| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 51880 |
2024-05-02 |
Chemical Shifts: 8 sets
|
Assignments for plectasin in complex with Lipid II in membranes |
Host defence peptide plectasin targets bacterial cell wall precursor lipid II by a calcium-sensitive supramolecular mechanism
|
Barend Elenbaas, Celine Fetz, Cornelis J Slingerland, Danique Ammerlaan, Eefjan Breukink, Eilidh J Matheson, Francesca Lavore, Joao Medeiros-Silva, Joseph H Lorent, Kamaleddin Tehrani, Maik Derks, Marc Baldus, Markus Kunzler, Markus Weingarth, Mick van der Weijde, Moreno Lelli, Naomi A Consoli, Nathaniel I Martin, Rachel Cochrane, Ruud Cox, Shehrazade Jekhmane, Sourav Maity, Stephen A Cochrane, Vicky Charitou, Wouter H Roos |
| 51022 |
2021-12-13 |
Chemical Shifts: 1 set
|
Backbone assignments of truncated form of TagA from Thermoanaerobacter italicus |
Insight into the molecular basis of substrate recognition by the wall teichoic acid glycosyltransferase TagA
|
Andrew K Goring, Brendan J Mahoney, Denise Tran, Duilio Cascio, Joseph A Loo, Martin L Phillips, Michael E Jung, Musleh M Muthana, Orlando E Martinez, Robert T Clubb, Sung-Wook Yi, Xi Chen |
| 34178 |
2018-10-02 |
Chemical Shifts: 1 set
|
Solid-state MAS NMR structure of the HELLF prion amyloid fibrils |
Structural and molecular basis of cross-seeding barriers in amyloids
|
Abdelmajid Noubhani, Antoine Loquet, Asen Daskalov, Benjamin Bardiaux, Birgit Habenstein, Brice Kauffmann, Denis Martinez, Guido Pintacuda, Jan Stanek, Joseph S Wall, Loren B Andreas, Melanie Berbon, Nadia El Mammeri, Sven J Saupe, Virginie Coustou |
| 27099 |
2017-06-29 |
Chemical Shifts: 1 set
|
Chemical shift assignment of gp17.1 by proton-detected solid-state NMR |
Bacteriophage Tail Tube Assembly Studied by Proton-Detected 4D Solid-State NMR
|
Adam Lange, Camille Samson, Joseph Wall, Maximilian Zinke, Pascal Fricke, Sascha Lange, Songhwan Hwang, Sophie Zinn-Justin |
| 25289 |
2014-11-24 |
Chemical Shifts: 3 sets
|
Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation |
Atomic-Resolution Three-Dimensional Structure of Amyloid beta Fibrils Bearing the Osaka Mutation
|
Anja Bockmann, Anne K Schuetz, Beat H Meier, Joseph Wall, Matthias Huber, Oxana Y Ovchinnikova, Peter Guentert, Riccardo Cadalbert, Rudi Glockshuber, Toni Vagt |
