmidt, Loren B Andreas, Riza Dervisoglu, Stefan Becker, Vrinda Sant |
| 27570 |
2019-02-26 |
Chemical Shifts: 1 set
|
Chemical shift assignment of wild-type E.coli diacylglycerol kinase (DGK) by solid-state NMR |
Global response of wild-type E.coli diacylglycerol kinase towards nucleotide and lipid substrate binding observed by 3D and 2D MAS NMR
|
Andreas Jakob, Clemens Glaubitz, Johanna Becker-Baldus, Kristin Moebius, Peter Guentert, Sina Kazemi |
| 15962 |
2009-01-20 |
Chemical Shifts: 1 set
|
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the heme bound form of Truncated HasAp. |
Structural characterization of the hemophore HasAp from Pseudomonas aeruginosa: NMR spectroscopy reveals protein-protein interactions between Holo-HasAp and hemoglobin.
|
Aileen Y Alontaga, Andreas Becker, Erik T Yukl, Ernst Schonbrunn, Jordan T Stobaugh, Juan C Rodriguez, Mario Rivera, Pierre Moenne-Loccoz, Takahiro Hayashi, Todd Funke |
| 15963 |
2009-01-20 |
Chemical Shifts: 1 set
|
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the heme bound form of Full-Length HasAp. |
Structural characterization of the hemophore HasAp from Pseudomonas aeruginosa: NMR spectroscopy reveals protein-protein interactions between Holo-HasAp and hemoglobin.
|
Aileen Y Alontaga, Andreas Becker, Erik T Yukl, Ernst Schonbrunn, Jordan T Stobaugh, Juan C Rodriguez, Mario Rivera, Pierre Moenne-Loccoz, Takahiro Hayashi, Todd Funke |
