Entry ID | Original Release date | Data summary | Entry Title | Citation Title | Authors |
---|---|---|---|---|---|
34850 | 2023-12-12 | Chemical Shifts: 1 set Spectral_peak_list: 1 set |
Conformations of macrocyclic peptides sampled by exact NOEs: models for cell-permeability. NMR structure of Omphalotin A in methanol / water indoleOut conformation. |
Conformations of Macrocyclic Peptides Sampled by Nuclear Magnetic Resonance: Models for Cell-Permeability.
|
A D Gossert, E Matabaro, L Sonderegger, M Kunzler, P Guntert, S H Rudisser |
34849 | 2023-11-22 | Chemical Shifts: 1 set Spectral_peak_list: 1 set |
Conformations of macrocyclic peptides sampled by NMR: models for cell-permeability. Chemical shift assignments of Omphalotin A in methanol / water |
Conformations of Macrocyclic Peptides Sampled by Nuclear Magnetic Resonance: Models for Cell-Permeability
|
A D Gossert, E Matabaro, L Sonderegger, M Kuenzler, P Guentert, S H Ruedisser |
34848 | 2023-11-22 | Chemical Shifts: 1 set Spectral_peak_list: 1 set |
Conformations of macrocyclic peptides sampled by NMR: models for cell-permeability. Chemical shift assignments of Omphalotin A in apolar solvents |
Conformations of Macrocyclic Peptides Sampled by Nuclear Magnetic Resonance: Models for Cell-Permeability
|
A D Gossert, E Matabaro, L Sonderegger, M Kuenzler, P Guentert, S H Ruedisser |
34846 | 2023-11-22 | Chemical Shifts: 1 set Spectral_peak_list: 1 set |
Conformations of macrocyclic peptides sampled by NMR: models for cell-permeability. Chemical shift assignments of Cyclosporin A in apolar solvents |
Conformations of Macrocyclic Peptides Sampled by Nuclear Magnetic Resonance: Models for Cell-Permeability
|
A D Gossert, E Matabaro, L Sonderegger, M Kuenzler, P Guentert, S H Ruedisser |
51635 | 2024-08-09 | Chemical Shifts: 2 sets |
Backbone 1H, 13C and 15N Assignments of MYC(256-351) |
Intrinsically Disordered Regions in the Transcription Factor MYC:MAX Modulate DNA Binding via Intramolecular Interactions
|
Alvar D Gossert, Andreas Lingel, Christian Bergsdorf, Martin Renatus, Sandra Hanni-Holzinger, Stefan Schutz, Wolfgang Jahnke |
51636 | 2024-08-09 | Chemical Shifts: 3 sets |
Backbone 1H, 13C and 15N Assignments of MYC(151-255) |
Intrinsically Disordered Regions in the Transcription Factor MYC:MAX Modulate DNA Binding via Intramolecular Interactions
|
Alvar D Gossert, Andreas Lingel, Christian Bergsdorf, Martin Renatus, Sandra Hanni-Holzinger, Stefan Schutz, Wolfgang Jahnke |
34704 | 2022-02-25 | Chemical Shifts: 1 set |
Solution structure of the DNA-binding minor pilin FimT from Legionella pneumophila |
The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation
|
Alvar D Gossert, Francesca L Short, Manuela K Hospenthal, Matthew Stedman, Sebastian Braus, Stefanie Holz |
30403 | 2018-08-20 | Chemical Shifts: 1 set |
NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc |
Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site
|
A D Gossert, C B Marshall, J M Jansen, M Ikura, T Nishikawa, W Jahnke, Z Fang |
30401 | 2018-08-20 | Chemical Shifts: 1 set |
NMR data-driven model of GTPase KRas-GMPPNP tethered to a nanodisc (E3 state) |
Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site
|
A D Gossert, C B Marshall, J M Jansen, M Ikura, T Nishikawa, W Jahnke, Z Fang |
30400 | 2018-08-31 | Chemical Shifts: 1 set |
NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc |
Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site
|
A D Gossert, C B Marshall, J M Jansen, M Ikura, T Nishikawa, W Jahnke, Z Fang |
15032 | 2007-05-09 | Chemical Shifts: 1 set |
Chemical shift assignments of the type 1 pilus subunit FimF |
NMR assignment of the E. coli type 1 pilus protein FimF.
|
Alvar D Gossert, Francesco Fiorito, Kurt Wuthrich, Sebastian Hiller |
6383 | 2005-01-14 | Chemical Shifts: 1 set |
NMR solution structure of the recombinant elk and mouse/elk variant prion proteins |
Prion protein NMR structures of the elk and of mouse/elk hybrids
|
Alvar D Gossert, Dominikus A Lysek, Francesco Fiorito, Kurt Wuthrich, Sophie Bonjour |